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Human Metabolome Database Version 2.5

 

Showing metabocard for Inosinic acid (HMDB00175)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:44
Accession Number HMDB00175
Secondary Accession Numbers Not Available
Common Name Inosinic acid
Description A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety. Inosinic acid is a nucleotide present in muscle and other tissues. It is formed by the deamination of AMP and when hydrolysed produces inosine. Inosinic acid is the ribonucleotide of hypoxanthine and is the first compound formed during the synthesis of purine. (Wikipedia)
Synonyms
  1. 5'-IMP
  2. 5'-Inosinate
  3. 5'-Inosine monophosphate
  4. 5'-Inosinic acid
  5. IMP
  6. Inosine 5'-monophosphate
  7. Inosine 5'-phosphate
  8. Inosine Monophosphate
  9. Inosine-5'-monophosphate
Chemical IUPAC Name [3,4-dihydroxy-5-(6-hydroxypurin-9-yl)-oxolan-2-yl]methoxyphosphonic acid
Chemical Formula C10H13N4O8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Purine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 348.206
Monoisotopic Molecular Weight 348.047089
Isomeric SMILES O[C@@H]1[C@@H](COP(O)(O)=O)O[C@H]([C@@H]1O)N1C=NC2=C1N=CNC2=O
Canonical SMILES OC1C(COP(O)(O)=O)OC(C1O)N1C=NC2=C1N=CNC2=O
KEGG Compound ID C00130 Link Image
BioCyc ID IMP Link Image
BiGG ID 33960 Link Image
Wikipedia Link Inosinic acid Link Image
NuGOwiki Link HMDB00175 Link Image
Metagene Link HMDB00175 Link Image
METLIN ID 5196 Link Image
PubChem Compound 8582 Link Image
PubChem Substance 6436024 Link Image
ChEBI ID 17202 Link Image
CAS Registry Number 131-99-7
InChI Identifier InChI=1/C10H13N4O8P/c15-6-4(1-21-23(18,19)20)22-10(7(6)16)14-3-13-5-8(14)11-2-12-9(5)17/h2-4,6-7,10,15-16H,1H2,(H,11,12,17)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Park, Yeong Hun; Cho, Gwang Myeong; Baek, Min Ji; Hong, Guk Gi; Lee, Jin Nam. Method for preparing 5'-inosinic acid by using microbe capable of over-expressing purC gene. Repub. Korea (2007), 7pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.92 mg/mL [MEYLAN,WM et al. (1996)]; 3.05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.04 [Predicted by ALOGPS]; -3 [Predicted by PubChem via XLOGP]; -1.50 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1B4D Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 63.0 +/- 41.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Traut TW: Physiological concentrations of purines and pyrimidines. Mol Cell Biochem. 1994 Nov 9;140(1):1-22. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Biofluid CSF
Value 3.19 (0.00 +/- 19.70) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Cerebrospinal fluid purine metabolite and neuron-specific enolase concentrations after febrile seizures. Brain Dev. 2000 Oct;22(7):427-31. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 2.31(0.00-41.40) uM
Age Adult:>18 yrs old
Sex Both
Condition Febrile seizures
Comments Not Available
References
  • Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Cerebrospinal fluid purine metabolite and neuron-specific enolase concentrations after febrile seizures. Brain Dev. 2000 Oct;22(7):427-31. [PubMed Link Image]
Biofluid CSF
Value 2.48 (0.00 +/- 27.20) uM
Age Adult:>18 yrs old
Sex Both
Condition Febrile seizures
Comments Not Available
References
  • Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Cerebrospinal fluid purine metabolite and neuron-specific enolase concentrations after febrile seizures. Brain Dev. 2000 Oct;22(7):427-31. [PubMed Link Image]
Associated Disorders
Condition References
Febrile seizures
  • Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Cerebrospinal fluid purine metabolite and neuron-specific enolase concentrations after febrile seizures. Brain Dev. 2000 Oct;22(7):427-31. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Green HJ, Grant SM, Phillips SM, Enns DL, Tarnopolsky MA, Sutton JR: Reduced muscle lactate during prolonged exercise following induced plasma volume expansion. Can J Physiol Pharmacol. 1997 Dec;75(12):1280-6. [PubMed Link Image]
  2. Rodriguez-Nunez A, Cid E, Rodriguez-Garcia J, Camina F, Rodriguez-Segade S, Castro-Gago M: Concentrations of nucleotides, nucleosides, purine bases, oxypurines, uric acid, and neuron-specific enolase in the cerebrospinal fluid of children with sepsis. J Child Neurol. 2001 Sep;16(9):704-6. [PubMed Link Image]
  3. Pouw EM, Schols AM, van der Vusse GJ, Wouters EF: Elevated inosine monophosphate levels in resting muscle of patients with stable chronic obstructive pulmonary disease. Am J Respir Crit Care Med. 1998 Feb;157(2):453-7. [PubMed Link Image]
  4. Castro-Gago M, Cid E, Trabazo S, Pavon P, Camina F, Rodriguez-Segade S, Einis Punal J, Rodriguez-Nunez A: Cerebrospinal fluid purine metabolites and pyrimidine bases after brief febrile convulsions. Epilepsia. 1995 May;36(5):471-4. [PubMed Link Image]
  5. Allison AC, Eugui EM: Purine metabolism and immunosuppressive effects of mycophenolate mofetil (MMF). Clin Transplant. 1996 Feb;10(1 Pt 2):77-84. [PubMed Link Image]
  6. van Hall G, van der Vusse GJ, Soderlund K, Wagenmakers AJ: Deamination of amino acids as a source for ammonia production in human skeletal muscle during prolonged exercise. J Physiol. 1995 Nov 15;489 ( Pt 1):251-61. [PubMed Link Image]
  7. McConell G, Snow RJ, Proietto J, Hargreaves M: Muscle metabolism during prolonged exercise in humans: influence of carbohydrate availability. J Appl Physiol. 1999 Sep;87(3):1083-6. [PubMed Link Image]
  8. McConell GK, Shinewell J, Stephens TJ, Stathis CG, Canny BJ, Snow RJ: Creatine supplementation reduces muscle inosine monophosphate during endurance exercise in humans. Med Sci Sports Exerc. 2005 Dec;37(12):2054-61. [PubMed Link Image]
  9. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  10. Klupp J, Pfitzmann R, Langrehr JM, Neuhaus P: Indications of mycophenolate mofetil in liver transplantation. Transplantation. 2005 Sep 27;80(1 Suppl):S142-6. [PubMed Link Image]
  11. Bangsbo J, Gollnick PD, Graham TE, Juel C, Kiens B, Mizuno M, Saltin B: Anaerobic energy production and O2 deficit-debt relationship during exhaustive exercise in humans. J Physiol. 1990 Mar;422:539-59. [PubMed Link Image]
  12. McCauley TG, Hamaguchi N, Stanton M: Aptamer-based biosensor arrays for detection and quantification of biological macromolecules. Anal Biochem. 2003 Aug 15;319(2):244-50. [PubMed Link Image]
