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Predicate	Value (sorted: none)
drugbank:description	" experimental This compound belongs to the morpholines. These are organic compounds containing a morpholine moiety, which consists of a six-member aliphatic saturated ring with the formula C4H9NO, where the oxygen and nitrogen atoms lie at positions 1 and 4, respectively. Morpholines Organic Compounds Heterocyclic Compounds Oxazinanes Morpholines Sulfonyls Sulfonic Acids and Derivatives Organic Sulfites Polyamines Ethers sulfonic acid derivative organic sulfite sulfonyl ether polyamine amine organonitrogen compound logP -0.87 ALOGPS logS -1.7 ALOGPS Water Solubility 4.58e+00 g/l ALOGPS logP -2.5 ChemAxon IUPAC Name 4-(2-sulfonatoethyl)morpholin-4-ium ChemAxon Traditional IUPAC Name 4-(2-sulfonatoethyl)morpholin-4-ium ChemAxon Molecular Weight 195.237 ChemAxon Monoisotopic Weight 195.056528599 ChemAxon SMILES [O-]S(=O)(=O)CC[NH+]1CCOCC1 ChemAxon Molecular Formula C6H13NO4S ChemAxon InChI InChI=1S/C6H13NO4S/c8-12(9,10)6-3-7-1-4-11-5-2-7/h1-6H2,(H,8,9,10) ChemAxon InChIKey InChIKey=SXGZJKUKBWWHRA-UHFFFAOYSA-N ChemAxon Polar Surface Area (PSA) 70.87 ChemAxon Refractivity 53.64 ChemAxon Polarizability 18.67 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 1 ChemAxon pKa (strongest acidic) -1.5 ChemAxon pKa (strongest basic) 6.51 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon ChEBI 39408 PubChem Compound 4478249 PubChem Substance 46507795 PDB MES BE0000426 Acetylcholinesterase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Acetylcholinesterase Lipid transport and metabolism Rapidly hydrolyzes choline released into the synapse ACHE 7q22 Cytoplasmic None 6.24 67797.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:108 GenAtlas ACHE GeneCards ACHE GenBank Gene Database M55040 GenBank Protein Database 177975 UniProtKB P22303 UniProt Accession ACES_HUMAN Acetylcholinesterase precursor AChE EC 3.1.1.7 >Acetylcholinesterase precursor MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN QFDHYSKQDRCSDL >1845 bp ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA PF00135 COesterase function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity function catalytic activity function hydrolase activity BE0001423 Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Cell wall/membrane/envelope biogenesis Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source glmS Cytoplasm None 5.74 66895.0 Escherichia coli (strain K12) GenBank Gene Database X01631 GenBank Protein Database 43268 UniProtKB P17169 UniProt Accession GLMS_ECOLI D-fructose-6- phosphate amidotransferase EC 2.6.1.16 GFAT Glucosamine-6-phosphate synthase Hexosephosphate aminotransferase L-glutamine-D-fructose-6-phosphate amidotransferase >Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAE EHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFV SETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLV IGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQ YDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILA CGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGL RLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKL SRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIA LEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRAR GGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPR NLAKSVTVE >1830 bp ATGTGTGGAATTGTTGGCGCGATCGCGCAACGTGATGTAGCAGAAATCCTTCTTGAAGGT TTACGTCGTCTGGAATACCGCGGATATGACTCTGCCGGTCTGGCCGTTGTTGATGCAGAA GGTCATATGACCCGCCTGCGTCGCCTCGGTAAAGTCCAGATGCTGGCACAGGCAGCGGAA GAACATCCTCTGCATGGCGGCACTGGTATTGCTCACACTCGCTGGGCGACCCACGGTGAA CCTTCAGAAGTGAATGCGCATCCGCATGTTTCTGAACACATTGTGGTGGTGCATAACGGC ATCATCGAAAACCATGAACCGCTGCGTGAAGAGCTAAAAGCGCGTGGCTATACCTTCGTT TCTGAAACCGACACCGAAGTGATTGCCCATCTGGTGAACTGGGAGCTGAAACAAGGCGGG ACTCTGCGTGAGGCCGTTCTGCGTGCTATCCCGCAGCTGCGTGGTGCGTACGGTACAGTG ATCATGGACTCCCGTCACCCGGATACCCTGCTGGCGGCACGTTCTGGTAGTCCGCTGGTG ATTGGCCTGGGGATGGGCGAAAACTTTATCGCTTCTGACCAGCTGGCGCTGTTGCCGGTG ACCCGTCGCTTTATCTTCCTTGAAGAGGGCGATATTGCGGAAATCACTCGCCGTTCGGTA AACATCTTCGATAAAACTGGCGCGGAAGTAAAACGTCAGGATATCGAATCCAATCTGCAA TATGACGCGGGCGATAAAGGCATTTACCGTCACTACATGCAGAAAGAGATCTACGAACAG CCGAACGCGATCAAAAACACCCTTACCGGACGCATCAGCCACGGTCAGGTTGATTTAAGC GAGCTGGGACCGAACGCCGACGAACTGCTGTCGAAGGTTGAGCATATTCAGATCCTCGCC TGTGGTACTTCTTATAACTCCGGTATGGTTTCCCGCTACTGGTTTGAATCGCTAGCAGGT ATTCCGTGCGACGTCGAAATCGCCTCTGAATTCCGCTATCGCAAATCTGCCGTGCGTCGT AACAGCCTGATGATCACCTTGTCACAGTCTGGCGAAACCGCGGATACCCTGGCTGGCCTG CGTCTGTCGAAAGAGCTGGGTTACCTTGGTTCACTGGCAATCTGTAACGTTCCGGGTTCT TCTCTGGTGCGCGAATCCGATCTGGCGCTAATGACCAACGCGGGTACAGAAATCGGCGTG GCATCCACTAAAGCATTCACCACTCAGTTAACTGTGCTGTTGATGCTGGTGGCGAACGTG TCTCGCCTGAAAGGTCTGGATGCCTCCATTGAACATGACATCGTGCATGGTCTGCAGGCG CTGCCGAGCCGTATTGAGCAGATGCTGTCTCAGGACAAACGCATTGAAGCGCTGGCAGAA GATTTCTCTGACAAACATCACGCGCTGTTCCTGGGCCGTGGCGATCAGTACCCAATCGCG CTGGAAGGCGCATTGAAGTTGAAAGAGATCTCTTACATTCACGCTGAAGCCTACGCTGCT GGCGAACTGAAACACGGTCCGCTGGCGCTAATTGATGCCGATATGCCGGTTATTGTTGTT GCACCGAACAACGAATTGCTGGAAAAACTGAAATCCAACATTGAAGAAGTTCGCGCGCGT GGCGGTCAGTTGTATGTCTTCGCCGATCAGGATGCGGGTTTTGTAAGTAGCGATAACATG CACATCATCGAGATGCCGCATGTGGAAGAGGTGATTGCACCGATCTTCTACACCGTTCCG CTGCAGCTGCTGGCTTACCATGTCGCGCTGATCAAAGGCACCGACGTTGACCAGCCGCGT AACCTGGCAAAATCGGTTACGGTTGAGTAA PF00310 GATase_2 PF01380 SIS component cell component intracellular component cytoplasm function catalytic activity function carbohydrate binding function sugar binding function glutamine-fructose-6-phosphate transaminase (isomerizing) activity function transferase activity function binding function transferase activity, transferring nitrogenous groups function transaminase activity process metabolism process macromolecule metabolism process carbohydrate biosynthesis process carbohydrate metabolism process macromolecule biosynthesis process physiological process BE0001302 Dihydrofolate reductase Yeast # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Dihydrofolate reductase Coenzyme transport and metabolism 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- dihydrofolate + NADPH DFR1 None 9.25 22139.0 Yeast GenBank Gene Database X78968 GenBank Protein Database 563852 UniProtKB P22906 UniProt Accession DYR_CANAX EC 1.5.1.3 >Dihydrofolate reductase MSKPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRNAVIMGRKTWE SIPQKFRPLPDRLNIILSRSYENKIIDDNIIHASSIESSLNLVSDVERVFIIGGAEIYNE LINNSLVSHLLITEIEHPSPESIEMDTFLKFPLESWTKQPKSELQKFVGDTVLEDDIKEG DFTYNYTLWTRK >579 bp ATGCTGAAACCAAATGTTGCAATCATTGTCGCGGCATTAAAGCCTGCTTTGGGAATTGGA TACAAAGGTAAAATGCCTTGGAGACTCCGTAAGGAAATAAGATATTTCAAAGACGTCACC ACCAGAACAACGAAACCAAATACTCGTAATGCTGTTATTATGGGAAGAAAGACGTGGGAA TCCATACCACAGAAGTTTAGACCTCTTCCAGATAGATTAAACATAATATTATCTAGATCA TACGAAAATAAAATTATTGATGACAATATCATTCATGCCAGCTCAATTGAGTCGTCACTT AATCTTGTATCTGATGTCGAAAGAGTTTTCATAATTGGAGGGGCAGAAATTTACAATGAA TTGATAAATAATTCTTTAGTGAGTCATCTATTAATTACAGAAATCGAACATCCAAGCCCA GAGTCTATTGAAATGGATACCTTTTTGAAATTCCCATTGGAAAGTTGGACCAAACAACCA AAATCAGAGTTGCAGAAATTTGTTGGAGATACTGTATTAGAAGACGATATCAAGGAAGGT GATTTTACCTATAATTATACGCTATGGACAAGAAAATAA PF00186 DHFR_1 function oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor function oxidoreductase activity function dihydrofolate reductase activity function cofactor binding function coenzyme binding function NADP binding function binding function catalytic activity function oxidoreductase activity, acting on the CH-NH group of donors process amino acid metabolism process amino acid and derivative metabolism process nucleotide biosynthesis process glycine biosynthesis process serine family amino acid metabolism process physiological process process glycine metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process metabolism process nucleotide metabolism process cellular metabolism BE0001495 Copper-containing nitrite reductase Achromobacter cycloclastes # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Copper-containing nitrite reductase Secondary metabolites biosynthesis, transport and catabolism Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+) nirK Periplasm None 6.26 40772.0 Achromobacter cycloclastes GenBank Gene Database Z48635 GenBank Protein Database 1125639 UniProtKB P25006 UniProt Accession NIR_ACHCY Copper-containing nitrite reductase precursor Cu-NIR EC 1.7.2.1 >Copper-containing nitrite reductase precursor MTEQLQMTRRTMLAGAALAGAVAPLLHTAQAHAAGAAAAAGAAPVDISTLPRVKVDLVKP PFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEIHAMTFNGSVPGPLMVVHENDYVE LRLINPDTNTLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMV PWHVTSGMNGAIMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEA YEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGGHGD YVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKV TGEWNDDLMTSVVKPASM >1137 bp ATGACTGAACAACTTCAGATGACCCGCCGGACGATGCTTGCCGGCGCTGCCCTGGCGGGC GCGGTTGCGCCGCTTCTCCACACCGCTCAGGCGCATGCCGCTGGCGCTGCCGCGGCAGCC GGTGCTGCCCCCGTCGATATCTCGACCCTGCCTCGCGTGAAGGTCGACCTCGTCAAGCCG CCTTTCGTGCACGCCCATGACCAGGTCGCCAAGACCGGACCGCGCGTCGTCGAGTTCACC ATGACGATCGAGGAAAAGAAGCTGGTGATCGACCGCGAGGGCACTGAGATCCACGCGATG ACCTTCAACGGTTCGGTGCCTGGTCCGCTGATGGTGGTGCATGAGAACGACTATGTTGAA CTGCGGCTGATCAACCCTGACACCAACACGTTGCTGCACAACATCGACTTCCACGCCGCA ACCGGTGCGCTCGGCGGCGGGGCGCTGACCCAGGTGAACCCGGGCGAGGAAACCACGCTT