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Predicate	Value (sorted: default)
rdfs:label	"Thymidine-5'-Triphosphate"
rdf:type	drugbank:drugs
drugbank:description	" experimental This compound belongs to the pyrimidine 2'-deoxyribonucleoside diphosphates. These are pyrimidine nucleotides with a diphosphate group linked to the ribose moiety lacking an hydroxyl group at position 2. Pyrimidine 2'-deoxyribonucleoside Diphosphates Organic Compounds Organooxygen Compounds Carbohydrates and Carbohydrate Conjugates Glycosyl Compounds Organic Pyrophosphates Pyrimidones Organophosphate Esters Organic Phosphoric Acids Hydropyrimidines Tetrahydrofurans Oxolanes Secondary Alcohols Polyamines Ethers organic pyrophosphate pyrimidone organic phosphate phosphoric acid ester hydropyrimidine pyrimidine tetrahydrofuran oxolane secondary alcohol polyamine ether alcohol organonitrogen compound amine logP -0.09 ALOGPS logS -1.8 ALOGPS Water Solubility 7.78e+00 g/l ALOGPS logP -2.1 ChemAxon IUPAC Name {[hydroxy({[hydroxy({[(2S,3R,5R)-3-hydroxy-5-(5-methyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-1-yl)oxolan-2-yl]methoxy})phosphoryl]oxy})phosphoryl]oxy}phosphonic acid ChemAxon Traditional IUPAC Name [hydroxy({hydroxy[(2S,3R,5R)-3-hydroxy-5-(5-methyl-2,4-dioxo-3H-pyrimidin-1-yl)oxolan-2-yl]methoxyphosphoryl}oxy)phosphoryl]oxyphosphonic acid ChemAxon Molecular Weight 482.1683 ChemAxon Monoisotopic Weight 481.989262798 ChemAxon SMILES CC1=CN([C@H]2C[C@@H](O)[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)OP(O)(O)=O)O2)C(=O)NC1=O ChemAxon Molecular Formula C10H17N2O14P3 ChemAxon InChI InChI=1S/C10H17N2O14P3/c1-5-3-12(10(15)11-9(5)14)8-2-6(13)7(24-8)4-23-28(19,20)26-29(21,22)25-27(16,17)18/h3,6-8,13H,2,4H2,1H3,(H,19,20)(H,21,22)(H,11,14,15)(H2,16,17,18)/t6-,7+,8-/m1/s1 ChemAxon InChIKey InChIKey=NHVNXKFIZYSCEB-GJMOJQLCSA-N ChemAxon Polar Surface Area (PSA) 238.69 ChemAxon Refractivity 88.03 ChemAxon Polarizability 36.43 ChemAxon Rotatable Bond Count 8 ChemAxon H Bond Acceptor Count 11 ChemAxon H Bond Donor Count 6 ChemAxon pKa (strongest acidic) 0.9 ChemAxon pKa (strongest basic) -3.2 ChemAxon Physiological Charge -3 ChemAxon Number of Rings 2 ChemAxon Bioavailability 0 ChemAxon ChEBI 18077 PubChem Compound 6324670 PubChem Substance 46508083 PDB TTP BE0002493 Glucose-1-phosphate thymidylyltransferase Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) unknown Glucose-1-phosphate thymidylyltransferase Involved in glucose-1-phosphate thymidylyltransferase activity rmlA None 5.02 32457.0 Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) GenBank Gene Database AE004091 UniProtKB Q9HU22 UniProt Accession Q9HU22_PSEAE Glucose-1-phosphate thymidyltransferase >Glucose-1-phosphate thymidylyltransferase MKRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPQDT PRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIGNDLSALVLGDNLYYGHDFHE LLGSASQRQTGASVFAYHVLDPERYGVVEFDQGGKAISLEEKPLEPKSNYAVTGLYFYDQ QVVDIARDLKPSPRGELEITDVNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIA TLENRQGLKVACPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY >882 bp ATGAAACGCAAGGGCATCATCCTCGCCGGAGGCTCGGGCACCCGCCTGCACCCGGCAACG