  13. Rush JW, MacLean DA, Hultman E, Graham TE: Exercise causes branched-chain oxoacid dehydrogenase dephosphorylation but not AMP deaminase binding. J Appl Physiol. 1995 Jun;78(6):2193-200. [PubMed Link Image]
  14. McConell GK, Canny BJ, Daddo MC, Nance MJ, Snow RJ: Effect of carbohydrate ingestion on glucose kinetics and muscle metabolism during intense endurance exercise. J Appl Physiol. 2000 Nov;89(5):1690-8. [PubMed Link Image]
  15. Swart PJ, Beljaars E, Smit C, Pasma A, Schuitemaker H, Meijer DK: Comparative pharmacokinetic, immunologic and hematologic studies on the anti-HIV-1/2 compounds aconitylated and succinylated HSA. J Drug Target. 1996;4(2):109-16. [PubMed Link Image]
  16. Scott GS, Spitsin SV, Kean RB, Mikheeva T, Koprowski H, Hooper DC: Therapeutic intervention in experimental allergic encephalomyelitis by administration of uric acid precursors. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16303-8. Epub 2002 Nov 25. [PubMed Link Image]
  17. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. 5'(3')-deoxyribonucleotidase, mitochondrial precursor
  5. Cytosolic purine 5'-nucleotidase
  6. Ectonucleoside triphosphate diphosphohydrolase 1
  7. Soluble calcium-activated nucleotidase 1
  8. Glycogen phosphorylase, liver form
  9. Glycogen phosphorylase, muscle form
  10. Glycogen phosphorylase, brain form
  11. Inosine triphosphate pyrophosphatase
  12. Hypoxanthine-guanine phosphoribosyltransferase
  13. AMP deaminase 2
  14. AMP deaminase 1
  15. GMP reductase 2
  16. GMP reductase 1
  17. Inosine-5'-monophosphate dehydrogenase 2
  18. Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
  19. Adenylosuccinate synthetase isozyme 1
  20. Cytosolic 5'-nucleotidase III
  21. ENTPD4 protein
  22. IMP
  23. Ectonucleoside triphosphate diphosphohydrolase 8
  24. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  25. Adenosine monophosphate deaminase (Isoform E) (Adenosine monophosphate deaminase (Isoform E), isoform CRA_b) (cDNA FLJ76195, highly similar to Homo sapiens adenosine monophosphate deaminase (isoform E) (AMPD3),mRNA)
  26. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  27. Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
  28. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  29. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  30. Adenylosuccinate synthetase
Enzyme 1 [top]
Enzyme 1 ID 5232
Enzyme 1 Name Cytosolic 5'-nucleotidase 1B
Enzyme 1 Synonyms
  1. Cytosolic 5'-nucleotidase IB
  2. cN1B
  3. cN-IB
  4. Autoimmune infertility-related protein
Enzyme 1 Gene Name NT5C1B
Enzyme 1 Protein Sequence >Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
Enzyme 1 Number of Residues 610
Enzyme 1 Molecular Weight 68804
Enzyme 1 Theoretical pI 9.03
Enzyme 1 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 13774961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96P26 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 5NT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1699 bp
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
Enzyme 1 GenBank Gene ID AF356185 Link Image
Enzyme 1 GeneCard ID NT5C1B Link Image
Enzyme 1 GenAtlas ID NT5C1B Link Image
Enzyme 1 HGNC ID HGNC:17818 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5233
Enzyme 2 Name Cytosolic 5'-nucleotidase 1A
Enzyme 2 Synonyms
  1. Cytosolic 5'-nucleotidase IA
  2. cN1A
  3. cN-IA
  4. cN-I
Enzyme 2 Gene Name NT5C1A
Enzyme 2 Protein Sequence >Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
Enzyme 2 Number of Residues 368
Enzyme 2 Molecular Weight 41021
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12659324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BXI3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 5NT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
Enzyme 2 GenBank Gene ID AF331801 Link Image
Enzyme 2 GeneCard ID NT5C1A Link Image
Enzyme 2 GenAtlas ID NT5C1A Link Image
Enzyme 2 HGNC ID HGNC:17819 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p34.3-p33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5234
Enzyme 3 Name 5'(3')-deoxyribonucleotidase, cytosolic type
Enzyme 3 Synonyms
  1. Cytosolic 5',3'-pyrimidine nucleotidase
  2. Deoxy-5'-nucleotidase 1
  3. dNT-1
Enzyme 3 Gene Name NT5C
Enzyme 3 Protein Sequence >5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
Enzyme 3 Number of Residues 201
Enzyme 3 Molecular Weight 23383
Enzyme 3 Theoretical pI 6.63
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7524492 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TCD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NT5C_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
Enzyme 3 GenBank Gene ID AF154829 Link Image
Enzyme 3 GeneCard ID NT5C Link Image
Enzyme 3 GenAtlas ID NT5C Link Image
Enzyme 3 HGNC ID HGNC:17144 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed Link Image]
  2. Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5236
Enzyme 4 Name 5'(3')-deoxyribonucleotidase, mitochondrial precursor
Enzyme 4 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 4 Gene Name NT5M
Enzyme 4 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial precursor
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 4 Number of Residues 228
Enzyme 4 Molecular Weight 25862
Enzyme 4 Theoretical pI 8.12
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9408106 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 4 PDB ID 1Q92 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 4 GenBank Gene ID AJ277557 Link Image
Enzyme 4 GeneCard ID NT5M Link Image
Enzyme 4 GenAtlas ID NT5M Link Image
Enzyme 4 HGNC ID HGNC:15769 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed Link Image]
  2. Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5237
Enzyme 5 Name Cytosolic purine 5'-nucleotidase
Enzyme 5 Synonyms
  1. 5'-nucleotidase cytosolic II
Enzyme 5 Gene Name NT5C2
Enzyme 5 Protein Sequence >Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
Enzyme 5 Number of Residues 561
Enzyme 5 Molecular Weight 64970
Enzyme 5 Theoretical pI 6.05
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5-prime-monophosphate (IMP) and other purine nucleotides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 633071 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P49902 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name 5NTC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1686 bp
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 5 GenBank Gene ID D38524 Link Image
Enzyme 5 GeneCard ID NT5C2 Link Image
Enzyme 5 GenAtlas ID NT5C2 Link Image