CGTTTCAAGGCGACCAAGCCCGGCGTCTTCGTCTACCATTGCGCGCCGGAGGGCATGGTG CCCTGGCACGTCACCTCGGGCATGAACGGCGCCATCATGGTGCTGCCGCGCGACGGACTG AAGGACGAGAAGGGCCAGCCGCTGACGTACGACAAGATCTACTATGTCGGCGAGCAGGAC TTCTACGTGCCGAAGGACGAGGCCGGGAACTACAAGAAGTACGAAACCCCCGGCGAAGCC TATGAAGATGCTGTCAAGGCGATGCGCACGCTGACCCCGACCCACATCGTCTTCAACGGT GCGGTCGGCGCGCTGACCGGCGACCATGCTTTGACTGCGGCCGTGGGCGAGCGTGTGCTC GTCGTCCATTCGCAGGCCAACCGCGATACGCGGCCGCACCTGATCGGCGGGCATGGTGAC TATGTCTGGGCGACCGGCAAGTTCCGCAACCCGCCGGATCTCGACCAGGAAACCTGGCTC ATTCCGGGCGGAACCGCGGGCGCTGCCTTCTACACCTTCCGCCAGCCGGGTGTGTACGCC TACGTCAACCACAACCTGATCGAGGCGTTCGAGCTGGGTGCCGCCGGCCACTTCAAGGTG ACCGGCGAATGGAACGATGATCTGATGACATCGGTCGTCAAGCCGGCGTCGATGTAG PF00394 Cu-oxidase PF07732 Cu-oxidase_3 function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors function oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor function nitrite reductase (NO-forming) activity function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function binding function copper ion binding process nitrogen compound metabolism process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0000329 Corticosteroid 11-beta-dehydrogenase isozyme 1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Corticosteroid 11-beta-dehydrogenase isozyme 1 Lipid transport and metabolism Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7- ketocholesterol to 7-beta-hydroxycholesterol HSD11B1 1q32-q41 Endoplasmic reticulum; endoplasmic reticulum membrane; single-pass type II membrane protein 7-23 8.77 32270.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:5208 GenAtlas HSD11B1 GeneCards HSD11B1 GenBank Gene Database M76665 GenBank Protein Database 179475 UniProtKB P28845 UniProt Accession DHI1_HUMAN 11-beta-HSD1 11-beta-hydroxysteroid dehydrogenase 1 11-DH EC 1.1.1.146 >Corticosteroid 11-beta-dehydrogenase isozyme 1 AFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHV VVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHI TNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVA AYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEEC ALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK >879 bp ATGGCTTTTATGAAAAAATATCTCCTCCCCATTCTGGGGCTCTTCATGGCCTACTACTAC TATTCTGCAAACGAGGAATTCAGACCAGAGATGCTCCAAGGAAAGAAAGTGATTGTCACA GGGGCCAGCAAAGGGATCGGAAGAGAGATGGCTTATCATCTGGCGAAGATGGGAGCCCAT GTGGTGGTGACAGCGAGGTCAAAAGAAACTCTACAGAAGGTGGTATCCCACTGCCTGGAG CTTGGAGCAGCCTCAGCACACTACATTGCTGGCACCATGGAAGACATGACCTTCGCAGAG CAATTTGTTGCCCAAGCAGGAAAGCTCATGGGAGGACTAGACATGCTCATTCTCAACCAC ATCACCAACACTTCTTTGAATCTTTTTCATGATGATATTCACCATGTGCGCAAAAGCATG GAAGTCAACTTCCTCAGTTACGTGGTCCTGACTGTAGCTGCCTTGCCCATGCTGAAGCAG AGCAATGGAAGCATTGTTGTCGTCTCCTCTCTGGCTGGGAAAGTGGCTTATCCAATGGTT GCTGCCTATTCTGCAAGCAAGTTTGCTTTGGATGGGTTCTTCTCCTCCATCAGAAAGGAA TATTCAGTGTCCAGGGTCAATGTATCAATCACTCTCTGTGTTCTTGGCCTCATAGACACA GAAACAGCCATGAAGGCAGTTTCTGGGATAGTCCATATGCAAGCAGCTCCAAAGGAGGAA TGTGCCCTGGAGATCATCAAAGGGGGAGCTCTGCGCCAAGAAGAAGTGTATTATGACAGC TCACTCTGGACCACTCTTCTGATCAGAAATCCATGCAGGAAGATCCTGGAATTTCTCTAC TCAACGAGCTATAATATGGACAGATTCATAAACAAGTAG PF00106 adh_short function oxidoreductase activity function catalytic activity process metabolism process physiological process BE0002025 Bifunctional protein GlmU Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Bifunctional protein GlmU Cell wall/membrane/envelope biogenesis Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. Responsible for the acetylation of Glc-N-1-P to give GlcNAc-1-P and for the uridyl transfer from UTP to GlcNAc-1-P which produces UDP-GlcNAc glmU Cytoplasm None 6.52 49191.0 Escherichia coli (strain K12) GenBank Gene Database X01631 UniProtKB P0ACC7 UniProt Accession GLMU_ECOLI EC 2.3.1.157] EC 2.7.7.23 Glucosamine-1-phosphate N-acetyltransferase N-acetylglucosamine-1-phosphate uridyltransferase >Bifunctional protein glmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGD LLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDA KPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADM KRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQ SEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKN SVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSK AGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGAT IAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKK PF00132 Hexapep PF01128 IspD function transferase activity function transferase activity, transferring phosphorus-containing groups function 4-diphosphocytidyl-2C-methyl-D-erythritol synthase activity function UDP-N-acetylglucosamine diphosphorylase activity function nucleotidyltransferase activity function catalytic activity process polysaccharide biosynthesis process lipopolysaccharide biosynthesis process macromolecule biosynthesis process primary metabolism process lipid metabolism process cellular lipid metabolism process physiological process process isoprenoid metabolism process isoprenoid biosynthesis process metabolism process carbohydrate biosynthesis process macromolecule metabolism BE0001799 Hydroxylamine reductase Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Hydroxylamine reductase Energy production and conversion Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O hcp Cytoplasm None 6.45 58660.0 Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) GenBank Gene Database Z11975 GenBank Protein Database 49286 UniProtKB Q01770 UniProt Accession HCP_DESDA EC 1.7.-.- HCP Hybrid-cluster protein Prismane protein >Hydroxylamine reductase MSNAMFCYQCQETVGNKGCTQVGVCGKKPETAALQDALIYVTKGLGQIATRLRAEGKAVD HRIDRLVTGNLFATITNANFDDDILAERVRMTCAAKKELAASLTDKSGLSDAALWEASEK SAMLAKAGTVGVMATTDDDVRSLRWLITFGLKGMAAYAKHADVLGKHENSLDAFMQEALA KTLDDSLSVADLVALTLETGKFGVSAMALLDAANTGTYGHPEITKVNIGVGSNPGILISG HDLRDLEMLLKQTEGTGVDVYTHSEMLPAHYYPAFKKYAHFKGNYGNAWWKQKEEFESFN GPVLLTTNCLVPPKDSYKDRVYTTGIVGFTGCKHIPGEIGEHKDFSAIIAHAKTCPAPTE IESGEIIGGFAHNQVLALADKVIDAVKSGAIKKFVVMAGCDGRAKSRSYYTDFAEGLPKD TVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLEDVNDLPI VYNIAWYEQKAVIVLLALLSLGVKNIHLGPTLPAFLSPNVAKVLVEQFNIGGITSPQDDL KAFFG >1638 bp ATGAGTAATGCCATGTTCTGCTACCAGTGCCAGGAAACCGTGGGTAACAAAGGCTGCACC CAGGTAGGCGTGTGCGGCAAAAAGCCTGAAACAGCCGCCCTTCAGGACGCGCTGATCTAT GTGACCAAGGGCCTCGGCCAGATCGCCACGCGCCTGCGCGCCGAAGGCAAGGCCGTTGAC CACAGGATAGACCGCCTGGTTACCGGCAACCTGTTTGCCACCATCACCAATGCCAACTTT GACGACGACATCCTTGCCGAGCGTGTGCGCATGACCTGTGCCGCCAAAAAGGAACTGGCC GCGTCCCTTACCGACAAGAGCGGCCTCAGCGATGCAGCCTTGTGGGAAGCATCCGAAAAG TCCGCCATGCTGGCCAAGGCCGGAACCGTAGGCGTTATGGCCACCACCGATGATGATGTG CGCTCCCTGCGCTGGCTCATCACCTTTGGGCTCAAGGGCATGGCGGCCTACGCCAAACAT GCGGATGTGCTTGGCAAGCATGAAAACAGCCTTGACGCCTTCATGCAGGAAGCCCTTGCC AAAACCCTGGATGACAGCCTGAGCGTGGCCGACCTTGTGGCCCTGACCCTTGAAACGGGC AAGTTCGGCGTATCGGCCATGGCCCTGCTGGATGCTGCCAATACCGGTACCTACGGCCAC CCAGAAATTACCAAGGTCAACATCGGCGTGGGCAGCAATCCCGGCATCCTCATTTCCGGG CATGACCTGCGCGACCTTGAAATGCTGCTCAAGCAGACCGAAGGCACAGGCGTTGACGTG TACACCCACTCTGAAATGCTGCCCGCCCATTACTACCCTGCCTTCAAGAAGTACGCGCAC TTCAAGGGCAACTACGGCAATGCATGGTGGAAACAGAAAGAAGAATTTGAAAGCTTTAAC GGCCCCGTGCTGCTGACCACCAACTGCCTTGTGCCGCCCAAGGACAGCTACAAGGACCGC GTGTACACCACCGGCATCGTGGGTTTTACGGGCTGCAAGCATATCCCCGGTGAAATCGGC GAACACAAGGACTTCAGCGCCATCATCGCCCATGCCAAGACCTGTCCCGCGCCTACGGAA ATCGAATCCGGCGAAATCATCGGCGGCTTCGCGCACAATCAGGTACTGGCCCTGGCCGAC AAGGTGATTGACGCGGTCAAATCCGGCGCCATCAAAAAGTTCGTGGTCATGGCCGGCTGC GACGGCCGCGCCAAGTCCCGCAGCTACTACACCGACTTTGCCGAAGGCCTGCCCAAAGAC ACGGTCATCCTTACCGCCGGTTGCGCCAAATATCGCTACAACAAGCTCAACCTGGGTGAC ATCGGCGGCATCCCGCGCGTACTGGACGCCGGGCAGTGCAACGACTCCTACTCCCTGGCC GTCATCGCCCTCAAGCTCAAGGAAGTATTCGGCCTCGAGGACGTCAACGACCTGCCCATC GTCTACAATATCGCCTGGTACGAGCAGAAGGCCGTTATCGTGCTGCTGGCCCTGCTGAGC CTCGGCGTGAAGAATATCCACCTCGGACCGACGCTGCCCGCCTTCCTTTCGCCCAACGTG GCCAAGGTGCTGGTGGAACAGTTCAACATCGGCGGCATCACCAGTCCGCAGGACGACCTC AAGGCGTTCTTCGGCTAA PF03063 Prismane component cell component intracellular component cytoplasm function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function binding function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism BE0001844 Diaminopimelate decarboxylase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Diaminopimelate decarboxylase Amino acid transport and metabolism Meso-2,6-diaminoheptanedioate = L-lysine + CO(2) lysA None 5.97 46178.0 Escherichia coli (strain K12) GenBank Gene Database J01614 GenBank Protein Database 455170 UniProtKB P00861 UniProt Accession DCDA_ECOLI DAP decarboxylase EC 4.1.1.20 >Diaminopimelate decarboxylase MPHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRFAQKACSNIH ILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVN AGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQR HHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVD TEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDA GFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRA LPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQARLIRRRQTIEELLALELL >1263 bp TTAAAGCAATTCCAGCGCCAGTAATTCTTCGATGGTCTGGCGACGGCGAATCAACCGCGC CTGACCATTATCAAACAGAACTTCTGGTAACAGCGGACGGCTATTGTAGTTGGATGACAT TGATGCGCCATATGCCCCTGTATCATGCAGTACCAGATAATCACCTGCCTTCACTTCCGG CAAGGCGCGGGTTTCAACATTTCCCCCTTCCTGCTGGGTAAAGACATCGCCCGATTCACA TAACGGTCCGGCGACGACGGTTTCCACCGTTGGCGCGTGTTCCAGAGAACGACCATCAGC TGCCAGGGCACTGATATGGTGGTAACTACCGTACATTGCCGGGCGCATCAGATCGTTGAA