CTGGCCATCTCCAAGCAGTTGCTGCCGGTGTACGACAAGCCGATGATCTACTACCCGCTC AGTACCCTGATGCTGGCGGGCATCCGCGAGATACTGATCATCTCGACCCCACAGGACACC CCACGCTTCCAGCAGTTGCTGGGCGACGGTTCGAACTGGGGCCTGGACCTGCAATATGCC GTGCAACCGTCGCCGGACGGCCTGGCCCAGGCCTTCCTGATCGGCGAGTCGTTCATCGGC AACGACCTCAGCGCGCTGGTCCTGGGCGACAACCTCTATTACGGCCACGACTTCCACGAG TTGCTCGGCAGCGCTTCGCAGCGCCAGACCGGCGCCAGTGTCTTCGCCTACCACGTGCTG GACCCGGAGCGCTACGGCGTGGTCGAGTTCGACCAGGGCGGCAAGGCCATCAGCCTGGAA GAGAAGCCACTGGAGCCGAAGTCGAACTACGCGGTCACCGGCCTGTATTTCTACGACCAG CAGGTGGTGGACATCGCCAGGGACCTGAAGCCTTCGCCGCGCGGCGAGCTGGAGATCACC GACGTCAACCGCGCCTATCTGGAGCGCGGCCAGCTCAGCGTGGAGATCATGGGCCGCGGC TACGCCTGGCTGGATACCGGCACCCACGATTCGCTGCTCGAGGCCGGCCAGTTCATCGCC ACCCTGGAGAACCGCCAGGGTCTCAAGGTGGCCTGCCCGGAAGAGATCGCCTACCGGCAG AAGTGGATCGACGCCGCGCAACTGGAAAAACTCGCCGCGCCGCTGGCCAAGAACGGCTAC GGCCAATACCTCAAGCGCCTGCTGACCGAGACCGTGTACTGA PF00483 NTP_transferase function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleotidyltransferase activity function glucose-1-phosphate thymidylyltransferase activity function catalytic activity process metabolism process macromolecule metabolism process biosynthesis process macromolecule biosynthesis process carbohydrate biosynthesis process polysaccharide biosynthesis process physiological process process extracellular polysaccharide biosynthesis BE0001912 Glucose-1-phosphate thymidylyltransferase 2 Shigella flexneri # 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 Glucose-1-phosphate thymidylyltransferase 2 Cell wall/membrane/envelope biogenesis Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis rmlA2 None 5.08 32735.0 Shigella flexneri GenBank Gene Database AE005674 GenBank Protein Database 24054349 UniProtKB P61888 UniProt Accession RMLA2_SHIFL dTDP- glucose synthase 2 dTDP-glucose pyrophosphorylase 2 EC 2.7.7.24 >Glucose-1-phosphate thymidylyltransferase 2 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPEDKGY FQRLLGDGSEFGIQLEYAEQPSPDGLAQAFIIGETFLNGEPSCLVLGDNIFFGQGFSPKL RHVAARTEGATVFGYQVMDPERFGVVEFDDNFRAISLEEKPKQPKSNWAVTGLYFYDSKV VEYAKQVKPSERGELEITSINQMYLEAGNLTVELLGRGFAWLDTGTHDSLIEASTFVQTV EKRQGFKIACLEEIAWRNGWLDDEGVKRAASSLAKTGYGQYLLELLRARPRQY >882 bp ATGAAGGGTATTATCCTGGCGGGCGGTTCCGGTACCCGATTGCATCCGATTACGCGCGGC GTATCGAAGCAACTGTTGCCGATTTACGATAAGCCAATGATTTACTATCCGCTGTCGGTG CTGATGCTGGCCGGTATCCGCGAAATTCTCATCATCACTACGCCGGAAGATAAAGGTTAT TTCCAGCGCCTGCTGGGCGATGGTAGTGAGTTCGGTATCCAGCTGGAATATGCCGAACAG CCCAGCCCGGACGGTCTGGCGCAGGCCTTTATCATCGGTGAAACCTTCCTTAATGGTGAA CCTTCTTGTCTGGTGCTGGGCGATAACATCTTCTTCGGTCAGGGCTTCAGTCCGAAGCTG CGTCATGTTGCGGCGCGCACGGAAGGGGCGACGGTTTTTGGCTATCAGGTGATGGACCCG GAACGCTTTGGCGTGGTGGAATTTGACGACAATTTCCGCGCTATCTCGCTTGAAGAAAAG CCAAAACAGCCGAAGTCAAACTGGGCGGTGACCGGGCTTTATTTCTACGACAGTAAAGTC GTGGAGTACGCAAAGCAGGTGAAGCCGTCGGAGCGCGGTGAACTGGAGATTACCTCCATC AACCAGATGTACCTCGAGGCGGGCAACCTGACCGTTGAACTGCTCGGGCGCGGATTTGCC TGGCTGGATACCGGCACTCACGACAGCCTGATTGAGGCCAGCACTTTTGTGCAGACAGTA GAAAAACGCCAGGGCTTTAAGATTGCCTGCCTGGAAGAGATCGCCTGGCGTAACGGCTGG CTCGATGACGAGGGTGTGAAGCGTGCTGCCAGTTCATTAGCGAAAACTGGCTACGGCCAA TATCTGCTGGAGTTACTTCGTGCCCGTCCGCGCCAGTATTGA PF00483 NTP_transferase function catalytic activity function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleotidyltransferase activity function glucose-1-phosphate