Enzyme 5 HGNC ID HGNC:8022 Link Image
Enzyme 5 Chromosome Location 10
Enzyme 5 Locus 10q24.32-q24.33
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5313
Enzyme 6 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 6 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 6 Gene Name ENTPD1
Enzyme 6 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 6 Number of Residues 510
Enzyme 6 Molecular Weight 57965
Enzyme 6 Theoretical pI 6.29
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 17-37 479-499
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 765256 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 6 GenBank Gene ID S73813 Link Image
Enzyme 6 GeneCard ID ENTPD1 Link Image
Enzyme 6 GenAtlas ID ENTPD1 Link Image
Enzyme 6 HGNC ID HGNC:3363 Link Image
Enzyme 6 Chromosome Location 10
Enzyme 6 Locus 10q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5314
Enzyme 7 Name Soluble calcium-activated nucleotidase 1
Enzyme 7 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 7 Gene Name CANT1
Enzyme 7 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 7 Number of Residues 401
Enzyme 7 Molecular Weight 44840
Enzyme 7 Theoretical pI 5.98
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 7 Pathways
Enzyme 7 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 45-62
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 22218108 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 7 PDB ID 1S1D Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 7 GenBank Gene ID AF328554 Link Image
Enzyme 7 GeneCard ID CANT1 Link Image
Enzyme 7 GenAtlas ID CANT1 Link Image
Enzyme 7 HGNC ID HGNC:19721 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5606
Enzyme 8 Name Glycogen phosphorylase, liver form
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name PYGL
Enzyme 8 Protein Sequence >Glycogen phosphorylase, liver form
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTV
RDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEA
DDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVN
TMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKL
PWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFP
KDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKF
QNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQ
ENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFV
PRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPA
TDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVA
ALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEA
YVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNE
SNKVNGN
Enzyme 8 Number of Residues 847
Enzyme 8 Molecular Weight 97150
Enzyme 8 Theoretical pI 7.17
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 8 Pathways
Enzyme 8 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 183353 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P06737 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PYGL_HUMAN Link Image
Enzyme 8 PDB ID 1L7X Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2544 bp
ATGGGCGAACCGCTGACAGACCAGGAGAAGCGGCGGCAGATCAGCATCCGCGGCATCGTG
GGCGTGGAGAACGTGGCAGAGCTGAAGAAGAGTTTCAACCGGCACCTGCACTTCACGCTG
GTCAAGGACCGCAACGTGGCCACCACCCGCGACTACTACTTCGCGCTGGCGCACACGGTG
CGGGACCACCTGGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTACGACAAGTGCCCC
AAGAGGGAATATTACCTCTCTCTGGAATTTTACATGGGCCGAACATTACAGAACACCATG
ATCAACCTCGGTCTGCAAAATGCCTGTGATGAGGCCATTTACCAGCTTGGATTGGATATA
GAAGAGTTAGAAGAAATTGAAGAAGATGCTGGACTTGGCAATGGTGGTCTTGGGAGACTT
GCTGCCTGCTTCTTGGATTCCATGGCAACCCTGGGACTTGCAGCCTATGGATACGGCATT
CGGTATGAATATGGGATTTTCAATCAGAAGATCCGAGATGGATGGCAGGTAGAAGAAGCA
GATGATTGGCTCAGATATGGAAACCCTTGGGAGAAGTCCCGCCCAGAATTCATGCTGCCT
GTGCACTTCTATGGAAAAGTAGAACACACCAACACCGGGACCAAGTGGATTGACACTCAA
GTGGTCCTGGCTCTGCCATATGACACCCCCGAGCCCGGCTACATGAATAACACTGTCAAC
ACCATGCGCCTCTGGTCTGCTCGGGCACCAAATGACTTTAACCTCAGAGACTTTAATGTT
GGAGACTACATTCAGGCTGTGCTGGACCGAAACCTGGCCGAGAACATCTCCCGGGTCCTC
TATCCCAATGACAATTTTTTTGAAGGGAAGGAGCTAAGATTGAAGCAGGAATACTTTGTG
GTGGCTGCAACCTTGCAAGATATCATCCGCCGTTTCAAAGCCTCCAAGTTTGGCTCCACC
CGTGGTCAAGGAACTGTGTTTGATGCCTTCCCGGATCAGGTGGCCATCCAGCTGAATGAT
ACTCACCCTCGCATCGCGATCCCTGAGCTGATGAGGATTTTTGTGGATATTGAAAAACTG
CCCTGGTCCAAGGCATGGGAGCTCAACCAGAAGACCTTCGCCTACACCAACCACACAGTG
CTCCCGGAAGCCCTGGAGCGCTGGCCCGTGGACCTGGTGGAGAAGCTGCTCCCTCGACAT
TTGGAAATCATTTATGAGATAAATCAGAAGCATTTAGATAGAATTGTGGCCTTGTTTCCT
AAAGATGTGGACCCTCTGAGAAGGATGTCTCTGATAGAAGAGGAAGGAAGCAAAAGGATC
AACATGGCCCATCTCTGCATTGTCGGTTCCCATGCTGTGAATGGCGTGGCTAAAATCCAC
TCAGACATCGTGAAGACTAAAGTATTCAAGGACTTCAGTGAGCTAGAACCTGACAAGTTT
CAGAATAAAACCAATGGGATCACTCCAAGGCGCTGGCTCCTACTCTGCAACCCAGGACTT
GCAGAGCTCATAGCAGAGAAAATTGGAGAAGACTATGTGAAAGACCTGAGCCAGCTGACG
AAGCTCCACAGCTTCCTGGGTGATGATGTCTTCCTCCGGGAACTCGCCAAGGTGAAGCAG
GAGAATAAGCTGAAGTTTTCTCAGTTCCTGGAGACGGAGTACAAAGTGAAGATCAACCCA
TCCTCCATGTTTGATGTCCAGGTGAAGAGGATACATGAGTACAAGCGACAGCTCTTGAAC
TGTCTGCATGTGATCACGATGTACAACCGCATTAAGAAAGACCCTAAGAAGTTATTCGTG
CCAAGGACAGTTATCATTGGTGGTAAAGCTGCCCCAGGATATCACATGGCCAAAATGATC
ATAAAGCTGATCACTTCAGTGGCAGATGTGGTGAACAATGACCCTATGGTTGGAAGCAAG
TTGAAAGTCATCTTCTTGGAGAACTACAGAGTATCTCTTGCTGAAAAAGTCATTCCAGCC
ACAGATCTGTCAGAGCAGATTTCCACTGCAGGCACCGAAGCCTCGGGGACAGGCAATATG
AAGTTCATGCTAAATGGGGCCCTAACTATCGGGACCATGGATGGGGCCAATGTGGAAATG
GCAGAAGAAGCTGGGGAAGAGAACCTGTTCATCTTTGGCATGAGCATAGATGATGTGGCT
GCTTTGGACAAGAAAGGGTACGAGGCAAAAGAATACTATGAGGCACTTCCAGAGCTGAAG
CTGGTCATTGATCAAATTGACAATGGCTTTTTTTCTCCCAAGCAGCCTGACCTCTTCAAA
GATATCATCAACATGCTATTTTATCATGACAGGTTTAAAGTCTTTGCAGACTACGAAGCC
TATGTCAAGTGTCAAGATAAAGTGAGTCAGCTGTACATGAATCCAAAGGCCTGGAACACA
ATGGTACTCAAAAACATAGCTGCCTCGGGGAAATTCTCCAGTGACCGAACAATTAAAGAA
TATGCCCAAAACATCTGGAACGTGGAACCTTCAGATCTAAAGATTTCTCTATCCAATGAA
TCTAACAAAGTCAATGGAAATTGA
Enzyme 8 GenBank Gene ID M14636 Link Image
Enzyme 8 GeneCard ID PYGL Link Image
Enzyme 8 GenAtlas ID PYGL Link Image
Enzyme 8 HGNC ID HGNC:9725 Link Image
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q21-q22
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Newgard CB, Nakano K, Hwang PK, Fletterick RJ: Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8132-6. [PubMed Link Image]
  2. Chang S, Rosenberg MJ, Morton H, Francomano CA, Biesecker LG: Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI. Hum Mol Genet. 1998 May;7(5):865-70. [PubMed Link Image]
  3. Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW: Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. [PubMed Link Image]
  4. Gorin FA, Mullinax RL, Ignacio PC, Neve RL, Kurnit DM: McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues. J Neurogenet. 1987 Dec;4(6):293-308. [PubMed Link Image]