CCCGGCATCAACCAGCACAAAGTGGCGGCTCCCCATTTGTTTGACGCTCCGCACCTGAGT AATTAATACGCCAGACTGCGCTACCAGGAAGCGACCCGGTTCAATTTCCAGTTTCACAGG GTGGCCCAAATGGCGGGCGATTTGCTCACGCGCGGCATTCCACAGACCATAATAATGTTC GGTATCAACCGCCTCTTCACCCTGTTGATAAGGAACAGAAAGCCCACCGCCCGCAGAAAT AGCCTGTAAATCCTGACCGAATTCGATGACCTGACGCACCATAGCACCACACACCTGTTC CAGATGGGCATAATCAACGCCAGAACCAATGTGCATGTGAATGCCGACCAGCTGCAGATG ATGACGTTGTATCACGTCCAGTGCGGCGGGCAGATCGGTGTACCAGATACCGTGCTTGCT GTTTTCGCCACCGGTATTGGTTTTTTGGCTATGTCCGTGACCAAACCCCGGATTAACGCG CAGCCATACCCGATGCCCTGGCGAAACCTGGCCCAGTTGGTCGAGCATATCAACAGAACC CGCATTCACCGGAATTTGCAATTCACTGACGCGTTCAAGCGTCGCCTGATCGATAACATC TGCCGTAAAAACAATATCATCGGGGTGCGTTTGCGGATTGTAACCCGCCGCCAACGCACG CTCTATTTCGCCTAACGAGACGGAATCCACTTTCACGCCCTGCTCACGCATTAAGCGCAA AATATGAATATTGGAACAGGCTTTCTGTGCAAAGCGCACCACATCAAACTGTTTCAGCGC TGCAATCTGCCGACGAATAATTTGCGCATCGTAGACCCACACCGGGCAGCCAAATTCAGC GGGCAAACGCAGCAGATTTTCGGCGGTGAGATCGGTATCGGTGCTGAACAGTGAATGTGG CAT PF02784 Orn_Arg_deC_N PF00278 Orn_DAP_Arg_deC function diaminopimelate decarboxylase activity function lyase activity function carbon-carbon lyase activity function carboxy-lyase activity function catalytic activity process lysine biosynthesis via diaminopimelate process metabolism process cellular metabolism process amino acid metabolism process amino acid and derivative metabolism process aspartate family amino acid metabolism process lysine metabolism process physiological process process lysine biosynthesis BE0001920 Alpha-xylosidase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Alpha-xylosidase Carbohydrate transport and metabolism yicI Cytoplasmic None 5.61 88080.0 Escherichia coli (strain K12) GenBank Gene Database L10328 GenBank Protein Database 290506 UniProtKB P31434 UniProt Accession XYLS_ECOLI >Putative family 31 glucosidase yicI MKISDGNWLIQPGLNLIHPLQVFEVEQQDNEMVVYAAPRDVRERTWQLDTPLFTLRFFSP QEGIVGVRIEHFQGALNNGPHYPLNILQDVKVTIENTERYAEFKSGNLSARVSKGEFWSL DFLRNGERITGSQVKNNGYVQDTNNQRNYMFERLDLGVGETVYGLGERFTALVRNGQTVE TWNRDGGTSTEQAYKNIPFYMTNRGYGVLVNHPQCVSFEVGSEKVSKVQFSVESEYLEYF VIDGPTPKAVLDRYTRFTGRPALPPAWSFGLWLTTSFTTNYDEATVNSFIDGMAERNLPL HVFHFDCFWMKAFQWCDFEWDPLTFPDPEGMIRRLKAKGLKICVWINPYIGQKSPVFKEL QEKGYLLKRPDGSLWQWDKWQPGLAIYDFTNPDACKWYADKLKGLVAMGVDCFKTDFGER IPTDVQWFDGSDPQKMHNHYAYIYNELVWNVLKDTVGEEEAVLFARSASVGAQKFPVHWG GDCYANYESMAESLRGGLSIGLSGFGFWSHDIGGFENTAPAHVYKRWCAFGLLSSHSRLH GSKSYRVPWAYDDESCDVVRFFTQLKCRMMPYLYREAARANARGTPMMRAMMMEFPDDPA CDYLDRQYMLGDNVMVAPVFTEAGDVQFYLPEGRWTHLWHNDELDGSRWHKQQHGFLSLP VYVRDNTLLALGNNDQRPDYVWHEGTAFHLFNLQDGHEAVCEVPAADGSVIFTLKAARTG NTITVTGAGEAKNWTLCLRNVVKVNGLQDGSQAESEQGLVVKPQGNALTITL >2319 bp TTACAACGTAATTGTCAGCGCATTCCCTTGAGGCTTCACCACCAGCCCCTGCTCACTTTC AGCCTGCGAACCGTCTTGCAGACCATTTACTTTCACAACATTGCGCAGGCACAGTGTCCA GTTCTTCGCCTCGCCCGCACCAGTCACAGTAATCGTGTTGCCAGTACGTGCTGCTTTTAA AGTAAAGATCACCGATCCGTCAGCAGCGGGCACTTCACAGACGGCTTCATGCCCGTCTTG CAGATTGAAGAGGTGGAATGCCGTGCCTTCGTGCCACACGTAATCGGGACGTTGATCGTT GTTGCCCAGCGCCAGTAGAGTGTTATCACGCACATAAACGGGCAGACTCAGGAAGCCGTG CTGCTGTTTATGCCAGCGACTACCGTCGAGTTCATCGTTGTGCCACAGGTGTGTCCAGCG ACCTTCCGGCAGGTAGAACTGCACATCGCCCGCTTCAGTGAACACCGGCGCAACCATCAC GTTGTCGCCTAACATGTATTGACGGTCAAGGTAATCACAAGCCGGATCGTCCGGGAACTC CATCATCATGGCCCGCATCATCGGCGTACCCCGCGCGTTCGCACGCGNAGCTTCACGATA CAGATACGGCATCATGCGGCATTTCAGTTGCGTGAAGAAGCGCACCACATCACAGGACTC ATCATCGTAGGCCCACGNNACACGATAAGATTTGCTACCGTGTAAACGGCTATGGCTGGA GAGCAAACCAAACGCGCACCAGCGTTTGTAAACGTGCGCCGGAGCGGTATTTTCAAAGCC GCCGATATCGTGGCTCCAGAAGCCAAAACCTGAAAGGCCAATAGACAAACCACCGCGCAG GCTTTCCGCCATTGATTCGTAGTTAGCGTAACAATCGCCACCCCAGTGTACCGGGAATTT CTGCGCACCGACGGAGGCCGAGCGGGCAAACAAGACAGCTTCTTCCTCACCAACGGTGTC CTTGAGCACGTTCCACACCAGTTCGTTGTAGATGTACGCATAATGGTTATGCATTTTCTG CGGATCGGAACCGTCAAACCACTGAACATCAGTTGGGATACGTTCGCCAAAGTCGGTCTT AAAGCAATCAACGCCCATCGCGACCAGACCTTTCAGTTTGTCGGCGTACCATTTGCAGGC ATCCGGATTGGTAAAGTCATAAATCGCCAGACCTGGCTGCCATTTATCCCACTGCCATAG CGAACCGTCCGGGCGTTTGAGTAAATAGCCTTTCTCTTGTAACTCTTTAAAGACGGGGGA TTTTTGACCGATATAGGGGTTAATCCAGACGCAGATTTTCAGTCCTTTCGCTTTCAGGCG GCGGATCATCCCTTCCGGGTCAGGGAAAGTCAGCGGGTCCCACTCAAAATCGCACCACTG GAAGGCTTTCATCCAGAAACAGTCAAAGTGGAAAACATGCAGCGGCAGATTGCGTTCCGC CATACCATCGATAAAGCTGTTTACCGTCGCTTCGTCGTAGTTGGTGGTAAATGAAGTGGT TANNCACAGGCCGAAGGACCACGCGGGCGNCANNGCCGGACGACCAGTAAAGCGGGTATA ACGATCAAGTACCGCTTTCGGCGTCGGGCCGTCGATAACAAAGTATTCGAGATATTCACT CTCAACGCTGAACTGCACTTTGGAGACTTTCTCCGATCCCACTTCAAAAGAGACACACTG GGGATGATTGACCAGTACCCCATAACCACGGTTAGTCATGTAGAACGGGATATTTTTATA CGCCTGTTCAGTACTTGTGCCGCCGTCCCGGTTCCAGGTCTCTACCGTCTGGCCATTGCG CACCAGGGCAGTAAAGCGCTCTCCCAGACCGTAAACTGTTTCGCCAACGCCAAGATCAAG CCGCTCAAACATATAATTGCGTTGATTATTCGTGTCCTGCACGTAGCCATTATTTTTCAC CTGACTACCGGTAATACGTTCGCCGTTGCGCAGAAAATCCAGTGACCAGAACTCACCTTT GCTGACACGCGCGCTTAAGTTGCCACTTTTAAACTCAGCATAACGTTCTGTGTTTTCGAT TGTGACCTTCACGTCCTGCAAAATATTGAGCGGATAATGAGGACCGTTATTCAGCGCCCC CTGAAAATGCTCAATCCGCACACCGACAATACCTTCCTGTGGGGAGAAAAAGCGCAACGT AAATAAAGGCGTATCAAGCTGCCAGGTACGTTCACGCACATCACGGGGGGCAGCATAGAC CACCATTTCATTATCCTGCTGTTCAACCTCGAACACCTGAAGCGGGTGAATCAAATTGAG GCCAGGTTGAATCAACCAGTTTCCATCGCTAATTTTCAT PF01055 Glyco_hydro_31 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function catalytic activity function hydrolase activity process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism BE0001865 Limonene-1,2-epoxide hydrolase Rhodococcus erythropolis # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Limonene-1,2-epoxide hydrolase Involved in limonene-1,2-epoxide hydrolase activity Limonene-1,2-epoxide + H(2)O = limonene-1,2- diol limA None 4.21 16521.0 Rhodococcus erythropolis GenBank Gene Database Y18005 GenBank Protein Database 4160334 UniProtKB Q9ZAG3 UniProt Accession LIMA_RHOER EC 3.3.2.8 >Limonene-1,2-epoxide hydrolase MTSKIEQPRWASKDSAAGAASTPDEKIVLEFMDALTSNDAAKLIEYFAEDTMYQNMPLPP AYGRDAVEQTLAGLFTVMSIDAVETFHIGSSNGLVYTERVDVLRALPTGKSYNLSILGVF QLTEGKITGWRDYFDLREFEEAVDLPLRG >450 bp ATGACATCAAAGATCGAACAACCTCGCTGGGCGTCCAAGGACAGTGCCGCCGGCGCTGCC TCGACTCCGGACGAAAAGATCGTTCTGGAGTTCATGGACGCACTGACCAGTAATGATGCT GCAAAACTCATTGAGTACTTTGCAGAAGACACGATGTACCAGAACATGCCACTCCCCCCT GCATACGGCCGCGACGCCGTCGAGCAAACTCTGGCTGGCCTGTTCACCGTCATGAGCATC GATGCGGTGGAGACGTTCCATATCGGCTCGAGTAACGGACTTGTGTACACCGAACGTGTC GATGTCCTACGCGCACTACCCACCGGCAAGAGCTACAACCTGTCAATCCTCGGAGTCTTC CAGCTCACCGAGGGCAAGATTACGGGTTGGCGTGACTACTTCGATCTGCGCGAATTCGAA GAAGCTGTCGACCTTCCCCTCCGCGGCTAA PF07858 LEH BE0001911 Mannan endo-1,4-beta-mannosidase Cellvibrio japonicus (strain Ueda107) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Mannan endo-1,4-beta-mannosidase Involved in mannan endo-1,4-beta-mannosidase activity Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Preferentially hydrolyzes the larger oligosaccharides manA Cytoplasmic None 5.46 47488.0 Cellvibrio japonicus (strain Ueda107) GenBank Gene Database X82179 GenBank Protein Database 14594858 UniProtKB P49424 UniProt Accession MANA_CELJU EC 3.2.1.78 Mannan endo-1,4-beta-mannosidase precursor Mannanase A >Mannan endo-1,4-beta-mannosidase precursor MKTITTARLPWAAQSFALGICLIALLGCNHAANKSSASRADVKPVTVKLVDSQATMETRS LFAFMQEQRRHSIMFGHQHETTQGLTITRTDGTQSDTFNAVGDFAAVYGWDTLSIVAPKA EGDIVAQVKKAYARGGIITVSSHFDNPKTDTQKGVWPVGTSWDQTPAVVDSLPGGAYNPV LNGYLDQVAEWANNLKDEQGRLIPVIFRLYHENTGSWFWWGDKQSTPEQYKQLFRYSVEY LRDVKGVRNFLYAYSPNNFWDVTEANYLERYPGDEWVDVLGFDTYGPVADNADWFRNVVA NAALVARMAEARGKIPVISEIGIRAPDIEAGLYDNQWYRKLISGLKADPDAREIAFLLVW RNAPQGVPGPNGTQVPHYWVPANRPENINNGTLEDFQAFYADEFTAFNRDIEQVYQRPTL IVK >1272 bp ATGAAAACTATTACCACTGCACGCCTTCCATGGGCTGCGCAGAGCTTTGCCTTGGGCATT TGCCTGATAGCGCTGTTGGGTTGTAATCACGCCGCTAATAAATCATCGGCATCCAGGGCA GATGTCAAACCTGTTACGGTCAAACTGGTCGATTCCCAGGCGACCATGGAAACCCGTTCC CTGTTTGCGTTTATGCAGGAGCAGCGCAGACATTCCATTATGTTTGGGCACCAGCACGAA ACAACCCAGGGACTCACTATTACCCGCACAGATGGTACCCAATCCGATACCTTTAATGCC GTTGGTGATTTTGCAGCGGTCTATGGTTGGGACACGCTGTCTATTGTTGCCCCTAAAGCG GAGGGCGATATTGTCGCCCAAGTAAAAAAGGCTTATGCGCGCGGGGGCATCATTACGGTG AGCTCGCATTTTGATAATCCAAAAACCGATACCCAAAAGGGCGTATGGCCCGTTGGCACT TCCTGGGATCAAACCCCGGCTGTTGTGGATTCCCTGCCTGGAGGCGCCTATAACCCGGTA TTAAATGGCTATCTCGACCAGGTGGCCGAGTGGGCCAATAACCTGAAAGACGAGCAGGGG CGGCTGATACCGGTCATCTTTCGCCTGTACCACGAAAATACCGGCAGTTGGTTCTGGTGG GGAGATAAGCAATCAACCCCTGAACAATACAAGCAATTGTTCCGCTATTCCGTCGAGTAT TTGCGCGATGTGAAAGGTGTGCGCAATTTCCTGTATGCCTATTCGCCCAACAACTTTTGG GACGTGACCGAGGCCAATTACCTGGAGCGTTATCCGGGGGATGAGTGGGTGGATGTACTG GGATTTGATACCTATGGCCCGGTGGCGGACAACGCTGACTGGTTCCGCAATGTGGTGGCC AATGCGGCCTTGGTTGCCCGCATGGCGGAAGCGCGGGGCAAAATACCGGTGATCTCCGAG ATAGGTATACGCGCTCCCGACATTGAAGCCGGGCTCTATGATAACCAGTGGTATCGCAAG CTTATCTCCGGCCTCAAGGCCGATCCGGATGCACGCGAGATTGCCTTCCTGCTGGTATGG CGCAATGCCCCGCAGGGAGTTCCTGGCCCCAATGGCACCCAGGTTCCCCATTATTGGGTG CCTGCTAACCGCCCGGAGAATATCAACAATGGCACCCTGGAGGACTTCCAGGCCTTTTAT GCCGATGAATTCACAGCGTTCAATCGCGACATCGAGCAGGTCTATCAGCGTCCGACCCTG ATAGTTAAATAG PF02156 Glyco_hydro_26 function hydrolase activity, acting on glycosyl bonds function hydrolase activity, hydrolyzing O-glycosyl compounds function mannosidase activity function beta-mannosidase activity function catalytic activity function mannan endo-1,4-beta-mannosidase activity function hydrolase activity process carbohydrate metabolism process polysaccharide metabolism process cellular polysaccharide metabolism process physiological process process metabolism process mannan metabolism process macromolecule metabolism BE0000259 Beta-1,4-galactosyltransferase 1 Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Beta-1,4-galactosyltransferase 1 Involved in transferase activity, transferring glycosyl groups The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix B4GALT1 9p13 Isoform Long, isoform Short:Golgi apparatus; Golgi stack; Golgi stack membrane; single-pass type II 25-44 8.77 43921.