thymidylyltransferase activity process extracellular polysaccharide biosynthesis process metabolism process macromolecule metabolism process biosynthesis process macromolecule biosynthesis process carbohydrate biosynthesis process polysaccharide biosynthesis process physiological process BE0001811 DNA primase/helicase Enterobacteria phage T7 # 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 DNA primase/helicase Replication, recombination and repair DNA primase synthesizes RNA primers necessary for replication by DNA polymerase. It also functions as an ATP- dependent unwinding protein. Has a 5'->3' helicase activity; 4a also has a DNA primase activity 4 Cytoplasmic None 5.23 62656.0 Enterobacteria phage T7 GenBank Gene Database V01127 GenBank Protein Database 15519 UniProtKB P03692 UniProt Accession PRIM_BPT7 EC 2.7.7.- >DNA primase/helicase MDNSHDSDSVFLYHIPCDNCGSSDGNSLFSDGHTFCYVCEKWTAGNEDTKERASKRKPSG GKPMTYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVS QKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGH GASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANE CHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTL GARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRV RLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDV IILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRP VSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETG WLEPSSYSGEEESHSESTDWSNDTDF >1701 bp ATGGACAATTCGCACGATTCCGATAGTGTATTTCTTTACCACATTCCTTGTGACAACTGT GGGAGTAGTGATGGGAACTCGCTGTTCTCTGACGGACACACGTTCTGCTACGTATGCGAG AAGTGGACTGCTGGTAATGAAGACACTAAAGAGAGGGCTTCAAAACGGAAACCCTCAGGA GGTAAACCAATGACTTACAACGTGTGGAACTTCGGGGAATCCAATGGACGCTACTCCGCG TTAACTGCGAGAGGAATCTCCAAGGAAACCTGTCAGAAGGCTGGCTACTGGATTGCCAAA GTAGACGGTGTGATGTACCAAGTGGCTGACTATCGGGACCAGAACGGCAACATTGTGAGT CAGAAGGTTCGAGATAAAGATAAGAACTTTAAGACCACTGGTAGTCACAAGAGTGACGCT CTGTTCGGGAAGCACTTGTGGAATGGTGGTAAGAAGATTGTCGTTACAGAAGGTGAAATC GACATGCTTACCGTGATGGAACTTCAAGACTGTAAGTATCCTGTAGTGTCGTTGGGTCAC GGTGCCTCTGCCGCTAAGAAGACATGCGCTGCCAACTACGAATACTTTGACCAGTTCGAA CAGATTATCTTAATGTTCGATATGGACGAAGCAGGGCGCAAAGCAGTCGAAGAGGCTGCA CAGGTTCTACCTGCTGGTAAGGTACGAGTGGCAGTTCTTCCGTGTAAGGATGCAAACGAG TGTCACCTAAATGGTCACGACCGTGAAATCATGGAGCAAGTGTGGAATGCTGGTCCTTGG ATTCCTGATGGTGTGGTATCGGCTCTTTCGTTACGTGAACGAATCCGTGAGCACCTATCG TCCGAGGAATCAGTAGGTTTACTTTTCAGTGGCTGCACTGGTATCAACGATAAGACCTTA GGTGCCCGTGGTGGTGAAGTCATTATGGTCACTTCCGGTTCCGGTATGGGTAAGTCAACG TTCGTCCGTCAACAAGCTCTACAATGGGGCACAGCGATGGGCAAGAAGGTAGGCTTAGCG ATGCTTGAGGAGTCCGTTGAGGAGACCGCTGAGGACCTTATAGGTCTACACAACCGTGTC CGACTGAGACAATCCGACTCACTAAAGAGAGAGATTATTGAGAACGGTAAGTTCGACCAA TGGTTCGATGAACTGTTCGGCAACGATACGTTCCATCTATATGACTCATTCGCCGAGGCT GAGACGGATAGACTGCTCGCTAAGCTGGCCTACATGCGCTCAGGCTTGGGCTGTGACGTA ATCATTCTAGACCACATCTCAATCGTCGTATCCGCTTCTGGTGAATCCGATGAGCGTAAG ATGATTGACAACCTGATGACCAAGCTCAAAGGGTTCGCTAAGTCAACTGGGGTGGTGCTG GTCGTAATTTGTCACCTTAAGAACCCAGACAAAGGTAAAGCACATGAGGAAGGTCGCCCC GTTTCTATTACTGACCTACGTGGTTCTGGCGCACTACGCCAACTATCTGATACTATTATT GCCCTTGAGCGTAATCAGCAAGGCGATATGCCTAACCTTGTCCTCGTTCGTATTCTCAAG TGCCGCTTTACTGGTGATACTGGTATCGCTGGCTACATGGAATACAACAAGGAAACCGGA TGGCTTGAACCATCAAGTTACTCAGGGGAAGAAGAGTCACACTCAGAGTCAACAGACTGG TCCAACGACACTGACTTCTGA PF01751 Toprim PF08273 