  5. Rath VL, Ammirati M, Danley DE, Ekstrom JL, Gibbs EM, Hynes TR, Mathiowetz AM, McPherson RK, Olson TV, Treadway JL, Hoover DJ: Human liver glycogen phosphorylase inhibitors bind at a new allosteric site. Chem Biol. 2000 Sep;7(9):677-82. [PubMed Link Image]
  6. Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J: Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core. Mol Cell. 2000 Jul;6(1):139-48. [PubMed Link Image]
  7. Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL: Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase. Chem Biol. 2002 Aug;9(8):915-24. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5610
Enzyme 9 Name Glycogen phosphorylase, muscle form
Enzyme 9 Synonyms
  1. Myophosphorylase
Enzyme 9 Gene Name PYGM
Enzyme 9 Protein Sequence >Glycogen phosphorylase, muscle form
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI
Enzyme 9 Number of Residues 842
Enzyme 9 Molecular Weight 97093
Enzyme 9 Theoretical pI 7.03
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 9 Pathways
Enzyme 9 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 190784 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P11217 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PYGM_HUMAN Link Image
Enzyme 9 PDB ID 1XL1 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >2529 bp
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGGTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAGGATCTACTACCTGTCTTTAGAGTTCTATATGGGACGGACGCTACAGAACACCATG
GTGAACCTGGCCTTAGAGAATGCCTGTGACGAGGCCACCTACCAGCTGGGCCTGGACATG
GAGGAGCTGGAGGAAATTGAGGAGGATGCGGGGCTGGGCAACGGGGGCCTGGGCCGGCTG
GCAGCCTGCTTTCTTGACTCCATGGCAACACTGGGCCTGGCTGCCTATGGCTACGGGATT
CGCTATGAGTTTGGGATTTTTAACCAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCC
GATGACTGGCTTCGCTACGGCAACCCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCT
GTGCACTTCTACGGCCATGTGGAGCACACCAGCCAGGGTGCCAAGTGGGTGGACACACAG
GTGGTACTGGCCATGCCCTACGATACCCCGGTGCCTGGCTATCGCAACAATGTTGTCAAC
ACCATGCGCCTCTGGTCTGCCAAGGCTCCCAATGACTTCAACCTCAAGGACTTCAATGTC
GGTGGCTACATCCAGGCTGTGTTGGACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTG
TACCCCAATGATAATTTCTTCGAAGGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTG
GTGGCTGCCACCCTCCAGGACATCATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGT
GATCCCGTGCGCACGAACTTCGATGCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGAC
ACCCACCCCTCCCTGGCCATCCCCGAGCTGATGAGGATCCTGGTGGACCTGGAACGGATG
GACTGGGACAAGGCGTGGGATGTGACAGTGAGGACCTGTGCCTACACCAACCACACGGTG
CTGCCCGAGGCCCTGGAGCGCTGGCCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCAC
CTCCAGATCATCTACGAGATCAACCAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCA
GGGGACGTAGACCGGCTGCGGCGCATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATC
AACATGGCACACCTGTGCATCGCGGGGTCGCACGCCGTCAACGGTGTGGCCCGCATCCAC
TCGGAGATCCTCAAGAAGACCATCTTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTC
CAGAATAAGACCAACGGCATCACCCCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTG
GCAGAGGTCATTGCTGAGCGCATCGGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGC
AAACTGCTCTCCTTTGTGGATGATGAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAG
GAAAACAAGTTGAAGTTTGCTGCCTACCTAGAGAGGGAATACAAAGTCCACATCAACCCC
AACTCACTCTTCGACATCCAGGTGAAGCGGATTCACGAATATAAACGACAGCTCCTCAAC
TGCCTCCATGTCATCACCCTGTACAACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTG
CCTCGGACTGTGATGATTGGAGGGAAGGCTGCACCTGGGTACCACATGGCCAAGATGATC
ATCAGACTCGTCACAGCCATCGGGGATGTGGTCAACCATGACCCGGCAGTGGGTGACCGC
CTCCGTGTCATCTTCCTGGAGAACTACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCT
GCAGACCTCTCTGAGCAGATCTCCACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATG
AAGTTCATGCTCAACGGGGCTCTGACCATTGGCACCATGGACGGGGCCAATGTGGAGATG
GCAGAAGAGGCGGGAGAGGAAAACTTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGAT
AAGCTTGACCAAAGAGGGTACAATGCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGG
CAGGTCATTGAGCAGCTGAGCAGTGGCTTCTTCTCCCCCAAACAACCCGACCTGTTCAAG
GACATTGTCAATATGCTCATGCACCATGACCGGTTTAAAGTCTTCGCAGATTATGAAGAC
TACATTAAATGCCAGGAGAAAGTCAGCGCCTGGTACAAGAACCCAAGAGAGTGGACGCGG
ATGGTGATCCGGAACATAGCCACTTCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAG
TATGCCCGGGAGATCTGGGGTGTGGAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAG
GCCATCTGA
Enzyme 9 GenBank Gene ID M32598 Link Image
Enzyme 9 GeneCard ID PYGM Link Image
Enzyme 9 GenAtlas ID PYGM Link Image
Enzyme 9 HGNC ID HGNC:9726 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11q12-q13.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [PubMed Link Image]
  2. Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [PubMed Link Image]
  3. Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [PubMed Link Image]
  4. Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [PubMed Link Image]
  5. Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [PubMed Link Image]
  6. Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve. 1995;3:S23-7. [PubMed Link Image]
  7. Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [PubMed Link Image]
  8. Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [PubMed Link Image]
  9. Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [PubMed Link Image]
  10. Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [PubMed Link Image]
  11. Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [PubMed Link Image]
  12. Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [PubMed Link Image]
  13. Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [PubMed Link Image]
  14. Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [PubMed Link Image]
  15. Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [PubMed Link Image]
  16. Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5612
Enzyme 10 Name Glycogen phosphorylase, brain form
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name PYGB
Enzyme 10 Protein Sequence >Glycogen phosphorylase, brain form
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
Enzyme 10 Number of Residues 843
Enzyme 10 Molecular Weight 96697
Enzyme 10 Theoretical pI 6.85
Enzyme 10 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 10 Pathways
Enzyme 10 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 307200 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P11216 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PYGB_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2592 bp
ATGGGCGAACCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGAATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCAAGGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGGCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGCTTCAGCACCTGCCCCAC