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:924 GenAtlas B4GALT1 GeneCards B4GALT1 GenBank Gene Database X14085 GenBank Protein Database 29424 UniProtKB P15291 UniProt Accession B4GT1_HUMAN b4Gal-T1 Beta-1,4-GalTase 1 Beta4Gal-T1 EC 2.4.1.- EC 2.4.1.22 EC 2.4.1.90 N-acetyllactosamine synthase UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 1 UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 1 >Beta-1,4-galactosyltransferase 1 MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS >1203 bp ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCGCCGCGATGCCAGGCGCGTCCCTACAGCGG GCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTACTAC CTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTGCAG GGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGAGGG GCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCCAGC CCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCCCAC ACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCCATG CTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAATGTG AAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAAGTGGCCATCATC ATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCAGTC CTGCAGCGCCAGCAGCTGGACTATGGCATCTATGGCATCTATGTTATCAACCAGGCGGGA GACACTATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGAC TATGACTACACCTGCTTTGTGTTTAGTGACGTGGACCTCATCCCAATGAATGACCATAAT GCGTACAGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTC AGCCTACCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTA ACCATCAATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTT AACAGATTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGT CGCATGATCCGCCACTCAAGAGACAAAAAAAATGAACCCAATCCTCAGAGGTTTGACCGA ATTGCACACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTG CTGGATGTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGC TAG PF02709 Galactosyl_T_2 function catalytic activity function transferase activity function transferase activity, transferring glycosyl groups process carbohydrate metabolism process physiological process process metabolism process macromolecule metabolism BE0001902 Tyrosine-protein kinase transforming protein Abl Abelson murine leukemia virus # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Tyrosine-protein kinase transforming protein Abl Involved in protein kinase activity ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate ABL None 9.33 81873.0 Abelson murine leukemia virus GenBank Gene Database V01541 UniProtKB P00521 UniProt Accession ABL_MLVAB EC 2.7.10.2 V- abl >Tyrosine-protein kinase transforming protein Abl YITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHY RINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDK WEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIK HPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVSAVVLLYMATQISSAMEYL EKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYN KFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRA CWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKRGTRGGAGSMLQAPELPTKTRT CRRAAEQKASPPSLTPKLLRRQVTASPSSGLSHKKEATKGSASGMGTPATAEPAPPSNKV GLSKASSEEMRVRRHKHSSESPGRDKGRLAKLKPAPPPPPACTGKAGKPAQSPSQEAGEA GGPTKTKCTSLAMDAVNTDPTKAGPPGEGLRKPVPPSVPKPQSTAKPPGTPTSPVSTPST APAPSPLAGDQQPSSAAFIPLISTRVSLRKTRQPPERIASGTITKGVVLDSTEALCLAIS RNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLESNLRELQICPATA SSGPAATQDFSKLLSSVKEISDIVRR PF07714 Pkinase_Tyr PF00017 SH2 PF08919 F_actin_bind function catalytic activity function protein-tyrosine kinase activity function ATP binding function transferase activity, transferring phosphorus-containing groups function kinase activity function nucleotide binding function protein kinase activity function purine nucleotide binding function adenyl nucleotide binding function binding function transferase activity process cell communication process metabolism process signal transduction process macromolecule metabolism process biopolymer metabolism process biopolymer modification process protein modification process intracellular signaling cascade process protein amino acid phosphorylation process physiological process process cellular process BE0002075 Thiol:disulfide interchange protein DsbC Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Thiol:disulfide interchange protein DsbC Posttranslational modification, protein turnover, chaperones Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase dsbC Periplasm None 6.78 25622.0 Escherichia coli (strain K12) GenBank Gene Database M54884 UniProtKB P0AEG6 UniProt Accession DSBC_ECOLI >Thiol:disulfide interchange protein dsbC precursor MKKGFMLFTLLAAFSGFAQADDAAIQQTLAKMGIKSSDIQPAPVAGMKTVLTNSGVLYIT DDGKHIIQGPMYDVSGTAPVNVTNKMLLKQLNALEKEMIVYKAPQEKHVITVFTDITCGY CHKLHEQMADYNALGITVRYLAFPRQGLDSDAEKEMKAIWCAKDKNKAFDDVMAGKSVAP ASCDVDIADHYALGVQLGVSGTPAVVLSNGTLVPGYQPPKEMKEFLDEHQKMTSGK function electron transporter activity function transporter activity process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism BE0002057 Glyceraldehyde-3-phosphate dehydrogenase A Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Glyceraldehyde-3-phosphate dehydrogenase A Carbohydrate transport and metabolism D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH gapA Cytoplasm None 7.13 35533.0 Escherichia coli (strain K12) GenBank Gene Database X02662 UniProtKB P0A9B2 UniProt Accession G3P1_ECOLI EC 1.2.1.12 GAPDH-A >Glyceraldehyde-3-phosphate dehydrogenase A MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEV KDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMT GPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATT ATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIA LNDNFVKLVSWYDNETGYSNKVLDLIAHISK PF02800 Gp_dh_C PF00044 Gp_dh_N function oxidoreductase activity function oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor function cofactor binding function glyceraldehyde-3-phosphate dehydrogenase activity function coenzyme binding function glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity function binding function catalytic activity function NAD binding function oxidoreductase activity, acting on the aldehyde or oxo group of donors process alcohol metabolism process monosaccharide metabolism process hexose metabolism process glucose metabolism process physiological process process glucose catabolism process glycolysis process metabolism process cellular metabolism BE0003028 (S)-mandelate dehydrogenase Pseudomonas putida unknown (S)-mandelate dehydrogenase Involved in catalytic activity Reduction of L(+)-mandelate to benzoylformate mdlB None 8.22 43438.0 Pseudomonas putida GenBank Gene Database AY143338 UniProtKB P20932 UniProt Accession MDLB_PSEPU EC 1.-.-.- MDH S-mandelate dehydrogenase >L(+)-mandelate dehydrogenase MSQNLFNVEDYRKLRQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRR SLQAEVLGKRQSMPLLIGPTGLNGALWPKGDLALARAATKAGIPFVLSTASNMSIEDLAR QCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFKIPMSYS AKVVLDGCLHPRWSLDFVRHGMPQLANFVSSQTSSLEMQAALMSRQMDASFNWEALRWLR DLWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPV LIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIG CPDITSLSPDYLQNEGVTNTAPVDHLIGKGTHA >1182 bp TCATGCGTGTGTTCCTTTACCAATGAGGTGATCGACTGGAGCGGTGTTAGTCACTCCCTC GTTTTGGAGGTAATCAGGAGAAAGGGAGGTGATGTCAGGGCATCCAATCTGGGCAAGGGT GCGGTCGATATCCGCTTTTAGGAGGGTTAGCACCTCGTCAACACCCGTTTCACCTCGTGC TGCAAGGCCATACAAAGTTGCACGACCCAGGAGTACAGCCTCAGCACCTAGCGCAAGTGC TTTAACGATGTCCGAACCCCGTCGGAAGCCGCTATCGATAAGCACTGGTTTTCCAGTTTT CGCTACCGATTGAGCCAAAACTTCCATTGGCGATATCGCGCAATCGAGTTGGCGACCGCC GTGGTTTGATAGGATTACGCCGTCTGCACCTTCAGCGATGCACCGATCGGCGTCCTCAGC ACTGAGCAACCCCTTTACGAGGAGTTTGTGCGGCCAGAGGTCACGCAGCCATCTCAATGC CTCCCAGTTGAAACTGGCATCCATTTGGCGGCTCATCAATGCTGCCTGCATTTCTAAGCT AGACGTTTGACTGCTGACGAAATTGGCCAGTTGCGGCATGCCGTGTCGCACGAAGTCGAG CGACCAGCGCGGATGCAGGCATCCGTCCAGCACCACCTTTGCGGAGTAGCTCATTGGTAT CTTGAATCGGTTATGCAGGTCGCGCTCGCGATAGCCGTTAACCGCCACATCCGTAGTAAG CACCAGTGTCGTGTAACCAGTGTGCAGGGCTTTGAGCACCATCCCCTGCGCAATCTCTCG GTGGATCACATAGAGCTGGAACCACAGATCGCCATCACACTGACGTGCGAGGTCTTCAAT GGACATGTTGGAGGCGGTCGACAGCACGAACGGGATTCCGGCCTTGGTTGCTGCTCGAGC TAAAGCGAGATCCCCCTTAGGCCACAGCGCACCGTTCAGCCCAGTAGGCCCAATCAAGAG AGGCATCGACTGCCTCTTTCCAAGTACTTCCGCTTGGAGGCTGCGGCGGCTGACGTCTAC TAGCCGCTTCGGTTTGAATCGCCATTGCTGGAAGACGTCGCGGTTGTGTTTCACCCCGTA TTCGTCTTCAGCCCCACCTTCCAGATAGTCGTAGACCATCTTCGGCAAGCGCTTTTGCCG AAGCTTGCGATAGTCCTCAACGTTAAAGAGATTCTGGCTCAT PF01070 FMN_dh function catalytic activity function nucleotide binding function FMN binding function oxidoreductase activity function binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0002802 Dissimilatory copper-containing nitrite reductase Alcaligenes xylosoxydans xylosoxydans unknown Dissimilatory copper-containing nitrite reductase Involved in copper ion binding nir None 7.55 38940.0 Alcaligenes xylosoxydans xylosoxydans GenBank Gene Database AF051831 UniProtKB O68601 UniProt Accession O68601_ALCXX NiR) precursor Nitrite Reductase >Dissimilatory