Prim_Zn_Ribbon function purine nucleotide binding function DNA-directed RNA polymerase activity function adenyl nucleotide binding function helicase activity function transferase activity function ATP binding function DNA helicase activity function transferase activity, transferring phosphorus-containing groups function DNA primase activity function binding function nucleic acid binding function catalytic activity function nucleotide binding function nucleotidyltransferase activity process DNA modification process DNA strand elongation process physiological process process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process lagging strand elongation process DNA replication process DNA replication, synthesis of RNA primer process metabolism process DNA-dependent DNA replication process cellular metabolism process DNA metabolism BE0001910 Glucose-1-phosphate thymidylyltransferase Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) # 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 Glucose-1-phosphate thymidylyltransferase Cell wall/membrane/envelope biogenesis Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy- alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars rmlA None 5.75 32454.0 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GenBank Gene Database X56793 GenBank Protein Database 47891 UniProtKB P26393 UniProt Accession RMLA_SALTY dTDP-glucose pyrophosphorylase dTDP-glucose synthase EC 2.7.7.24 Ep >Glucose-1-phosphate thymidylyltransferase MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQD TPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIGHDDCALVLGDNIFYGHDLP KLMEAAVNKESGATVFAYHVNDPERYGVVEFDQKGTAVSLEEKPLQPKSNYAVTGLYFYD NSVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFI ATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMVKGL >879 bp ATGAAAACGCGTAAGGGCATTATTTTAGCGGGGGGCTCCGGCACCCGTCTTTATCCGGTG ACCATGGCGGTAAGTAAGCAATTGCTACCAATTTATGATAAACCGATGATTTACTATCCC CTTTCCACGCTTATGCTGGCAGGCATTCGGGATATCCTGATCATCAGTACGCCACAGGAC ACGCCGCGTTTTCAACAACTGCTGGGAGACGGCAGCCAGTGGGGGCTGAATCTTCAATAT AAAGTACAGCCAAGCCCGGATGGCTTAGCACAGGCGTTTATTATTGGTGAAGAGTTCATT GGTCATGATGATTGTGCATTAGTGCTGGGTGACAATATCTTCTATGGTCATGATTTACCA AAGTTAATGGAAGCTGCCGTTAATAAAGAAAGTGGTGCTACCGTCTTCGCTTATCATGTA AACGATCCGGAGCGCTACGGTGTGGTTGAGTTTGACCAAAAGGGCACAGCCGTTAGTCTG GAAGAAAAACCATTACAACCGAAGAGTAATTACGCGGTAACGGGGCTGTATTTTTATGAT AATAGCGTGGTGGAGATGGCGAAAAATCTTAAGCCTTCCGCTCGCGGTGAGTTAGAAATC ACGGATATTAACCGTATCTATATGGAGCAGGGAAGATTGTCTGTCGCTATGATGGGGCGC GGTTATGCCTGGCTGGATACAGGGACGCATCAGAGTTTGATAGAGGCCAGTAATTTTATT GCAACCATCGAAGAACGCCAGGGGCTAAAAGTGTCCTGCCCGGAAGAGATCGCATTTCGT AAAAATTTTATAAATGCACAACAGGTTATAGAACTGGCCGGGCCATTATCAAAAAATGAT TATGGCAAATATTTGCTGAAGATGGTGAAAGGTTTATAA PF00483 NTP_transferase function transferase activity function transferase activity, transferring phosphorus-containing groups function nucleotidyltransferase activity function glucose-1-phosphate thymidylyltransferase activity function catalytic activity process metabolism process macromolecule metabolism process biosynthesis process macromolecule biosynthesis process carbohydrate biosynthesis process polysaccharide biosynthesis process physiological process