CCAGAGTGGGAGTCAGGTGGAGCCACCTGCTGGGCTCCCCCAGAACTTTGCACACATCTT
GCTATGTATTAG
Enzyme 10 GenBank Gene ID J03544 Link Image
Enzyme 10 GeneCard ID PYGB Link Image
Enzyme 10 GenAtlas ID PYGB Link Image
Enzyme 10 HGNC ID HGNC:9723 Link Image
Enzyme 10 Chromosome Location 20
Enzyme 10 Locus 20p11.2-p11.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed Link Image]
  2. Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5668
Enzyme 11 Name Inosine triphosphate pyrophosphatase
Enzyme 11 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 11 Gene Name ITPA
Enzyme 11 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 11 Number of Residues 194
Enzyme 11 Molecular Weight 21446
Enzyme 11 Theoretical pI 5.34
Enzyme 11 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 11 General Function Nucleotide transport and metabolism
Enzyme 11 Specific Function Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells
Enzyme 11 Pathways
Enzyme 11 Reactions
  • A nucleoside triphosphate + H2O = a nucleotide + diphosphate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 13398328 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
Enzyme 11 GenBank Gene ID AF219116 Link Image
Enzyme 11 GeneCard ID ITPA Link Image
Enzyme 11 GenAtlas ID ITPA Link Image
Enzyme 11 HGNC ID HGNC:6176 Link Image
Enzyme 11 Chromosome Location 20
Enzyme 11 Locus 20p
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed Link Image]
  4. Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5715
Enzyme 12 Name Hypoxanthine-guanine phosphoribosyltransferase
Enzyme 12 Synonyms
  1. HGPRT
  2. HGPRTase
Enzyme 12 Gene Name HPRT1
Enzyme 12 Protein Sequence >Hypoxanthine-guanine phosphoribosyltransferase
MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Enzyme 12 Number of Residues 218
Enzyme 12 Molecular Weight 24580
Enzyme 12 Theoretical pI 6.67
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hypoxanthine phosphoribosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • physiological process
  • purine ribonucleoside salvage
  • purine salvage
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 12 General Function Nucleotide transport and metabolism
Enzyme 12 Specific Function IMP + diphosphate = hypoxanthine + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 306885 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P00492 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name HPRT_HUMAN Link Image
Enzyme 12 PDB ID 1BZY Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >657 bp
ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA
Enzyme 12 GenBank Gene ID M31642 Link Image
Enzyme 12 GeneCard ID HPRT1 Link Image
Enzyme 12 GenAtlas ID HPRT1 Link Image
Enzyme 12 HGNC ID HGNC:5157 Link Image
Enzyme 12 Chromosome Location X
Enzyme 12 Locus Xq26.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed Link Image]
  2. Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [PubMed Link Image]
  3. Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed Link Image]
  4. Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed Link Image]
  5. Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed Link Image]
  6. Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed Link Image]
  7. Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed Link Image]
  8. Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed Link Image]
  9. Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed Link Image]
  10. Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed Link Image]
  11. Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed Link Image]
  12. Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed Link Image]
  13. Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed Link Image]
  14. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed Link Image]
  15. Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed Link Image]
  16. Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed Link Image]
  17. Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed Link Image]
  18. Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed Link Image]
  19. Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed Link Image]
  20. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed Link Image]
  21. Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed Link Image]
  22. Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed Link Image]
  23. Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed Link Image]
  24. Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed Link Image]
  25. Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed Link Image]
  26. Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed Link Image]
  27. Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed Link Image]
  28. Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed Link Image]
  29. Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed Link Image]
  30. Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed Link Image]
  31. Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed Link Image]
  32. Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed Link Image]
  33. Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed Link Image]
  34. Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed Link Image]
  35. Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5871
Enzyme 13 Name AMP deaminase 2
Enzyme 13 Synonyms
  1. AMP deaminase isoform L
Enzyme 13 Gene Name AMPD2
Enzyme 13 Protein Sequence >AMP deaminase 2
MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPS
GSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMD
GKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLR
AKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDA
AKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPP
ALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVN
VLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIH
ASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHAD
RNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELR
LSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLP
LFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYL
YYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQ
YLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEY
SIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRV
GYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ
Enzyme 13 Number of Residues 879
Enzyme 13 Molecular Weight 100689
Enzyme 13 Theoretical pI 6.93
Enzyme 13 GO Classification