copper-containing nitrite reductase MNALRPTLLAAALAFTMAAGTAWAQDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFT MTIEEKKMVIDDKGTTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGA TGALGGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLPRDGL KDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTVQVMRTLTPSHIVFNG KVGALTGANALTAKVGETVLLIHSQANRDTRPHLIGGHGDWVWETGKFANPPQRDLETWF IRGGSAGAALYTFKQPGVYAYLNHNLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR >1083 bp ATGAACGCATTACGGCCCACTTTGCTGGCGGCGGCGCTGGCTTTTACGATGGCCGCCGGG ACCGCCTGGGCGCAGGACGCCGACAAGCTGCCCCATACCAAGGTCACGCTGGTCGCTCCG CCCCAGGTGCATCCGCACGAGCAGGCGACCAAGTCGGGCCCCAAAGTCGTCGAATTCACC ATGACCATCGAGGAAAAGAAGATGGTGATCGACGACAAGGGCACGACGCTGCAGGCCATG ACGTTCAACGGCTCCATGCCCGGCCCCACGCTGGTGGTGCACGAGGGCGACTACGTCCAG CTGACGCTGGTCAACCCGGCCACCAACGCCATGCCGCACAACGTCGACTTCCACGGCGCC ACCGGCGCGCTGGGCGGCGCCAAGCTCACCAACGTCAACCCTGGCGAGCAGGCTACGCTG CGCTTCAAGGCCGACCGCAGCGGCACCTTCGTCTACCACTGCGCGCCCGAAGGCATGGTG CCCTGGCACGTGGTGTCGGGCATGAGCGGCACGCTGATGGTGCTGCCGCGCGACGGCCTG AAGGATCCGCAGGGCAAGCCGCTGCATTACGACCGCGCCTACACCATCGGCGAGTTCGAC CTGTACATCCCCAAGGGCCCGGACGGCAAGTACAAGGACTACGCCACGCTGGCCGAAAGC TATGGCGACACGGTGCAGGTGATGCGCACGCTGACGCCGTCGCACATCGTCTTCAATGGC AAGGTCGGCGCGCTGACCGGCGCCAACGCGCTCACCGCCAAGGTCGGCGAGACCGTGCTG CTGATCCACTCGCAGGCCAATCGCGACACCCGCCCGCACCTGATCGGCGGCCATGGCGAC TGGGTCTGGGAGACCGGCAAGTTCGCCAACCCGCCGCAGCGCGACCTGGAAACCTGGTTC ATCCGCGGCGGGTCGGCCGGCGCCGCGCTCTACACCTTCAAGCAGCCTGGCGTGTATGCC TACCTGAACCACAACCTGATCGAGGCCTTCGAACTGGGCGCGGCCGGCCACATCAAGGTC GAGGGCAAGTGGAACGACGACCTGATGAAGCAGATCAAGGCGCCCGCGCCGATTCCGCGC TGA PF00394 Cu-oxidase PF07732 Cu-oxidase_3 function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors function oxidoreductase activity, acting on other nitrogenous compounds as donors, cytochrome as acceptor function nitrite reductase (NO-forming) activity function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function binding function copper ion binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process process nitrogen compound metabolism BE0003186 33 kDa chaperonin Escherichia coli (strain K12) unknown 33 kDa chaperonin Involved in unfolded protein binding Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress hslO Cytoplasm None 4.1 32535.0 Escherichia coli (strain K12) GenBank Gene Database AP009048 UniProtKB P0A6Y5 UniProt Accession HSLO_ECOLI Heat shock protein 33 HSP33 >33 kDa chaperonin MPQHDQLHRYLFENFAVRGELVTVSETLQQILENHDYPQPVKNVLAELLVATSLLTATLK FDGDITVQLQGDGPMNLAVINGNNNQQMRGVARVQGEIPENADLKTLVGNGYVVITITPS EGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGDVDGKPAAGGMLLQVMPAQNA QQDDFDHLATLTETIKTEELLTLPANEVLWRLYHEEEVTVYDPQDVEFKCTCSRERCADA LKTLPDEEVDSILAEDGEIDMHCDYCGNHYLFNAMDIAEIRNNASPADPQVH >879 bp TTAATGAACTTGCGGATCTGCCGGAGACGCGTTGTTGCGGATTTCAGCAATATCCATCGC ATTGAACAGATAGTGGTTACCGCAGTAATCACAATGCATGTCAATTTCGCCATCTTCCGC CAGGATGCTATCAACTTCTTCATCAGGCAGCGTTTTCAGCGCATCGGCGCAACGTTCACG CGAGCAGGTGCATTTGAACTCCACATCCTGCGGATCGTAAACCGTCACCTCTTCTTCGTG ATACAAACGCCACAACACTTCGTTTGCCGGTAAGGTCAGCAGTTCTTCGGTTTTGATGGT TTCGGTTAGCGTCGCCAGGTGGTCAAAGTCGTCCTGCTGGGCATTTTGCGCAGGCATTAC CTGCAACAACATACCGCCTGCAGCCGGTTTGCCGTCTACGTCGCCGGTGCGAATAAACAG GCGCGTCGGCAGCTGTTCAGAACGCATAAAGTAATCTTCCAGGCAGGCCGCCAGGGTATC ACCTTCCAGACCAACTACGCCCTGATAGCGTTCGCCTTCGCTCGGGGTAATGGTGATCAC CACGTAACCATTGCCGACCAGCGTTTTCAGGTCGGCATTTTCTGGAATTTCGCCCTGCAC GCGCGCCACACCGCGCATCTGCTGGTTATTGTTACCGTTAATAACCGCCAGATTCATCGG ACCGTCGCCCTGCAGCTGTACGGTGATATCACCATCAAACTTCAGCGTAGCGGTTAACAG GCTGGTCGCAACCAGCAGTTCTGCCAGCACGTTTTTAACGGGCTGCGGATAATCGTGGTT CTCAAGGATCTGTTGCAGGGTTTCCGAAACGGTTACCAGTTCGCCGCGCACGGCAAAGTT TTCAAACAGATAGCGATGTAATTGGTCATGTTGCGGCAT PF01430 HSP33 component cell component intracellular component cytoplasm function protein binding function binding function unfolded protein binding process protein metabolism process cellular protein metabolism process protein folding process physiological process process metabolism process macromolecule metabolism BE0003187 Free methionine-R-sulfoxide reductase Escherichia coli (strain K12) unknown Free methionine-R-sulfoxide reductase Signal transduction mechanisms yebR None 4.45 20277.0 Escherichia coli (strain K12) GenBank Gene Database U00096 UniProtKB P76270 UniProt Accession MSRC_ECOLI >UPF0067 protein yebR MLILIGWQIQVRQPSDYIMNKTEFYADLNRDFNALMAGETSFLATLANTSALLYERLTDI NWAGFYLLEDDTLVLGPFQGKIACVRIPVGRGVCGTAVARNQVQRIEDVHVFDGHIACDA ASNSEIVLPLVVKNQIIGVLDIDSTVFGRFTDEDEQGLRQLVAQLEKVLATTDYKKFFAS VAG >552 bp TTATCCTGCGACGCTCGCAAAGAATTTTTTGTAATCCGTCGTTGCAAGCACTTTTTCAAG CTGTGCCACAAGCTGACGTAAGCCTTGCTCGTCCTCGTCTGTAAAGCGACCGAAGACGGT ACTATCGATGTCGAGAACACCAATAATCTGATTTTTCACCACCAGCGGCAGAACAATTTC AGAATTACTCGCCGCATCACAGGCAATATGCCCGTCAAACACATGAACATCCTCGATACG CTGCACTTGATTGCGGGCAACCGCAGTGCCGCACACGCCGCGCCCGACGGGTATCCGGAC ACAGGCAATTTTGCCCTGAAATGGTCCGAGTACCAGTGTATCGTCCTCAAGCAAATAAAA ACCTGCCCAGTTTATGTCAGTGAGACGCTCATATAACAACGCACTGGTGTTCGCAAGCGT TGCCAGAAAACTGGTTTCTCCCGCCATCAGCGCGTTAAAGTCGCGATTTAAATCCGCGTA AAATTCTGTTTTGTTCATTATATAATCACTTGGTTGTCTTACCTGGATCTGCCAGCCTAT TAAAATAAGCAT PF01590 GAF function molecular function unknown BE0002626 Ornithine cyclodeaminase Pseudomonas putida (strain KT2440) unknown Ornithine cyclodeaminase Amino acid transport and metabolism PP3533 None 6.25 38425.0 Pseudomonas putida (strain KT2440) GenBank Gene Database AE015451 UniProtKB Q88H32 UniProt Accession Q88H32_PSEPK >Ornithine cyclodeaminase MTYFIDVPTMSDLVHDIGVAPFIGELAAALRDDFKRWQAFDKSARVASHSEVGVIELMPV ADKSRYAFKYVNGHPANTARNLHTVMAFGVLADVDSGYPVLLSELTIATALRTAATSLMA AQALARPNARKMALIGNGAQSEFQALAFHKHLGIEEIVAYDTDPLATAKLIANLKEYSGL TIRRASSVAEAVKGVDIITTVTADKAYATIITPDMLEPGMHLNAVGGDCPGKTELHADVL RNARVFVEYEPQTRIEGEIQQLPADFPVVDLWRVLRGETEGRQSDSQVTVFDSVGFALED YTVLRYVLQQAEKRGMGTKIDLVPWVEDDPKDLFSHTRGRAGKRRIRRVA >1053 bp ATGACGTATTTCATTGATGTTCCAACCATGTCGGACTTGGTGCATGACATTGGCGTAGCG CCGTTTATTGGCGAGCTTGCCGCTGCCCTGCGGGACGATTTCAAACGCTGGCAGGCGTTT GACAAGTCCGCGCGCGTTGCCAGCCACTCGGAAGTGGGCGTGATCGAACTGATGCCGGTC GCCGACAAAAGCCGCTATGCCTTCAAATACGTCAACGGCCACCCGGCCAATACTGCACGC AACCTGCATACGGTGATGGCCTTCGGTGTACTGGCCGATGTCGACTCCGGTTACCCGGTG CTGCTGTCCGAACTGACCATCGCCACCGCCCTGCGCACCGCAGCGACTTCGCTGATGGCA GCCCAGGCACTGGCCCGCCCGAACGCGCGCAAGATGGCGCTGATCGGCAACGGCGCGCAA AGCGAATTCCAGGCCCTGGCCTTCCACAAGCACCTGGGCATCGAAGAAATCGTCGCCTAC GACACCGACCCGCTGGCCACCGCCAAGCTTATCGCCAACCTCAAGGAATACAGCGGCTTG ACCATCCGCCGGGCCAGCTCGGTAGCCGAGGCAGTGAAAGGCGTGGACATCATCACCACG GTAACGGCCGACAAGGCCTACGCCACCATCATTACCCCCGACATGCTGGAGCCCGGTATG CACCTGAACGCCGTGGGTGGTGACTGCCCTGGCAAAACCGAGCTGCACGCCGATGTGCTG CGCAACGCGCGGGTGTTCGTCGAGTACGAGCCACAAACCCGTATCGAAGGTGAGATCCAG CAGCTGCCGGCGGACTTTCCGGTGGTCGACCTGTGGCGCGTGCTGCGCGGAGAAACCGAG GGCCGCCAAAGCGACAGCCAGGTCACTGTATTCGATTCGGTGGGCTTCGCCCTCGAAGAT TACACCGTACTACGGTACGTACTACAGCAAGCCGAAAAGCGCGGGATGGGCACCAAGATC GACCTGGTGCCGTGGGTGGAGGACGACCCGAAAGACCTGTTCAGCCACACCCGAGGCCGC GCTGGCAAAAGGCGTATCCGACGGGTTGCCTGA PF02423 OCD_Mu_crystall BE0000540 Dihydropteridine reductase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Dihydropteridine reductase Lipid transport and metabolism The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases QDPR 4p15.31 None 7.45 25804.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9752 GenAtlas QDPR GeneCards QDPR GenBank Gene Database X04882 GenBank Protein Database 30819 UniProtKB P09417 UniProt Accession DHPR_HUMAN EC 1.5.1.34 HDHPR Quinoid dihydropteridine reductase >Dihydropteridine reductase MAAAAAAGEARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASATIIVKMTDSF TEQADQVTAEVGKLLGEEKVDAILCVAGGWAGGNAKSKSLFKNCDLMWKQSIWTSTISSH LATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMPPGAAAIAV LPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVTTEGRTELT PAYF >735 bp ATGGCGGCGGCGGCGGCTGCAGGCGAGGCGCGCCGGGTGCTGGTGTACGGCGGCAGGGGC GCTCTGGGTTCTCGATGCGTGCAGGCTTTTCGGGCCCGCAACTGGTGGGTTGCCAGCGTT GATGTGGTGGAGAATGAAGAGGCCAGCGCTACGATCATTGTTAAAATGACAGACTCGTTC ACTGAGCAGGCTGACCAGGTGACTGCTGAGGTTGGAAAGCTCTTGGGTGAAGAGAAGGTG GATGCAATTCTTTGCGTTGCTGGAGGATGGGCCGGGGGCAATGCCAAATCCAAGTCTCTC TTTAAGAACTGTGACCTGATGTGGAAGCAGAGCATATGGACATCGACCATCTCCAGCCAT CTGGCTACCAAGCATCTCAAGGAAGGAGGCCTCCTGACCTTGGCTGGCGCAAAGGCTGCC CTGGATGGGACTCCTGGTATGATCGGGTACGGCATGGCCAAGGGTGCTGTTCACCAGCTC TGCCAGAGCCTGGCTGGGAAGAACAGCGGCATGCCGCCCGGGGCAGCCGCCATCGCTGTG CTCCCGGTTACCCTGGATACCCCGATGAACAGGAAATCAATGCCTGAGGCTGACTTCAGC TCCTGGACACCCTTAGAATTCCTAGTTGAAACTTTCCATGACTGGATCACAGGGAAAAAC CGACCGAGCTCAGGAAGCCTAATCCAGGTGGTAACCACAGAAGGAAGGACGGAACTCACC CCAGCATATTTTTAG PF00106 adh_short function oxidoreductase activity function catalytic activity process metabolism process physiological process BE0000520 Argininosuccinate lyase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Argininosuccinate lyase Amino acid transport and metabolism ASL 7cen-q11.2 None 6.59 51744.