process extracellular polysaccharide biosynthesis BE0004639 Thymidine kinase 2, mitochondrial 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 Thymidine kinase 2, mitochondrial TK2 Human UniProtKB O00142 UniProt Accession KITM_HUMAN BE0001883 Thymidine kinase Ureaplasma parvum serovar 3 (strain ATCC 700970) # 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 Thymidine kinase Nucleotide transport and metabolism ATP + thymidine = ADP + thymidine 5'- phosphate tdk Cytoplasm (Potential) None 8.92 25367.0 Ureaplasma parvum serovar 3 (strain ATCC 700970) GenBank Gene Database AE002158 GenBank Protein Database 6899605 UniProtKB Q9PPP5 UniProt Accession KITH_UREPA EC 2.7.1.21 >Thymidine kinase MAKVNAFSKKIGWIELITGPMFAGKTAELIRRLHRLEYADVKYLVFKPKIDTRSIRNIQS RTGTSLPSVEVESAPEILNYIMSNSFNDETKVIGIDEVQFFDDRICEVANILAENGFVVI ISGLDKNFKGEPFGPIAKLFTYADKITKLTAICNECGAEATHSLRKIDGKHADYNDDIVK IGCQEFYSAVCRHHHKVPNRPYLNSNSEEFIKFFKNKKRNKNI >672 bp TTATATATTTTTATTTCGTTTTTTATTTTTAAAAAATTTAATAAATTCCTCAGAATTACT ATTTAAATAAGGACGATTAGGTACCTTATGATGATGACGACAAACAGCAGAATAGAATTC CTGACAGCCAATTTTAACAATATCATCATTATAGTCAGCGTGTTTACCATCAATCTTACG CAATGAATGCGTTGCTTCAGCGCCACACTCATTACATATCGCTGTTAGTTTTGTAATTTT ATCAGCATAAGTAAAAAGTTTAGCAATTGGACCAAAAGGCTCGCCTTTAAAATTTTTATC TAATCCTGAAATAATAACAACAAAACCATTTTCTGCTAAAATATTTGCAACTTCACAAAT CCGATCATCAAAAAATTGAACCTCATCAATGCCAATAACTTTTGTTTCATCATTAAAACT GTTTGACATAATATAATTTAAAATTTCTGGTGCGCTTTCTACTTCAACTGATGGTAAAGA CGTTCCTGTTCGTGATTGGATATTTCTAATAGATCTAGTATCAATTTTAGGTTTAAAAAC CAAATATTTAACATCTGCATATTCTAAACGATGTAAGCGACGAATTAACTCTGCTGTTTT TCCAGCAAACATTGGGCCAGTAATTAATTCTATTCATCCTATTTTTTTTGAAAATGCATT CACTTTAGCCAT PF00265 TK function ATP binding function transferase activity, transferring phosphorus-containing groups function kinase activity function nucleobase, nucleoside, nucleotide kinase activity function nucleoside kinase activity function binding function deoxynucleoside kinase activity function catalytic activity function thymidine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function transferase activity BE0001782 Ribonucleoside-diphosphate reductase 2 subunit alpha Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) # 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 Ribonucleoside-diphosphate reductase 2 subunit alpha Nucleotide transport and metabolism Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide nrdE None 7.04 80588.0 Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GenBank Gene Database X73226 GenBank Protein Database 1050838 UniProtKB Q08698 UniProt Accession RIR3_SALTY EC 1.17.4.1 R1E protein Ribonucleotide reductase 2 >Ribonucleoside-diphosphate reductase 2 alpha subunit MATTTPERVMQETMDYHALNAMLNLYDKAGHIQFDKDQQAIDAFFATHVRPHSVTFASQH ERLGTLVREGYYDDAVLARYDRAFVLRLFEHAHASGFRFQTFLGAWKFYTSYTLKTFDGK RYLEHFEDRVTMVALTLAQGDETLATQLTDEMLSGRFQPATPTFLNCGKQQRGELVSCFL LRIEDNMESIGRAVNSALQLSKRGGGVAFLLSNLREAGAPIKRIENQSSGVIPVMKMLED AFSYANQLGARQGAGAVYLHAHHPDILRFLDTKRENADEKIRIKTLSLGVVIPDITFRLA KENAQMALFSPYDIQRRYGKPFGDIAISERYDELIADPHVRKTYINARDFFQTLAEIQFE SGYPYIMFEDTVNRANPIAGRINMSNLCSEILQVNSASRYDDNLDYTHIGHDISCNLGSL NIAHVMDSPDIGRTVETAIRGLTAVSDMSHIRSVPSIAAGNAASHAIGLGQMNLHGYLAR EGIAYGSPEALDFTNLYFYTITWHAVHTSMRLARERGKTFAGFAQSRYASGDYFTQYLQD