Function
  • AMP deaminase activity
  • catalytic activity
  • deaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function AMP deaminase plays a critical role in energy metabolism
Enzyme 13 Pathways
Enzyme 13 Reactions
  • AMP + H2O = IMP + ammonia
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 644509 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q01433 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name AMPD2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >2263 bp
CGCCGAGGAGCTGTTCACCCGCTCACTGGCTGAGAGCGAGCTCCGTAGTGCCCCGTATGA
GTTCCCCGAGGAGAGCCCCATTGAACAGCTGGAGGAGCGGCGGCAGCGGCTGGAGCGGCA
GATCAGCCAGGATGTCAAGCTGGAGCCAGACATCCTGCTTCGGGCCAAGCAAGATTTCCT
GAAGACGGACAGTGACTCGGACCTACAGCTCTACAAGGAACAGGGTGAGGGGCAGGGTGA
CCGGAGCCTGCGGGAGCGTGATGTGCTGGAACGGGAGTTTCAGCGGGTCACCATCTCTGG
GGAGGAGAAGTGTGGGGTGCCGTTCACAGACCTGCTGGATGCAGCCAAGAGTGTGGTGCG
GGCGCTCTTCATCCGGGAGAAGTACATGGCCCTGTCCCTGCAGAGCTTCTGCCCCACCAC
CCGCCGCTACCTGCAGCAGCTGGCTGAAAAGCCTCTGGAGACCCGGACCTATGAACAGGG
CCCCGACACCCCTGTGTCTGCTGATGCCCCGGTGCACCCCCCTGCGCTGGAGCAGCACCC
GTATGAGCACTGTGAGCCAAGCACCATGCCTGGGGACCTGGGCTTGGGTCTGCGCATGGT
GCGGGGTGTGGTGCACGTCTACACCCGCAGGGAACCCGACGAGCATTGCTCAGAGGTGGA
GCTGCCATACCCTGACCTGCAGGAATTTGTGGCTGACGTCAATGTGCTGATGGCCCTGAT
TATCAATGGCCCCATAAAGTCATTCTGCTACCGCCGGCTGCAGTACCTGAGCTCCAAGTT
CCAGATGCATGTGCTACTCAATGAGATGAAGGAGCTGGCCGCCCAGAAGAAAGTGCCACA
CCGAGATTTCTACAACATCCGCAAGGTGGACACCCACATCCATGCCTCGTCCTGCATGAA
CCAGAAGCATCTGCTGCGCTTCATCAAGCGGGCAATGAAGCGGCACCTGGAGGAGATCGT
GCACGTGGAGCAGGGCCGTGAACAGACGCTGCGGGAGGTCTTTGAGAGCATGAATCTCAC
GGCCTACGACCTGAGTGTGGACACGCTGGATGTGCATGCGGACAGGAACACTTTCCATCG
CTTTGACAAGTTTAATGCCAAATACAACCCTATTGGGGAGTCCGTCCTCCGAGAGATCTT
CATCAAGACGGACAACAGGGTATCTGGGAAGTACTTTGCTCACATCATCAAGGAGGTGAT
GTCAGACCTGGAGGAGAGCAAATACCAGAATGCAGAGCTGCGGCTCTCCATTTACGGGCG
CTCGAGGGATGAGTGGGACAAGCTGGCGCGCTGGGCCGTCATGCACCGCGTGCACTCCCC
CAACGTGCGCTGGCTGGTGCAGGTGCCCCGCCTCTTTGATGTGTACCGTACCAAGGGCCA
GCTGGCCAACTTCCAGGAGATGCTGGAGAACATCTTCCTGCCACTGTTCGAGGCCACTGT
GCACCCTGCCAGCCACCCGGAACTGCATCTCTTCTTAGAGCACGTGGATGGTTTTGACAG
CGTGGATGATGAGTCCAAGCCTGAAAACCATGTCTTCAACCTGGAGAGCCCCCTGCCTGA
GGCGTGGGTGGAGGAGGACAACCCACCCTATGCCTACTACCTGTACTACACCTTTGCCAA
CATGGCCATGTTGAACCACCTGCGCAGGCAGAGGGGCTTCCACACGTTTGTGCTGAGGCC
ACACTGTGGGGAGGCTGGGCCCATCCACCACCTGGTGTCAGCCTTCATGCTGGCTGAGAA
CATTTCCCACGGGCTCCTTCTGCGCAAGGCCCCCGTCCTGCAGTACCTGTACTACCTGGC
CCAGATCGGCATCGCCATGTCTCCGCTCAGCAACAACAGCCTCTTCCTCAGCTATCACCG
GAATCCGCTACCGGAGTACCTGTCCCGCGGCCTCATGGTCTCCCTGTCCACTGATGATCC
CTTGCAGTTCCACTTCACCAAGGAGCCGCTGATGGAGGAGTACAGCATCGCCACCCAGGT
GTGGAAGCTCAGCTCCTGCGATATGTGTGAGCTGGCCCGCAACAGCGTGCTCATGAGCGG
CTTCTCGCACAAGGTAAAGAGCCACTGGCTGGGACCCAACTATACCAAGGAAGGCCCTGA
GGGGAATGACATCCGCCGGACCAATGTGCCAGACATCCGCGTGGGCTACCGCTACGAGAC
CCTGTGCCAGGAGCTGGCGCTCATCACGCAGGCAGTCCAGAGTGAGATGCTGGAGACCAT
TCCAGAGGAGGCGGGTATCACCATGAGCCCAGGGCCTCAATGA
Enzyme 13 GenBank Gene ID M91029 Link Image
Enzyme 13 GeneCard ID AMPD2 Link Image
Enzyme 13 GenAtlas ID AMPD2 Link Image
Enzyme 13 HGNC ID HGNC:469 Link Image
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL: Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J Biol Chem. 1992 Nov 5;267(31):22407-13. [PubMed Link Image]
  2. Van den Bergh F, Sabina RL: Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extensions of isoform L. Biochem J. 1995 Dec 1;312 ( Pt 2):401-10. [PubMed Link Image]
  3. Mahnke-Zizelman DK, van den Bergh F, Bausch-Jurken MT, Eddy R, Sait S, Shows TB, Sabina RL: Cloning, sequence and characterization of the human AMPD2 gene: evidence for transcriptional regulation by two closely spaced promoters. Biochim Biophys Acta. 1996 Aug 14;1308(2):122-32. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5929
Enzyme 14 Name AMP deaminase 1
Enzyme 14 Synonyms
  1. Myoadenylate deaminase
  2. AMP deaminase isoform M
Enzyme 14 Gene Name AMPD1
Enzyme 14 Protein Sequence >AMP deaminase 1
MPLFKLPAEEKQIDDAMRNFAEKVFASEVKDEGGRQEISPFDVDEICPISHHEMQAHIFH
LETLSTSTEARRKKRFQGRKTVNLSIPLSETSSTKLSHIDEYISSSPTYQTVPDFQRVQI
TGDYASGVTVEDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESF
YPVFTPPVKKGEDPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTF
LDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKV
DTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSL
DVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQ
HAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLE
NIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSPKPQEWTLEKNPS
YTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKK
SPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEP
LMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNV
AQIRMAYRYETWCYELNLIAEGLKSTE
Enzyme 14 Number of Residues 747
Enzyme 14 Molecular Weight 86491
Enzyme 14 Theoretical pI 6.89
Enzyme 14 GO Classification
Function
  • AMP deaminase activity
  • catalytic activity
  • deaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function AMP deaminase plays a critical role in energy metabolism
Enzyme 14 Pathways
Enzyme 14 Reactions
  • AMP + H2O = IMP + ammonia
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 10864686 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P23109 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name AMPD1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2244 bp
ATGCCTCTGTTCAAACTCCCAGCTGAAGAGAAACAAATTGATGATGCAATGCGCAACTTT
GCTGAAAAAGTGTTTGCCTCTGAAGTCAAAGATGAAGGAGGTCGTCAGGAGATTTCCCCC
TTTGATGTGGATGAGATCTGTCCGATTTCTCATCATGAGATGCAAGCACACATATTCCAT
CTGGAGACTCTGTCCACCTCCACAGAAGCCAGGAGAAAAAAGCGTTTCCAAGGACGGAAG
ACTGTTAATTTGTCCATTCCACTAAGTGAAACATCTTCCACCAAACTGTCCCACATTGAT
GAATACATTTCCTCATCTCCAACCTACCAGACCGTGCCTGATTTTCAGAGAGTGCAGATT
ACTGGTGACTATGCCTCTGGGGTTACAGTTGAAGATTTTGAAATTGTTTGCAAAGGTCTG
TATCGGGCACTATGCATACGTGAGAAATACATGCAGAAGTCGTTTCAGAGGTTCCCTAAA
ACCCCTTCCAAATACTTGCGGAACATTGATGGTGAGGCTTGGGTAGCAAATGAGAGCTTC
TATCCAGTCTTTACTCCTCCTGTGAAGAAGGGAGAGGACCCCTTCCGAACAGACAACCTT
CCTGAAAACCTGGGCTATCACCTCAAAATGAAGGACGGTGTAGTTTACGTCTATCCTAAT
GAAGCAGCAGTCAGCAAAGATGAGCCTAAGCCACTTCCTTACCCAAATCTGGACACCTTC
TTAGACGATATGAATTTTTTACTTGCTTTAATTGCTCAAGGACCTGTTAAGACCTATACC
CACCGGCGCCTGAAGTTCCTCTCCTCGAAGTTCCAGGTCCATCAGATGCTTAACGAGATG
GACGAGTTAAAGGAGCTGAAAAACAACCCCCACCGAGATTTTTATAACTGCAGGAAGGTG
GACACCCATATCCATGCAGCCGCTTGCATGAACCAGAAACATCTGCTGCGTTTTATTAAG
AAATCTTACCAAATTGATGCTGACAGAGTGGTCTATAGCACCAAAGAGAAGAATCTGACC
CTAAAGGAACTTTTTGCTAAATTAAAAATGCATCCTTATGACCTGACTGTTGATTCTCTG
GATGTTCATGCTGGACGCCAGACCTTCCAGCGTTTTGATAAGTTCAATGACAAATATAAT
CCTGTAGGAGCAAGTGAGCTACGGGACCTCTACTTGAAGACAGACAATTACATTAATGGG
GAATATTTTGCCACTATCATCAAGGAGGTAGGTGCGGACCTGGTGGAGGCCAAGTACCAG