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:746 GenAtlas ASL GeneCards ASL GenBank Gene Database Y00753 GenBank Protein Database 28878 UniProtKB P04424 UniProt Accession ARLY_HUMAN Arginosuccinase ASAL EC 4.3.2.1 >Argininosuccinate lyase MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEM DQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTD LRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVAL TRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA EFLFWRSLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKA GRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENM GQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLF SGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA >1395 bp ATGGCCTCGGAGAGTGGGAAGCTTTGGGGTGGCCGGTTTGTGGGTGCAGTGGACCCCATC ATGGAGAAGTTCAACGCGTCCATTGCCTACGACCGGCACCTTTGGGAGGTGGATGTTCAA GGCAGCAAAGCCTACAGCAGGGGCCTGGAGAAGGCAGGGCTCCTCACCAAGGCCGAGATG GACCAGATACTCCATGGCCTAGACAAGGTGGCTGAGGAGTGGGCCCAGGGCACCTTCAAA CTGAACTCCAATGATGAGGACATCCACACAGCCAATGAGCGCCGCCTGAAGGAGCTCATT GGTGCAACGGCAGGGAAGCTGCACACGGGACGGAGCCGGAATGACCAGGTGGTCACAGAC CTCAGGCTGTGGATGCGGCAGACCTGCTCCACGCTCTCGGGCCTCCTCTGGGAGCTCATT AGGACCATGGTGGATCGGGCAGAGGCGGAACGTGATGTTCTCTTCCCGGGGTACACCCAT TTGCAGAGGGCCCAGCCCATCCGCTGGAGCCACTGGATTCTGAGCCACGCCGTGGCACTG ACCCGAGACTCTGAGCGGCTGCTGGAGGTGCGGAAGCGGATCAATGTCCTGCCCCTGGGG AGTGGGGCCATTGCAGGCAATCCCCTGGGTGTGGACCGAGAGCTGCTCCGAGCAGAACTC AACTTTGGGGCCATCACTCTCAACAGCATGGATGCCACTAGTGAGCGGGACTTTGTGGCC GAGTTCCTGTTCTGGCGTTCGCTGTGCATGACCCATCTCAGCAGGATGGCCGAGGACCTC ATCCTCTACTGCACCAAGGAATTCAGCTTCGTGCAGCTCTCAGATGCCTACAGCACGGGA AGCAGCCTGATGCCCCAGAAGAAAAACCCCGACAGTTTGGAGCTGATCCGGAGCAAGGCT GGGCGTGTGTTTGGGCGGTGTGCCGGGCTCCTGATGACCCTCAAGGGACTTCCCAGCACC TACAACAAAGACTTACAGGAGGACAAGGAAGCTGTGTTTGAAGTGTCAGACACTATGAGT GCCGTGCTCCAGGTGGCCACTGGCGTCATCTCTACGCTGCAGATTCACCAAGAGAACATG GGACAGGCTCTCAGCCCCGACATGCTGGCCACTGACCTTGCCTATTACCTGGTCCGCAAA GGGATGCCATTCCGCCAGGCCCATGAGGCCTCCGGGAAAGCTGTGTTCATGGCCGAGACC AAGGGGGTCGCCCTCAACCAGCTGTCACTGCAGGAGCTGCAGACCATCAGCCCCCTGTTC TCGGGCGACGTGATCTGCGTGTGGGACTACCGGCACAGTGTGGAGCAGTATGGTGCCCTG GGCGGCACTGCGCGCTCCAGCGTCGACTGGCAAATCCGCCAGGTGCGGGCGCTACTGCAG GCACAGCAGGCCTAG PF00206 Lyase_1 function catalytic activity BE0003188 O-acetyl-ADP-ribose deacetylase Escherichia coli (strain K12) unknown O-acetyl-ADP-ribose deacetylase ymdB None 5.52 18881.0 Escherichia coli (strain K12) GenBank Gene Database U00096 UniProtKB P0A8D6 UniProt Accession YMDB_ECOLI >UPF0189 protein ymdB MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDC PTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPA ISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE >534 bp ATGAAAACGCGTATTCATGTTGTGCAGGGTGATATTACCAAACTGGCCGTTGATGTGATT GTGAATGCGGCTAATCCGTCATTAATGGGAGGCGGCGGCGTCGATGGGGCCATTCATCGC GCAGCGGGTCCGGCCCTGCTGGATGCTTGTTTAAAAGTCAGGCAACAGCAGGGCGATTGC CCTACGGGGCATGCCGTTATTACGCTTGCAGGCGATCTTCCCGCTAAAGCCGTAGTGCAC ACCGTCGGGCCAGTCTGGCGTGGTGGTGAACAAAACGAAGACCAGCTTTTGCAGGATGCC TATCTCAATAGCCTACGACTGGTGGCGGCAAACAGCTATACGTCAGTGGCTTTTCCTGCA ATCAGTACTGGGGTTTATGGTTACCCTCGTGCGGCAGCGGCTGAAATCGCAGTAAAAACC GTTTCAGAATTTATTACCCGTCACGCTTTACCCGAACAGGTATACTTTGTCTGTTATGAT GAAGAAAACGCCCACCTCTACGAAAGACTCCTTACCCAACAAGGAGATGAATGA PF01661 A1pp BE0004638 ADP-ribosylation factor-like protein 3 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown ADP-ribosylation factor-like protein 3 ARL3 Human UniProtKB P36405 UniProt Accession ARL3_HUMAN BE0003189 Beta-lactamase Proteus vulgaris unknown Beta-lactamase Involved in beta-lactamase activity Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefuroxime and cefotaxime blaB Cytoplasmic None 9.35 32992.0 Proteus vulgaris GenBank Gene Database X80128 UniProtKB P52664 UniProt Accession BLAB_PROVU Beta-lactamase precursor Cefuroximase EC 3.5.2.6 >Beta-lactamase MTMFKTTFRQTATIAVSLISLLVSPMLWANTNNTIEEQLSTLEKYSQGRLGVALINTEDN SQITYRGEERFAMASTSKVMAVAAVLKESEKQAGLLDKNITIKKSDLVAYSPITEKHLVT GMSLAQLSAATLQYSDNTAMNKILDYLGGPAKVTQFARSINDVTYRLDRKEPELNTAIHG DPRDTTSPIAMAKSLQALTLGDALGQSQRQQLVTWLKGNTTGDHSIKAGLPKHWIVGDKT GSGDYGTTNDIAVIWPKNHAPLILVVYFTQQEQDAKYRKDIIVKATEIVTKEISNSPQTK >903 bp ATGACTATGTTTAAAACAACATTTCGCCAAACAGCGACGATTGCAGTTTCATTAATATCT CTATTGGTATCTCCAATGCTATGGGCTAACACCAATAATACGATTGAAGAGCAATTAAGT ACGCTTGAAAAATATAGCCAAGGTCGTTTAGGTGTTGCTTTAATCAACACGGAAGATAAT TCACAAATAACATATCGTGGTGAAGAACGTTTTGCGATGGCAAGTACAAGTAAGGTTATG GCTGTTGCGGCAGTTTTAAAAGAGAGTGAAAAACAAGCGGGATTATTAGATAAGAATATT ACAATTAAAAAATCCGACTTAGTTGCTTACAGCCCTATTACAGAAAAACATTTAGTAACA GGAATGTCTTTAGCTCAATTAAGTGCTGCTACGTTGCAATATAGCGATAATACAGCAATG AATAAAATCTTAGATTATTTAGGTGGTCCAGCCAAAGTCACTCAATTTGCACGTTCAATT AATGATGTAACTTATCGCCTAGATCGTAAAGAGCCTGAATTAAATACAGCAATTCATGGT GATCCTCGTGATACGACTTCTCCAATTGCTATGGCTAAAAGCCTTCAAGCATTGACATTA GGTGACGCATTAGGTCAATCTCAACGTCAACAGCTTGTTACTTGGTTAAAAGGCAATACA ACAGGTGATCACAGTATTAAAGCGGGTTTACCAAAACACTGGATTGTTGGGGATAAAACT GGCAGTGGTGATTATGGTACGACTAATGATATCGCCGTTATTTGGCCTAAAAACCATGCA CCATTAATTTTAGTGGTCTATTTCACACAACAAGAACAAGATGCAAAATACCGTAAAGAT ATTATTGTGAAAGCCACAGAGATTGTAACAAAAGAAATATCTAATTCACCTCAAACAAAA TAA PF00144 Beta-lactamase function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides function catalytic activity function beta-lactamase activity process metabolism process drug metabolism process cellular metabolism process antibiotic metabolism process antibiotic catabolism process beta-lactam antibiotic catabolism process response to stimulus process response to abiotic stimulus process response to chemical stimulus process response to drug process response to antibiotic process physiological process BE0003190 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) unknown 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC Involved in catalytic activity Catalyzes the hydrolysis of KDO 8-P to KDO and inorganic phosphate HI_1679 Cytoplasmic None 5.63 19433.0 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GenBank Gene Database L42023 UniProtKB P45314 UniProt Accession KDSC_HAEIN EC 3.1.3.45 KDO 8-P phosphatase >3-deoxy-D-manno-octulosonate 8-phosphate phosphatase MQQKLENIKFVITDVDGVLTDGQLHYDANGEAIKSFHVRDGLGIKMLMDADIQVAVLSGR DSPILRRRIADLGIKLFFLGKLEKETACFDLMKQAGVTAEQTAYIGDDSVDLPAFAACGT SFAVADAPIYVKNAVDHVLSTHGGKGAFREMSDMILQAQGKSSVFDTAQGFLKSVKSMGQ >543 bp ATGCAACAAAAATTAGAAAATATTAAATTTGTCATTACTGATGTAGACGGCGTACTCACT GATGGACAACTTCATTATGATGCCAATGGTGAAGCCATCAAAAGCTTTCATGTACGAGAT GGTTTAGGCATAAAAATGCTGATGGATGCGGATATTCAAGTGGCAGTGCTTTCTGGTCGC GACTCCCCTATTTTACGTCGTCGCATTGCCGATCTTGGTATTAAATTATTCTTTCTTGGC AAACTTGAAAAAGAAACGGCTTGTTTTGATCTCATGAAACAAGCTGGCGTCACCGCCGAG CAAACCGCTTATATTGGCGATGATAGCGTAGATCTCCCCGCCTTTGCAGCGTGTGGAACT TCTTTTGCTGTGGCTGATGCCCCTATTTATGTGAAAAATGCTGTTGATCATGTACTTTCC ACCCATGGCGGCAAAGGCGCATTCCGTGAAATGTCCGATATGATTTTACAGGCACAGGGA AAATCTTCTGTGTTTGATACCGCCCAAGGTTTCCTAAAATCAGTGAAAAGTATGGGGCAG TAA PF00702 Hydrolase function hydrolase activity function 3-deoxy-manno-octulosonate-8-phosphatase activity function ion binding function hydrolase activity, acting on ester bonds function phosphoric ester hydrolase activity function phosphoric monoester hydrolase activity function binding function metal ion binding function magnesium ion binding function catalytic activity process polysaccharide biosynthesis process lipopolysaccharide biosynthesis process macromolecule metabolism process macromolecule biosynthesis process physiological process process carbohydrate biosynthesis process metabolism BE0003191 Lethal(3)malignant brain tumor-like protein 1 Human unknown Lethal(3)malignant brain tumor-like protein 1 Involved in transcription factor activity Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis L3MBTL1 20q13.12 Nucleus None 6.04 85917.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:15905 GenAtlas L3MBTL GenBank Gene Database U89358 UniProtKB Q9Y468 UniProt Accession LMBL1_HUMAN H-L(3)MBT H-l(3)mbt protein L(3)mbt protein homolog L(3)mbt-like L3MBTL1 >Lethal(3)malignant brain tumor-like protein MRRREGHGTDSEMGQGPVRESQSSDPPALQFRISEYKPLNMAGVEQPPSPELRQEGVTEY EDGGAPAGDGEAGPQQAEDHPQNPPEDPNQDPPEDDSTCQCQACGPHQAAGPDLGSSNDG CPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEG QPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKL GMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTG HKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPS LVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPD NFCWEKYLEETGASAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIK IHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLP HTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASAR KKNLSGFSPRKKPRHHGRIGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSAHPDRSLSV CWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGK TLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY >2319 bp ATGAGGCGAAGAGAGGGCCATGGCACCGACTCCGAGATGGGTCAAGGACCCGTACGGGAG TCGCAATCCTCAGACCCTCCCGCGCTCCAGTTCCGGATAAGCGAGTATAAGCCGCTGAAC ATGGCGGGAGTGGAGCAGCCCCCGAGCCCCGAGCTGCGGCAGGAAGGCGTGACCGAATAC GAAGATGGCGGGGCCCCGGCGGGAGATGGCGAGGCGGGCCCCCAACAGGCGGAGGACCAC CCCCAGAATCCTCCAGAAGATCCCAATCAGGACCCCCCAGAGGATGATAGCACCTGTCAG TGCCAGGCGTGCGGGCCTCACCAAGCCGCGGGTCCAGATCTTGGTTCCTCTAATGATGGC TGCCCTCAGCTGTTCCAGGAGCGGTCAGTCATAGTGGAGAACTCCTCAGGCTCTACCAGC GCTTCTGAGCTCCTCAAACCCATGAAGAAGAGGAAGCGCAGGGAATACCAGAGCCCATCA GAGGAGGAGTCGGAGCCAGAGGCCATGGAGAAGCAAGAAGAAGGAAAGGACCCAGAGGGA CAACCCACTGCTAGCACCCCAGAGAGTGAGGAGTGGAGCAGCAGCCAGCCTGCAACAGGT GAGAAGAAGGAATGCTGGTCGTGGGAGTCCTACCTAGAGGAGCAGAAGGCCATTACTGCT CCAGTCAGCCTCTTCCAGGACTCCCAGGCAGTCACTCACAACAAGAATGGCTTCAAACTG GGCATGAAGTTGGAAGGCATTGACCCTCAACACCCGTCCATGTACTTCATCCTCACCGTG GCTGAGGTATGTGGCTATCGCCTACGCCTGCACTTTGATGGGTATTCTGAGTGCCATGAC TTCTGGGTCAATGCCAACTCCCCTGACATTCACCCTGCTGGCTGGTTCGAGAAGACGGGC CACAAGCTGCAGCTTCCCAAAGGTTACAAGGAGGAGGAGTTCAGCTGGAGCCAGTACATG