DWQPKTAKVRALFARSGITLPTREMWLKLRDDVMRYGIYNQNLQAVPPTGSISYINHATS SIHPIVAKIEIRKEGKTGRVYYPAPFMTNENLDMYQDAYDIGPEKIIDTYAEATRHVDQG LSLTLFFPDTATTRDINKAQIYAWRKGIKSLYYIRLRQLALEGTEIEGCVSCAL >2145 bp TTGGCAACAACTACCCCGGAGCGCGTAATGCAGGAAACCATGGATTACCACGCCCTGAAC GCGATGCTGAATCTTTACGATAAAGCAGGCCATATTCAGTTCGACAAGGACCAGCAGGCG ATCGACGCCTTCTTTGCCACCCACGTCCGCCCGCATTCCGTGACGTTTGCCAGCCAGCAT GAACGTCTGGGGACGCTGGTTCGGGAAGGGTATTACGATGACGCCGTCCTCGCGCGTTAC GACCGCGCCTTCGTCCTTCGCCTGTTCGAGCACGCCCATGCCAGCGGCTTTCGCTTCCAG ACGTTTCTTGGCGCCTGGAAGTTCTATACCAGTTACACGCTGAAAACCTTCGACGGCAAA CGTTATCTGGAACACTTTGAAGATCGGGTGACAATGGTGGCGTTGACGCTGGCGCAGGGT GACGAAACGCTGGCCACCCAACTGACCGATGAAATGCTTTCTGGTCGCTTTCAGCCCGCT ACCCCGACTTTTTTAAATTGCGGCAAACAGCAGCGTGGGGAACTGGTCTCCTGCTTCCTG CTCCGTATCGAAGACAACATGGAGTCGATCGGGCGGGCGGTGAATTCGGCGCTGCAACTC TCCAAACGCGGCGGCGGCGTCGCGTTTTTACTCTCCAATCTGCGCGAGGCGGGCGCGCCG ATCAAACGCATTGAGAATCAGTCTTCCGGCGTGATCCCGGTGATGAAAATGCTGGAAGAC GCGTTTTCGTATGCCAACCAACTTGGCGCGCGCCAGGGGGCCGGCGCGGTTTATCTCCAT GCGCACCATCCGGATATTCTGCGTTTTCTGGATACCAAACGAGAAAACGCTGACGAAAAA ATCCGGATCAAAACGCTCTCTCTCGGCGTGGTGATCCCGGATATCACCTTCCGGCTGGCG AAAGAAAACGCGCAAATGGCGCTCTTTTCGCCCTATGACATACAACGACGCTACGGCAAA CCGTTTGGCGATATCGCCATTAGCGAACGGTACGATGAATTAATTGCCGATCCGCACGTG CGCAAAACCTATATTAACGCCCGTGACTTTTTTCAAACACTGGCGGAGATTCAGTTCGAA TCCGGGTATCCCTACATCATGTTTGAAGATACGGTAAACCGCGCGAATCCCATTGCTGGT CGCATTAATATGAGCAACCTGTGCTCAGAAATTTTACAGGTCAATAGCGCTTCCCGTTAC GACGATAACCTTGACTATACCCACATCGGGCATGACATCTCCTGCAATCTCGGCTCGCTG AATATCGCTCACGTCATGGATTCACCGGACATTGGCCGTACCGTAGAAACCGCTATTCGC GGCCTGACGGCGGTGTCGGACATGAGCCATATACGCAGCGTGCCCTCAATAGCCGCCGGT AATGCCGCCTCTCATGCCATCGGTCTGGGCCAGATGAATCTGCATGGCTATCTGGCGAGG GAAGGTATTGCCTACGGTTCGCCGGAGGCGTTGGATTTCACCAATCTCTATTTTTACACC ATTACCTGGCATGCCGTGCATACTTCAATGCGGCTAGCCCGCGAACGCGGCAAAACCTTC GCCGGATTTGCGCAGTCGCGCTATGCCAGCGGCGACTATTTTACGCAGTATTTACAGGAC GACTGGCAACCGAAAACAGCGAAAGTCAGGGCGCTATTTGCCCGCAGCGGCATTACGCTG CCCACACGAGAAATGTGGCTAAAGCTGCGCGACGATGTGATGCGCTATGGCATCTATAAC CAAAATTTGCAGGCGGTGCCGCCGACCGGTTCGATTTCTTACATTAATCATGCGACCTCC AGCATTCATCCGATTGTGGCCAAAATTGAGATTCGCAAAGAGGGCAAAACCGGGCGTGTG TATTACCCCGCGCCGTTTATGACCAATGAAAACCTGGACATGTATCAGGATGCTTACGAT ATCGGTCCGGAAAAAATTATTGATACCTATGCCGAGGCCACGCGCCACGTCGATCAAGGG CTGTCGCTCACCCTGTTTTTCCCCGATACCGCCACGACCCGCGATATCAACAAGGCGCAG ATCTATGCCTGGCGAAAAGGTATTAAGTCCCTGTATTACATCCGGCTTCGCCAGTTGGCG CTGGAAGGTACTGAAATTGAAGGCTGCGTATCCTGCGCGCTATAA PF02867 Ribonuc_red_lgC PF00317 Ribonuc_red_lgN PF08343 RNR_N component protein complex component ribonucleoside-diphosphate reductase complex function oxidoreductase activity function oxidoreductase activity, acting on CH2 groups function oxidoreductase activity, acting on CH2 groups, disulfide as acceptor function ribonucleoside-diphosphate reductase activity function catalytic activity process metabolism process cellular metabolism process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process DNA replication process DNA metabolism process physiological process BE0001260 Thymidine kinase, cytosolic 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 Thymidine kinase, cytosolic Nucleotide transport and metabolism ATP + thymidine = ADP + thymidine 5'- phosphate TK1 17q23.2-q25.3 Cytoplasm None 8.61 25469.