CATGCTGAGCCCCGCCTGTCCATCTATGGCCGCAGTCCTGATGAGTGGAGCAAACTCTCC
TCCTGGTTCGTCTGCAATCGCATCCACTGCCCCAACATGACATGGATGATCCAGGTTCCC
AGGATCTATGATGTGTTCCGTTCCAAGAATTTCCTTCCACATTTTGGAAAAATGCTGGAG
AATATTTTCATGCCAGTGTTTGAGGCCACCATCAACCCCCAGGCTGACCCAGAACTCAGT
GTCTTCCTCAAGCATATCACTGGCTTTGACAGTGTGGATGATGAGTCCAAACACAGTGGC
CACATGTTCTCCTCCAAGAGTCCCAAGCCCCAGGAGTGGACATTGGAAAAGAATCCATCT
TACACTTACTATGCCTACTACATGTATGCAAACATCATGGTGCTCAACAGCCTGAGAAAG
GAACGAGGCATGAATACGTTTCTGTTCCGACCTCACTGTGGAGAAGCTGGAGCCCTCACC
CATCTCATGACAGCATTCATGATAGCAGATGATATCTCTCATGGCCTAAATTTAAAAAAG
AGTCCCGTGCTACAGTACTTGTTTTTCTTAGCCCAAATTCCCATCGCCATGTCACCACTA
AGTAACAATAGCCTATTTCTAGAGTATGCCAAAAATCCTTTTTTGGATTTCCTTCAGAAA
GGGCTAATGATCTCACTGTCTACAGATGACCCAATGCAATTCCACTTTACCAAGGAGCCC
CTAATGGAAGAATATGCTATTGCTGCACAAGTCTTCAAGCTGAGCACCTGTGATATGTGC
GAAGTGGCAAGGAACAGTGTCTTGCAGTGTGGAATTTCTCATGAGGAGAAAGTAAAGTTT
CTGGGCGACAATTACCTTGAGGAAGGCCCTGCTGGAAATGATATCCGGAGGACAAATGTA
GCCCAAATCCGCATGGCCTATCGCTATGAAACCTGGTGTTATGAACTCAATTTAATTGCT
GAGGGTCTTAAATCAACAGAATAA
Enzyme 14 GenBank Gene ID M37931 Link Image
Enzyme 14 GeneCard ID AMPD1 Link Image
Enzyme 14 GenAtlas ID AMPD1 Link Image
Enzyme 14 HGNC ID HGNC:468 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 1p13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Sabina RL, Morisaki T, Clarke P, Eddy R, Shows TB, Morton CC, Holmes EW: Characterization of the human and rat myoadenylate deaminase genes. J Biol Chem. 1990 Jun 5;265(16):9423-33. [PubMed Link Image]
  2. Sabina RL, Fishbein WN, Pezeshkpour G, Clarke PR, Holmes EW: Molecular analysis of the myoadenylate deaminase deficiencies. Neurology. 1992 Jan;42(1):170-9. [PubMed Link Image]
  3. Morisaki T, Gross M, Morisaki H, Pongratz D, Zollner N, Holmes EW: Molecular basis of AMP deaminase deficiency in skeletal muscle. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6457-61. [PubMed Link Image]
  4. Morisaki H, Higuchi I, Abe M, Osame M, Morisaki T: First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient. Hum Mutat. 2000 Dec;16(6):467-72. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5951
Enzyme 15 Name GMP reductase 2
Enzyme 15 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 2
  2. Guanosine monophosphate reductase 2
Enzyme 15 Gene Name GMPR2
Enzyme 15 Protein Sequence >GMP reductase 2
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGT
FEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI
PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI
GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM
LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGD
VEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
Enzyme 15 Number of Residues 348
Enzyme 15 Molecular Weight 37875
Enzyme 15 Theoretical pI 7.25
Enzyme 15 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 15 General Function Nucleotide transport and metabolism
Enzyme 15 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation
Enzyme 15 Pathways
Enzyme 15 Reactions
  • inosine 5'-phosphate + ammonia + NADP+ = guanosine 5'-phosphate + NADPH + H+
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 23451216 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9P2T1 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GMPR2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1047 bp
ATGCCTCATATTGACAACGATGTGAAACTGGACTTCAAGGATGTCCTTTTGAGGCCCAAA
CGCAGTACCCTTAAGTCTCGAAGTGAGGTGGATCTCACAAGATCCTTTTCATTTCGGAAC
TCAAAGCAGACATACTCTGGGGTTCCCATCATTGCTGCCAATATGGATACTGTGGGCACC
TTTGAGATGGCCAAGGTTCTCTGTAAGTTCTCTCTCTTCACTGCTGTCCATAAGCACTAT
AGCCTCGTTCAGTGGCAAGAGTTTGCTGGCCAGAATCCTGACTGTCTTGAGCATCTGGCT
GCCAGCTCAGGCACAGGCTCTTCTGACTTTGAGCAGCTGGAACAGATCCTGGAAGCTATT
CCCCAGGTGAAGTATATATGCCTGGATGTGGCAAATGGCTACTCTGAACACTTTGTTGAA
TTTGTAAAAGATGTACGGAAGCGCTTCCCCCAGCACACCATCATGGCAGGGAATGTGGTA
ACAGGAGAGATGGTAGAAGAGCTCATCCTTTCTGGGGCTGACATCATCAAAGTGGGAATT
GGGCCAGGCTCTGTGTGTACTACTCGGAAGAAAACTGGAGTGGGGTATCCACAGCTCAGC
GCAGTGATGGAGTGTGCAGATGCTGCTCATGGCCTCAAAGGCCACATCATTTCAGATGGA
GGTTGCAGCTGTCCTGGGGATGTGGCCAAGGCTTTTGGGGCAGGAGCTGACTTCGTGATG
CTGGGTGGCATGCTGGCTGGGCACAGTGAGTCAGGTGGTGAGCTCATCGAGAGGGATGGC
AAGAAGTACAAGCTCTTCTATGGAATGAGTTCTGAAATGGCCATGAAGAAGTATGCTGGG
GGCGTGGCTGAGTACAGAGCCTCAGAGGGAAAGACAGTGGAAGTTCCTTTTAAAGGAGAT
GTGGAACATACCATCCGAGACATCCTAGGAGGGATCCGCTCTACGTGTACCTATGTGGGA
GCAGCTAAGCTCAAAGAGTTGAGCAGGAGAACTACCTTCATCCGAGTCACCCAGCAGGTG
AATCCAATCTTCAGTGAGGCGTGCTAG
Enzyme 15 GenBank Gene ID AF419346 Link Image
Enzyme 15 GeneCard ID GMPR2 Link Image
Enzyme 15 GenAtlas ID GMPR2 Link Image
Enzyme 15 HGNC ID HGNC:4377 Link Image
Enzyme 15 Chromosome Location 14
Enzyme 15 Locus 14q12
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y: NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5958
Enzyme 16 Name GMP reductase 1
Enzyme 16 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 1
  2. Guanosine monophosphate reductase 1
Enzyme 16 Gene Name GMPR
Enzyme 16 Protein Sequence >GMP reductase 1
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Enzyme 16 Number of Residues 345
Enzyme 16 Molecular Weight 37419
Enzyme 16 Theoretical pI 7.08
Enzyme 16 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 16 General Function Nucleotide transport and metabolism
Enzyme 16 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides
Enzyme 16 Pathways
Enzyme 16 Reactions
  • inosine 5'-phosphate + ammonia + NADP+ = guanosine 5'-phosphate + NADPH + H+
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 529232 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P36959 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name GMPR1_HUMAN Link Image
Enzyme 16 PDB ID 2BLE Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >87 bp
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGATGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAG
Enzyme 16 GenBank Gene ID L35304 Link Image
Enzyme 16 GeneCard ID GMPR Link Image
Enzyme 16 GenAtlas ID GMPR Link Image
Enzyme 16 HGNC ID HGNC:4376 Link Image
Enzyme 16 Chromosome Location 6
Enzyme 16 Locus 6p23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed Link Image]
  2. Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Kondoh T, Kanno H, Chang LF, Yoshida A: Identification of common variant alleles of the human guanosine monophosphate reductase gene. Hum Genet. 1991 Dec;88(2):225-7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6163
Enzyme 17 Name Inosine-5'-monophosphate dehydrogenase 2
Enzyme 17 Synonyms
  1. IMP dehydrogenase 2
  2. IMPDH-II
  3. IMPD 2
Enzyme 17 Gene Name IMPDH2
Enzyme 17 Protein Sequence >Inosine-5'-monophosphate dehydrogenase 2