TGCAGCACAAGAGCTCAGGCTGCCCCCAAGCACATGTTTGTGAGCCAGAGCCACAGTCCC CCACCCTTGGGCTTCCAGGTGGGCATGAAGCTGGAGGCTGTTGACCGCATGAACCCGTCC CTTGTCTGCGTGGCCAGTGTGACCGATGTGGTGGACAGCCGCTTCCTGGTGCACTTTGAC AACTGGGATGATACTTATGACTACTGGTGTGATCCCAGCAGCCCCTACATCCACCCAGTG GGCTGGTGCCAGAAGCAAGGAAAGCCCCTCACCCCTCCACAAGACTACCCAGACCCTGAT AACTTCTGTTGGGAGAAATATCTGGAAGAAACTGGGGCCTCTGCTGTCCCCACCTGGGCC TTCAAGGTGCGACCCCCTCACAGCTTCCTGGTCAATATGAAGCTGGAGGCTGTGGACCGC AGGAACCCAGCCCTGATTCGCGTGGCCAGCGTGGAGGATGTGGAGGACCATCGGATAAAG ATCCACTTTGATGGCTGGAGTCATGGCTATGATTTCTGGATCGACGCTGATCACCCAGAC ATCCACCCTGCCGGCTGGTGCTCCAAGACAGGACATCCCCTGCAGCCTCCTCTCGGACCC AGAGAGCCCAGCTCTGCCTCCCCTGGGGGCTGTCCCCCTCTCAGCTATAGGAGCCTGCCC CACACTAGGACCTCCAAATACAGCTTTCACCACCGGAAGTGCCCCACTCCTGGTTGCGAC GGCTCTGGCCATGTCACAGGCAAGTTCACAGCTCACCATTGCCTCTCAGGCTGCCCACTG GCTGAGAGGAACCAGAGCCGGCTGAAAGCGGAGCTGTCTGACCCGGAGGCCTCAGCCCGC AAGAAGAACCTCTCAGGCTTCTCCCCAAGGAAGAAGCCTCGCCATCACGGCCGAATTGGA CGCCCTCCGAAGTATCGAAAGATTCCGCAGGAAGATTTCCAGACCCTCACGCCCGATGTC GTGCACCAGTCCCTCTTCATGTCAGCCCTGTCGGCCCACCCTGACCGCTCACTCTCAGTG TGCTGGGAGCAGCACTGCAAGCTCCTGCCAGGAGTAGCGGGCATCTCAGCCTCGACAGTC GCCAAGTGGACCATCGATGAGGTCTTCGGCTTTGTTCAGACCCTGACAGGTTGTGAGGAC CAAGCACGCCTCTTCAAAGACGAGGCAAGAATAGTCAGAGTGACCCATGTATCTGGGAAG ACTCTAGTCTGGACTGTGGCCCAGCTTGGGGACCTTGTGTGCTCAGATCATCTTCAGGAA GGAAAAGGCATCCTGGAGACAGGAGTCCATTCACTCCTCTGCTCTCTACCCACTCATTTG CTTGCCAAACTTAGCTTTGCCAGTGATAGTCAATATTAA PF02820 MBT PF01530 zf-C2HC component organelle component membrane-bound organelle component intracellular membrane-bound organelle component nucleus function transcription factor activity function DNA binding function binding function nucleic acid binding process regulation of biological process process regulation of physiological process process regulation of metabolism process regulation of cellular metabolism process regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism process regulation of transcription process regulation of transcription, DNA-dependent BE0002180 Cholinesterase Human unknown Cholinesterase Lipid transport and metabolism An acylcholine + H(2)O = choline + a carboxylate BCHE 3q26.1-q26.2 Cytoplasmic None 7.47 68419.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:983 GenAtlas BCHE GeneCards BCHE GenBank Gene Database M32391 GenBank Protein Database 1311630 UniProtKB P06276 UniProt Accession CHLE_HUMAN Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Cholinesterase precursor EC 3.1.1.8 Pseudocholinesterase >Cholinesterase MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV GL >1809 bp ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG GGTCTCTAA PF00135 COesterase PF08674 AChE_tetra function catalytic activity function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity BE0003192 Ribonuclease Z Bacillus subtilis (strain 168) unknown Ribonuclease Z Involved in hydrolase activity Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3' trailer from precursor tRNA rnz None 6.19 34023.0 Bacillus subtilis (strain 168) GenBank Gene Database D84432 UniProtKB P54548 UniProt Accession RNZ_BACSU EC 3.1.26.11 RNase Z tRNA 3 endonuclease tRNase Z >Ribonuclease Z MELLFLGTGAGIPAKARNVTSVALKLLEERRSVWLFDCGEATQHQILHTTIKPRKIEKIF ITHMHGDHVYGLPGLLGSRSFQGGEDELTVYGPKGIKAFIETSLAVTKTHLTYPLAIQEI EEGIVFEDDQFIVTAVSVIHGVEAFGYRVQEKDVPGSLKADVLKEMNIPPGPVYQKIKKG ETVTLEDGRIINGNDFLEPPKKGRSVVFSGDTRVSDKLKELARDCDVLVHEATFAKEDRK LAYDYYHSTTEQAAVTAKEARAKQLILTHISARYQGDASLELQKEAVDVFPNSVAAYDFL EVNVPRG >924 bp GTGGAATTACTTTTTTTAGGGACGGGAGCCGGCATCCCCGCCAAGGCGAGAAATGTAACG TCGGTGGCATTAAAATTGCTTGAAGAAAGGCGTTCGGTATGGCTTTTTGACTGCGGGGAA GCCACACAGCATCAAATTTTACATACAACGATTAAACCTCGTAAAATAGAGAAAATCTTT ATTACACACATGCACGGCGATCATGTATACGGACTTCCGGGGCTTCTGGGGAGCCGTTCC TTTCAAGGCGGAGAGGACGAGCTGACAGTGTACGGACCTAAAGGGATCAAGGCGTTTATT GAAACAAGCCTTGCCGTCACGAAAACCCATTTGACATATCCGCTTGCGATCCAGGAAATT GAAGAAGGAATCGTGTTTGAGGACGATCAGTTTATTGTCACAGCGGTATCTGTTATTCAT GGAGTGGAAGCCTTCGGGTACCGTGTGCAGGAAAAAGACGTACCGGGTTCCTTGAAGGCT GACGTATTAAAAGAAATGAACATCCCGCCCGGACCTGTATATCAGAAAATCAAAAAAGGC GAAACGGTAACGCTTGAAGACGGACGAATCATCAATGGGAATGATTTTCTGGAGCCTCCT AAAAAGGGAAGATCTGTTGTGTTCTCCGGTGATACGAGAGTAAGTGACAAACTAAAAGAG CTTGCGAGGGATTGTGATGTGCTTGTTCATGAAGCAACCTTTGCTAAGGAAGACCGTAAA CTTGCTTATGATTATTATCACAGTACAACGGAACAAGCGGCTGTAACAGCGAAAGAAGCA AGAGCGAAGCAGCTCATTTTAACCCATATCAGCGCAAGATATCAGGGAGATGCTTCTTTG GAGCTTCAAAAAGAAGCGGTTGACGTTTTCCCCAATAGCGTGGCGGCATATGATTTCTTA GAGGTAAACGTCCCGCGAGGCTGA PF00753 Lactamase_B BE0004641 Peroxiredoxin-6 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Peroxiredoxin-6 PRDX6 Human UniProtKB P30041 UniProt Accession PRDX6_HUMAN BE0003193 Hypothetical gliding protein Thermus thermophilus unknown Hypothetical gliding protein mglB None 4.7 17775.0 Thermus thermophilus GenBank Gene Database L09121 UniProtKB Q9X9L0 UniProt Accession Q9X9L0_THETH >Hypothetical gliding protein MVEPSLVLYGAPYERAVEVLEETLRETGARYALLIDRKGFVLAHKEALWAPKPPPLDTLA TLVAGNAAATQALAKLLGEARFQEEVHQGERMGLYVDEAGEHALLVLVFDETAPLGKVKL HGKRAAEALARIAEEALANPPRLALDTEYREGAEALLDDLLRN >492 bp ATGGTGGAGCCTTCCCTGGTCCTTTACGGCGCCCCCTACGAGCGGGCCGTGGAGGTCCTC GAGGAGACCCTAAGGGAAACGGGTGCCCGCTACGCCCTCCTCATTGACCGCAAGGGCTTC GTCCTCGCCCACAAGGAGGCCCTCTGGGCCCCCAAGCCTCCCCCCCTGGACACCCTCGCC ACCCTGGTGGCGGGGAACGCCGCCGCCACCCAGGCCCTGGCCAAGCTCCTGGGCGAAGCC CGCTTCCAAGAGGAGGTCCACCAGGGGGAGAGGATGGGCCTCTACGTGGACGAGGCCGGG GAGCACGCCCTCCTCGTCCTCGTCTTTGACGAGACCGCGCCCCTCGGCAAGGTGAAGCTC CACGGCAAGCGGGCCGCGGAGGCCCTCGCCCGCATCGCCGAGGAGGCCCTGGCCAATCCG CCCCGCCTCGCCCTGGACACGGAGTACCGGGAAGGGGCGGAAGCCCTCCTGGACGACCTC CTCCGCAACTAA PF03259 Robl_LC7 BE0003194 Prolyl endopeptidase Pep Myxococcus xanthus unknown Prolyl endopeptidase Pep Involved in prolyl oligopeptidase activity pep Cytoplasmic None 7.04 76848.0 Myxococcus xanthus GenBank Gene Database AF127082 UniProtKB Q9X5N2 UniProt Accession Q9X5N2_MYXXA >Prolyl endopeptidase Pep MSYPATRAEQVVDTLHGVQVADPYRWLEDEKAPEVQTWMTAQNAHAREALAKFPGREALA ARFKELFYTDSVSTPSRRNGRFFYVRTHKDKEKAILYWRQGESGQEKVLLDPNGWSKDGT VSLGTWAVSWDGKKVAFAQKPNAADEAVLHVIDVDSGEWSKVDVIEGGKYATPKWTPDSK GFYYEWLPTDPSIKVDERPGYTTIRYHTLGTEPSKDTVVHERTGDPTTFLQSDLSRDGKY LFVYILRGWSENDVYWKRPGEKDFRLLVKGVGAKYEVHAWKDRFYVLTDEGAPRQRVFEV DPAKPARASWKEIVPEDSSASLLSVSIVGGHLSLEYLKDATSEVRVATLKGKPVRTVQLP GVGAASNLMGLEDLDDAYYVFTSFTTPRQIYKTSVSTGKSELWAKVDVPMNPEQYQVEQV FYASKDGTKVPMFVVHRKDLKRDGNAPTLLYGYGGFNVNMEANFRSSILPWLDAGGVYAV ANLRGGGEYGKAWHDAGRLDKKQNVFDDFHAAAEYLVQQKYTQPKRLAIYGGSNGGLLVG AAMTQRPELYGAVVCAVPLLDMVRYHLFGSGRTWIPEYGTAEKPEDFKTLHAYSPYHHVR PDVRYPALLMMAADHDDRVDPMHARKFVAAVQNSPGNPATALLRIEANAGHGGADQVAKA IESSVDLYSFLFQVLDVQGAQGGVAAQGR >2070 bp ATGTCCTACCCGGCGACCCGGGCGGAGCAGGTTGTCGACACGTTGCACGGCGTCCAGGTA GCGGACCCGTATCGCTGGCTCGAGGACGAGAAGGCCCCCGAGGTCCAGACGTGGATGACG GCGCAGAACGCGCACGCCCGCGAAGCGCTGGCGAAGTTCCCCGGCCGTGAGGCCCTGGCC GCGCGCTTCAAGGAGCTGTTCTACACCGACTCCGTCTCCACCCCGTCGCGCCGCAACGGG CGCTTCTTCTACGTCCGCACCCACAAGGACAAGGAGAAGGCCATCCTCTACTGGCGCCAG GGGGAGAGCGGGCAGGAGAAGGTGCTGTTGGATCCGAACGGCTGGAGCAAGGACGGCACC GTGTCCCTGGGGACGTGGGCCGTGTCCTGGGACGGCAAGAAGGTGGCCTTCGCCCAGAAG CCCAACGCCGCGGATGAGGCGGTGCTGCACGTCATCGACGTGGACTCTGGCGAGTGGTCC AAGGTGGACGTCATCGAGGGCGGCAAGTACGCCACGCCCAAGTGGACGCCCGACAGCAAG GGCTTCTATTACGAGTGGCTGCCCACGGACCCGTCCATCAAGGTGGACGAGCGCCCCGGC TACACCACCATCCGCTACCACACGCTGGGCACGGAGCCGTCGAAGGACACCGTGGTGCAC GAGCGCACCGGCGACCCGACGACGTTCCTCCAGAGCGACCTGAGCCGCGACGGCAAGTAC CTGTTCGTCTACATCCTCCGCGGCTGGAGCGAGAACGACGTCTACTGGAAGCGGCCGGGT GAGAAGGACTTCCGCCTGCTGGTGAAGGGCGTGGGCGCCAAGTACGAGGTGCACGCCTGG AAGGACCGCTTCTACGTCCTCACCGACGAGGGCGCCCCGCGCCAGCGCGTCTTCGAGGTG GATCCGGCGAAGCCGGCCCGCGCGTCGTGGAAGGAGATTGTCCCCGAGGACTCGTCCGCG TCCCTGCTGTCCGTCAGCATCGTCGGCGGGCACCTGTCGCTGGAGTACCTCAAGGACGCG ACGTCCGAGGTGCGCGTGGCCACGCTGAAGGGCAAGCCGGTGCGCACGGTGCAGCTGCCG GGCGTGGGCGCGGCGTCCAACCTGATGGGGCTGGAGGACCTGGATGACGCCTACTACGTC TTCACGTCCTTCACCACGCCCCGTCAAATCTACAAGACGTCCGTCAGCACCGGGAAGTCT GAGCTCTGGGCCAAGGTGGACGTGCCCATGAACCCGGAGCAGTACCAGGTCGAGCAGGTC TTCTACGCGTCCAAGGACGGGACGAAGGTGCCCATGTTCGTGGTGCACCGCAAGGACCTG AAGCGTGACGGCAACGCGCCCACGCTGCTCTACGGCTACGGCGGCTTCAACGTGAACATG GAGGCCAACTTCCGCTCGAGCATCCTGCCCTGGCTGGACGCGGGCGGCGTGTACGCGGTG GCCAACCTGCGCGGCGGCGGCGAGTACGGCAAGGCCTGGCACGACGCCGGCCGCCTGGAC AAGAAGCAGAACGTCTTCGACGACTTCCACGCGGCGGCCGAGTACTTGGTCCAGCAGAAG TACACGCAGCCCAAGCGGCTGGCCATCTACGGCGGCAGCAACGGCGGCCTGCTGGTGGGC GCGGCCATGACGCAGCGGCCGGAGCTGTACGGCGCGGTGGTGTGCGCGGTGCCCCTGCTG GACATGGTGCGCTACCACCTCTTCGGCAGCGGCCGGACCTGGATTCCGGAGTACGGCACG GCGGAGAAGCCCGAGGACTTCAAGACGCTGCACGCCTACTCGCCCTACCACCACGTGCGG CCGGACGTGCGCTACCCCGCGCTGCTGATGATGGCGGCGGACCACGACGACCGGGTGGAC CCCATGCACGCCCGCAAGTTCGTGGCGGCGGTGCAGAACTCGCCCGGAAACCCGGCGACG GCCCTGCTGCGCATCGAGGCCAACGCGGGCCACGGTGGCGCGGATCAGGTGGCCAAGGCC ATTGAGTCCAGCGTGGACCTGTATTCGTTCCTGTTCCAAGTCCTGGATGTCCAGGGGGCA CAGGGTGGGGTGGCGGCGCAGGGCCGCTGA PF00326 Peptidase_S9 PF02897 Peptidase_S9_N function prolyl oligopeptidase activity function hydrolase activity function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function serine-type peptidase activity function catalytic activity process metabolism process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process BE0004481 Pulmonary surfactant-associated protein A1 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Pulmonary surfactant-associated protein A1 SFTPA1 Human UniProtKB Q8IWL2 UniProt Accession SFTA1_HUMAN BE0002762 Manganese