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:11830 GenAtlas TK1 GeneCards TK1 GenBank Gene Database K02581 GenBank Protein Database 339709 UniProtKB P04183 UniProt Accession KITH_HUMAN EC 2.7.1.21 >Thymidine kinase, cytosolic MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN >705 bp ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA PF00265 TK function catalytic activity function thymidine kinase activity function nucleotide binding function purine nucleotide binding function adenyl nucleotide binding function transferase activity function ATP binding function transferase activity, transferring phosphorus-containing groups function kinase activity function nucleobase, nucleoside, nucleotide kinase activity function nucleoside kinase activity function binding function deoxynucleoside kinase activity BE0001442 Anaerobic ribonucleoside-triphosphate reductase Enterobacteria phage T4 # 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 Anaerobic ribonucleoside-triphosphate reductase Nucleotide transport and metabolism 2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin NRDD None 7.06 67957.0 Enterobacteria phage T4 GenBank Gene Database Y00122 GenBank Protein Database 1177560 UniProtKB P07071 UniProt Accession NRDD_BPT4 EC 1.17.4.2 >Anaerobic ribonucleoside-triphosphate reductase MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHES GIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVA SHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEY EVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEE GVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDS TGNEILDGRNNLGVVTLNLPRIALDSYIGTQFNEQKFVELFNERMDLCFEALMCRISSLK GVKATVAPILYQEGAFGVRLKPDDDIIELFKNGRSSVSLGYIGIHELNILVGRDIGREIL TKMNAHLKQWTERTGFAFSLYSTPAENLCYRFCKLDTEKYGSVKDVTDKGWYTNSFHVSV EENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPV DKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMH RVKHQ >1818 bp ATGACAATTGAAAAAGAAATTGAAGGATTAATTCATAAAACTAATAAAGACCTTTTAAAC GAGAATGCTAATAAAGATTCTCGTGTTTTTCCAACTCAACGGGACCTTATGGCTGGTATT GTGTCTAAACACATTGCCAAAAATATGGTCCCGTCTTTTATTATGAAAGCGCATGAAAGC GGAATTATTCACGTGCATGATATTGATTATTCCCCTGCTCTTCCATTTACTAATTGCTGT TTAGTAGATTTAAAAGGAATGCTTGAAAACGGATTTAAGCTTGGTAATGCGCAGATTGAA ACTCCTAAATCAATTGGAGTTGCTACTGCAATTATGGCACAAATTACTGCGCAAGTTGCT TCTCACCAATACGGCGGAACGACTTTTGCGAATGTAGATAAAGTACTTTCTCCTTATGTT AAACGCACCTATGCAAAACATATTGAGGATGCAGAAAAATGGCAAATCGCTGATGCGTTG AATTATGCTCAATCTAAAACAGAAAAAGACGTATACGATGCATTCCAAGCTTATGAGTAT GAAGTGAACACGTTATTCAGTTCAAACGGACAGACTCCTTTTGTAACAATTACATTTGGT ACGGGAACTGACTGGACTGAACGAATGATTCAGAAAGCAATTCTGAAAAATCGTATTAAA GGTCTTGGTCGTGATGGGATAACTCCTATTTTCCCTAAGCTTGTTATGTTCGTTGAAGAA GGTGTTAATCTTTATAAAGACGATCCGAACTATGATATTAAACAGCTTGCTCTAGAGTGC GCAAGCAAAAGGATGTATCCTGATATTATTTCAGCTAAGAACAATAAAGCTATCACTGGT TCATCTGTTCCTGTTTCTCCGATGGGTTGCCGTAGTTTCTTGAGCGTATGGAAAGATTCG ACTGGCAATGAAATTCTTGATGGACGCAATAATCTTGGTGTTGTAACACTGAATCTTCCT CGCATCGCGTTAGATTCTTATATTGGAACACAGTTCAATGAACAGAAATTTGTTGAGCTA TTTAATGAACGAATGGATTTATGTTTTGAAGCTTTGATGTGTAGAATTAGTTCCTTAAAA GGAGTTAAAGCTACTGTTGCTCCTATTCTTTACCAAGAAGGTGCATTCGGGGTTCGTCTT AAACCTGATGACGACATAATTGAGTTATTTAAAAACGGTAGAAGTTCAGTGTCTTTAGGA TACATTGGTATTCACGAATTGAATATTCTTGTCGGTCGTGATATTGGACGAGAAATTTTA ACTAAAATGAATGCTCATCTTAAACAGTGGACTGAAAGAACCGGATTTGCTTTTAGTTTA TATTCGACTCCTGCTGAAAACCTGTGTTATCGCTTCTGTAAACTCGATACAGAAAAATAT GGAAGCGTAAAAGATGTTACCGATAAAGGCTGGTACACTAACAGTTTCCATGTTTCAGTA GAAGAAAATATTACTCCGTTTGAAAAGATTTCTCGTGAAGCGCCATATCATTTCATTGCG ACAGGTGGTCACATTTCTTATGTTGAACTTCCTGATATGAAAAATAACTTAAAAGGTCTT GAGGCCGTGTGGGATTATGCTGCACAGCATTTAGATTATTTTGGTGTTAATATGCCAGTA GATAAATGTTTTACATGTGGAAGTACCCATGAAATGACTCCTACTGAAAACGGATTTGTT TGTTCTATTTGTGGAGAAACTGATCCTAAAAAGATGAATACCATAAGAAGAACATGTGGT TATTTGGGAAATCCGAACGAACGCGGATTTAATCTCGGTAAAAATAAAGAAATCATGCAT AGGGTTAAGCACCAATGA PF01228 Gly_radical function catalytic activity process physiological process process metabolism BE0001218 Thymidylate kinase Mycobacterium tuberculosis # 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 Thymidylate kinase Nucleotide transport and metabolism Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with ITP, GTP, CTP and UTP tmk None 7.66 22635.0 Mycobacterium tuberculosis GenBank Gene Database BX842582 GenBank Protein Database 2072714 UniProtKB O05891 UniProt Accession KTHY_MYCTU dTMP kinase EC 2.7.4.9 Thymidine monophosphate kinase TMPK >Thymidylate kinase MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAEALHGEHGDLA SSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASNAAYSAARLHENAAGKAAAWV QRIEFARLGLPKPDWQVLLAVSAELAGERSRGRAQRDPGRARDNYERDAELQQRTGAVYA ELAAQGWGGRWLVVGADVDPGRLAATLAPPDVPS >645 bp TCAACTTGGCACGTCTGGAGGCGCCAAAGTCGCCGCTAGTCGGCCCGGATCAACATCGGC GCCGACAACCAGCCACCGGCCGCCCCACCCTTGGGCCGCCAACTCGGCGTAGACCGCACC GGTGCGCTGCTGAAGTTCAGCGTCGCGTTCGTAATTGTCGCGCGCCCGACCGGGGTCACG CTGGGCACGGCCGCGGGATCGTTCCCCGGCGAGCTCGGCAGAGACCGCAAGGAGCACCTG CCAGTCGGGCTTGGGCAACCCGAGTCTTGCAAATTCGATCCGCTGAACCCAGGCCGCTGC CTTCCCGGCCGCGTTTTCATGTAGGCGCGCCGCGCTGTAGGCCGCGTTGGAGGCGACGTA GCGATCCAGGATCACCACGTCGTAGCCGCGACACAGCCCCTGGATCGTGTGGACCGCGCC AGCGCGGTCGAGCGCGAACAGCGTCGCCATCGCATACACCGACGATGCGAGGTCACCGTG CTCGCCGTGCAGCGCCTCCGCTGCGATGTCGGCGGCCACCGACTGTCCGTAGCGCGGGAA CGCCAGTGTGGCCACCGATCTCCCGGCTGCTCGAAAGGCCCCGGACAGCTTTTCCACCAA CGTCCGCTTGCCAGCGCCGTCAACGCCCTCAATCGCGATTAGCAC PF02223 Thymidylate_kin function catalytic activity function phosphotransferase activity, phosphate group as acceptor function nucleotide binding function thymidylate kinase activity function purine nucleotide binding function adenyl nucleotide binding function transferase activity function ATP binding function transferase activity, transferring phosphorus-containing groups function binding process pyrimidine nucleotide metabolism process metabolism process pyrimidine nucleotide biosynthesis process cellular metabolism process pyrimidine nucleoside triphosphate biosynthesis process pyrimidine deoxyribonucleoside triphosphate biosynthesis process dTTP biosynthesis process pyrimidine nucleoside diphosphate biosynthesis process pyrimidine deoxyribonucleoside diphosphate biosynthesis process nucleobase, nucleoside, nucleotide and nucleic acid metabolism process dTDP biosynthesis process physiological process process nucleotide metabolism "
owl:sameAs	drug:EXPT03131

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

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