catalase Lactobacillus plantarum unknown Manganese catalase Involved in oxidoreductase activity 2 H(2)O(2) = O(2) + 2 H(2)O None 4.87 29744.0 Lactobacillus plantarum GenBank Gene Database D87070 UniProtKB P60355 UniProt Accession MCAT_LACPN EC 1.11.1.6 Pseudocatalase >Manganese catalase MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSYLSQGWASTGAEKYKDLLL DTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATTMAGMDPEHSLVHGLNASLNN PNGAAWNAGYVTSSGNLVADMRFNVVRESEARLQVSRLYSMTEDEGVRDMLKFLLARETQ HQLQFMKAQEELEEKYGIIVPGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFT YQENPEAMGGIPHIKPGDPRLHNHQG >801 bp ATGTTCAAACATACAAGAAAACTGCAATACAACGCAAAACCTGATCGTTCAGATCCAATT ATGGCAAGACGCTTACAAGAATCTCTTGGTGGTCAATGGGGAGAAACCACTGGGATGATG TCTTATCTCTCACAAGGTTGGGCGTCAACTGGTGCTGAAAAATATAAAGATTTATTATTA GATACTGGTACAGAAGAAATGGCACACGTTGAAATGATTTCTACAATGATTGGCTACTTA CTTGAAGATGCCCCATTTGGTCCAGAAGATTTAAAAAGAGATCCGTCATTGGCAACTACA ATGGCCGGCATGGACCCAGAACACTCGTTAGTTCACGGTTTAAACGCTAGTTTAAATAAT CCTAATGGTGCTGCTTGGAATGCTGGATATGTGACATCAAGTGGTAATTTAGTTGCTGAT ATGAGATTTAATGTTGTTCGTGAATCTGAAGCCAGATTACAAGTTAGTCGTCTGTACTCA ATGACTGAAGATGAAGGTGTGCGTGACATGCTTAAATTCCTATTAGCTCGTGAAACTCAA CATCAATTACAATTTATGAAAGCTCAAGAAGAATTAGAAGAAAAATATGGGATAATTGTA CCTGGCGATATGAAAGAGATCGAGCATAGTGAATTTAGTCATGTACTTATGAATTTCTCA GATGGTGATGGATCAAAAGCATTTGAAGGACAAGTTGCTAAAGATGGTGAAAAATTCACC TATCAAGAAAACCCAGAAGCAATGGGTGGTATTCCACATATTAAACCGGGTGATCCTAGA TTACACAACCACCAAGGTTAG PF05067 Mn_catalase BE0002709 Chorismate mutase AroH Thermus thermophilus unknown Chorismate mutase AroH aroG None 5.68 13650.0 Thermus thermophilus GenBank Gene Database AY196198 UniProtKB Q84FH6 UniProt Accession AROH_THETH EC 5.4.99.5 >Chorismate mutase MVRGIRGAITVEEDTPEAIHQATRELLLKMLEANGIQSYEELAAVIFTVTEDLTSAFPAE AARQIGMHRVPLLSAREVPVPGSLPRVIRVLALWNTDTPQDRVRHVYLREAVRLRPDLES AQ >369 bp ATGGTCCGGGGCATCCGCGGCGCCATCACCGTGGAAGAGGACACCCCGGAGGCCATCCAC CAGGCCACCCGGGAACTCCTCCTGAAGATGCTGGAGGCGAACGGCATCCAGAGCTACGAG GAGCTCGCCGCCGTCATCTTCACCGTCACCGAGGACCTCACCTCCGCCTTCCCCGCCGAG GCCGCGCGGCAGATCGGCATGCACCGGGTGCCCCTCCTCTCCGCCCGGGAGGTGCCGGTG CCGGGAAGCCTCCCCCGGGTGATCCGCGTCCTCGCCCTCTGGAACACGGACACCCCCCAG GACCGGGTGCGCCACGTCTACCTCAGGGAGGCGGTGCGGCTCCGGCCCGACCTGGAAAGC GCCCAGTAG PF07736 CM_1 function isomerase activity function intramolecular transferase activity function chorismate mutase activity function catalytic activity process amino acid and derivative metabolism process amino acid biosynthesis process aromatic amino acid family biosynthesis process physiological process process metabolism process cellular metabolism process amino acid metabolism BE0002707 Putative cytochrome P450 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) unknown Putative cytochrome P450 Involved in monooxygenase activity SCO1207 None 5.02 44355.0 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) GenBank Gene Database AL939108 UniProtKB Q9FCA6 UniProt Accession Q9FCA6_STRCO >Putative cytochrome P450 MTEETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLVTRHDDV RLVTNDPRFGREAVMDRQVTRLAPHFIPARGAVGFLDPPDHTRLRRSVAAAFTARGVERV RERSRGMLDELVDAMLRAGPPADLTEAVLSPFPIAVICELMGVPATDRHSMHTWTQLILS SSHGAEVSERAKNEMNAYFSDLIGLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQ IGGEAVTNNSGQMFHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALED VEIKGVRIRAGDAVYVSYLAANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYCPGGMLAR LESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEALPVTW >1215 bp ATGACTGAAGAAACGATTTCCCAGGCCGTGCCACCCGTCCGGGACTGGCCGGCCGTCGAC CTTCCCGGCAGCGACTTCGACCCGGTGCTGACCGAGCTGATGCGCGAGGGTCCCGTCACC CGGATCTCGCTGCCCAACGGCGAGGGCTGGGCCTGGCTCGTGACCCGCCACGACGACGTC CGCCTGGTCACCAACGACCCCCGGTTCGGGCGCGAGGCCGTCATGGACCGCCAGGTCACC CGGCTGGCCCCGCACTTCATCCCGGCGCGCGGCGCGGTGGGCTTCCTGGACCCGCCCGAC CACACCCGGCTGCGCCGCTCGGTGGCCGCGGCCTTCACCGCGCGGGGCGTGGAGCGGGTG CGCGAGCGGTCCCGGGGCATGCTCGACGAGCTGGTCGACGCCATGCTGAGGGCCGGTCCG CCCGCCGACCTCACCGAGGCGGTGCTGAGCCCGTTCCCCATCGCGGTGATCTGCGAGCTG ATGGGTGTGCCGGCCACCGACCGGCACTCCATGCACACCTGGACCCAGCTGATCCTGTCC TCCTCGCACGGCGCCGAGGTCAGCGAGCGGGCCAAGAACGAGATGAACGCCTACTTCTCG GATCTCATCGGGCTCCGCTCCGACAGCGCGGGCGAGGACGTCACCTCGCTGCTGGGTGCC GCCGTGGGGCGGGACGAGATCACGCTGTCGGAGGCCGTCGGGCTCGCGGTGCTGCTCCAG ATCGGCGGCGAGGCGGTCACCAACAACAGCGGGCAGATGTTCCACCTGCTGCTGAGCCGC CCGGAGCTGGCCGAACGCCTGCGCTCCGAGCCGGAGATCCGCCCCCGGGCCATCGACGAG CTGCTGCGCTGGATCCCGCACCGCAACGCCGTGGGGCTGTCCCGGATCGCCCTGGAGGAC GTGGAGATCAAGGGGGTGCGGATCCGCGCGGGCGACGCCGTCTACGTCTCGTACCTGGCG GCCAACCGCGACCCGGAGGTGTTCCCCGACCCGGACCGCATCGACTTCGAGCGCTCCCCC AACCCGCACGTCTCCTTCGGCTTCGGCCCGCACTACTGTCCCGGCGGCATGCTGGCGCGG CTGGAGTCGGAGCTGCTCGTCGACGCGGTCCTGGACCGCGTGCCGGGGCTGAAGCTCGCG GTGGCGCCGGAGGACGTGCCCTTCAAGAAGGGTGCGCTGATCCGCGGGCCCGAGGCCCTG CCGGTGACGTGGTGA PF00067 p450 function tetrapyrrole binding function catalytic activity function heme binding function monooxygenase activity function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0004634 Interferon-inducible GTPase 5 Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Interferon-inducible GTPase 5 IRGC Human UniProtKB Q6NXR0 UniProt Accession IIGP5_HUMAN BE0001038 Chymase Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Chymase Involved in protease activity Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion CMA1 14q11.2 Secreted protein. Cytoplasmic granule. Note=Mast cell granules None 9.71 27325.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:2097 GenAtlas CMA1 GeneCards CMA1 GenBank Gene Database M64269 GenBank Protein Database 180542 UniProtKB P23946 UniProt Accession CMA1_HUMAN Chymase precursor EC 3.4.21.39 Mast cell protease I >Chymase precursor MLLLPLPLLLFLLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNF VLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKA SLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRD FDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWI NQILQAN >744 bp ATGCTGCTTCTTCCTCTCCCCCTGCTGCTCTTTCTCTTGTGCTCCAGAGCTGAAGCTGGG GAGATCATCGGGGGCACAGAATGCAAGCCACATTCCCGCCCCTACATGGCCTACCTGGAA ATTGTAACTTCCAACGGTCCCTCAAAATTTTGTGGTGGTTTCCTTATAAGACGGAACTTT GTGCTGACGGCTGCTCATTGTGCAGGAAGGTCTATAACAGTCACCCTTGGAGCCCATAAC ATAACAGAGGAAGAAGACACATGGCAGAAGCTTGAGGTTATAAAGCAATTCCGTCATCCA AAATATAACACTTCTACTCTTCACCACGATATCATGTTACTAAAGTTGAAGGAGAAAGCC AGCCTGACCCTGGCTGTGGGGACACTCCCCTTCCCATCACAATTCAACTTTGTCCCACCT GGGAGAATGTGCCGGGTGGCTGGCTGGGGAAGAACAGGTGTGTTGAAGCCGGGCTCAGAC ACTCTGCAAGAGGTGAAGCTGAGACTCATGGATCCCCAGGCCTGCAGCCACTTCAGAGAC TTTGACCACAATCTTCAGCTGTGTGTGGGCAATCCCAGGAAGACAAAATCTGCATTTAAG GGAGACTCTGGGGGCCCTCTTCTGTGTGCTGGGGTGGCCCAGGGCATCGTATCCTATGGA CGGTCGGATGCAAAGCCCCCTGCTGTCTTCACCCGAATCTCCCATTACCGGCCCTGGATC AACCAGATCCTGCAGGCAAATTAA PF00089 Trypsin function peptidase activity function endopeptidase activity function serine-type endopeptidase activity function catalytic activity function hydrolase activity process macromolecule metabolism process protein metabolism process cellular protein metabolism process proteolysis process physiological process process metabolism BE0000814 Glutathione S-transferase P Human # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Glutathione S-transferase P Involved in glutathione transferase activity Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles GSTP1 11q13 None 5.3 23225.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:4638 GenAtlas GSTP1 GeneCards GSTP1 GenBank Gene Database M24485 GenBank Protein Database 31946 UniProtKB P09211 UniProt Accession GSTP1_HUMAN EC 2.5.1.18 GST class-pi GSTP1-1 >Glutathione S-transferase P PPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDL TLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVK ALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYV GRLSARPKLKAFLASPEYVNLPINGNGKQ >633 bp ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG AACCTCCCCATCAATGGCAACGGGAAACAGTGA PF00043 GST_C PF02798 GST_N function transferase activity function transferase activity, transferring alkyl or aryl (other than methyl) groups function glutathione transferase activity function catalytic activity process metabolism process physiological process BE0002180 Cholinesterase Human unknown Cholinesterase Lipid transport and metabolism An acylcholine + H(2)O = choline + a carboxylate BCHE 3q26.1-q26.2 Cytoplasmic None 7.47 68419.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:983 GenAtlas BCHE GeneCards BCHE GenBank Gene Database M32391 GenBank Protein Database 1311630 UniProtKB P06276 UniProt Accession CHLE_HUMAN Acylcholine acylhydrolase Butyrylcholine esterase Choline esterase II Cholinesterase precursor EC 3.1.1.8 Pseudocholinesterase >Cholinesterase MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV GL >1809 bp ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGTTGGGCA AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG GGTCTCTAA PF00135 COesterase PF08674 AChE_tetra function catalytic activity function hydrolase activity function hydrolase activity, acting on ester bonds function carboxylic ester hydrolase activity function cholinesterase activity unknown unknown "
owl:sameAs	drug:EXPT02154
rdfs:label	"2-(N-Morpholino)-Ethanesulfonic Acid"
rdf:type	drugbank:drugs

All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

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