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKIT
LKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVV
LSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMT
KREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDA
KKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVI
GGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVP
VIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAM
DKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR
AMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Enzyme 17 Number of Residues 514
Enzyme 17 Molecular Weight 55806
Enzyme 17 Theoretical pI 6.90
Enzyme 17 GO Classification
Function
  • IMP dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • GMP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 17 General Function Nucleotide transport and metabolism
Enzyme 17 Specific Function Rate limiting enzyme in the de novo synthesis of guanine nucleotides and therefore is involved in the regulation of cell growth. It may also have a role in the development of malignancy and the growth progression of some tumors
Enzyme 17 Pathways
Enzyme 17 Reactions
  • inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH + H+
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 307066 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P12268 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name IMDH2_HUMAN Link Image
Enzyme 17 PDB ID 1NFB Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1545 bp
ATGGCCGACTACCTGATTAGTGGGGGCACGTCCTACGTGCCAGACGACGGACTCACAGCA
CAGCAGCTCTTCAACTGCGGAGACGGCCTCACCTACAATGACTTTCTCATTCTCCCTGGG
TACATCGACTTCACTGCAGACCAGGTGGACCTGACTTCTGCTCTGACCAAGAAAATCACT
CTTAAGACCCCACTGGTTTCCTCTCCCATGGACACAGTCACAGAGGCTGGGATGGCCATA
GCAATGGCGCTTACAGGCGGTATTGGCTTCATCCACCACAACTGTACACCTGAATTCCAG
GCCAATGAAGTTCGGAAAGTGAAGAAATATGAACAGGGATTCATCACAGACCCTGTGGTC
CTCAGCCCCAAGGATCGCGTGCGGGATGTTTTTGAGGCCAAGGCCCGGCATGGTTTCTGC
GGTATCCCAATCACAGACACAGGCCGGATGGGGAGCCGCTTGGTGGGCATCATCTCCTCC
AGGGACATTGATTTTCTCAAAGAGGAGGAACATGACTGTTTCTTGGAAGAGATAATGACA
AAGAGGGAAGACTTGGTGGTAGCCCCCCGCAGCATCACACTGAAGGAGGCAAATGAAATT
CTGCAGCGCAGCAAGAAGGGAAAGTTGCCCATTGTAAATGAAGATGATGAGCTTGTGGCC
ATCATTGCCCGGACAGACCTGAAGAAGAATCGGGACTACCCACTAGCCTCCAAAGATGCC
AAGAAACAGCTGCTGTGTGGGGCAGCCATTGGCACTCATGAGGATGACAAGTATAGGCTG
GACTTGCTCGCCCAGGCTGGTGTGGATGTAGTGGTTTTGGACTCTTCCCAGGGAAATTCC
ATCTTCCAGATCAATATGATCAAGTACATCAAAGACAAATACCCTAATCTCCAAGTCATT
GGAGGCAATGTGGTCACTGCTGCCCAGGCCAAGAACCTCATTGATGCAGGTGTGGATGCC
CTGCGGGTGGGCATGGGAAGTGGCTCCATCTGCATTACGCAGGAAGTGCTGGCCTGTGGG
CGGCCCCAAGCAACAGCAGTGTACAAGGTGTCAGAGTATGCACGGCGCTTTGGTGTTCCG
GTCATTGCTGATGGAGGAATCCAAAATGTGGGTCATATTGCGAAAGCCTTGGCCCTTGGG
GCCTCCACAGTCATGATGGGCTCTCTCCTGGCTGCCACCACTGAGGCCCCTGGTGAATAC
TTCTTTTCCGATGGGATCCGGCTAAAGAAATATCGCGGTATGGGTTCTCTCGATGCCATG
GACAAGCACCTCAGCAGCCAGAACAGATATTTCAGTGAAGCTGACAAAATCAAAGTGGCC
CAGGGAGTGTCTGGTGCTGTGCAGGACAAAGGGTCAATCCACAAATTTGTCCCTTACCTG
ATTGCTGGCATCCAACACTCATGCCAGGACATTGGTGCCAAGAGCTTGACCCAAGTCCGA
GCCATGATGTACTCTGGGGAGCTTAAGTTTGAGAAGAGAACGTCCTCAGCCCAGGTGGAA
GGTGGCGTCCATAGCCTCCATTCGTATGAGAAGCGGCTTTTCTGA
Enzyme 17 GenBank Gene ID J04208 Link Image
Enzyme 17 GeneCard ID IMPDH2 Link Image
Enzyme 17 GenAtlas ID IMPDH2 Link Image
Enzyme 17 HGNC ID HGNC:6053 Link Image
Enzyme 17 Chromosome Location 3
Enzyme 17 Locus 3p21.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Collart FR, Huberman E: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs. J Biol Chem. 1988 Oct 25;263(30):15769-72. [PubMed Link Image]
  2. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K: Two distinct cDNAs for human IMP dehydrogenase. J Biol Chem. 1990 Mar 25;265(9):5292-5. [PubMed Link Image]
  3. Glesne DA, Huberman E: Cloning and sequence of the human type II IMP dehydrogenase gene. Biochem Biophys Res Commun. 1994 Nov 30;205(1):537-44. [PubMed Link Image]
  4. Zimmermann AG, Spychala J, Mitchell BS: Characterization of the human inosine-5'-monophosphate dehydrogenase type II gene. J Biol Chem. 1995 Mar 24;270(12):6808-14. [PubMed Link Image]
  5. Glesne D, Collart F, Varkony T, Drabkin H, Huberman E: Chromosomal localization and structure of the human type II IMP dehydrogenase gene (IMPDH2). Genomics. 1993 Apr;16(1):274-7. [PubMed Link Image]
  6. Hager PW, Collart FR, Huberman E, Mitchell BS: Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding. Biochem Pharmacol. 1995 May 11;49(9):1323-9. [PubMed Link Image]
  7. Colby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM: Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3531-6. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6164
Enzyme 18 Name Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
Enzyme 18 Synonyms
  1. 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
  2. AICAR transformylase
  3. IMP cyclohydrolase
  4. Inosinicase
  5. IMP synthetase
  6. ATIC]
Enzyme 18 Gene Name ATIC
Enzyme 18 Protein Sequence >Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEM
LGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEA
VEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFT
HTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINL
CDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPIS
AAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNG
NYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIV
ATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKT
GVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDA
FFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Enzyme 18 Number of Residues 592
Enzyme 18 Molecular Weight 64616
Enzyme 18 Theoretical pI 6.70
Enzyme 18 GO Classification
Function
  • IMP cyclohydrolase activity
  • catalytic activity
  • cyclohydrolase activity
  • glycine hydroxymethyltransferase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
  • hydroxymethyl-, formyl- and related transferase activity
  • methyltransferase activity
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
Enzyme 18 General Function Nucleotide transport and metabolism
Enzyme 18 Specific Function 10-formyltetrahydrofolate + 5-amino-1-(5- phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Enzyme 18 Pathways
Enzyme 18 Reactions
  • IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 1263196 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P31939 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PUR9_HUMAN Link Image
Enzyme 18 PDB ID 1P4R Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1776 bp
ATGTCTTCTCTCTCAGCCTTATTTAGTGTCTCTGACAAAACCGGCCTTGTGGAATTTGCA
AGAAACCTGACCGCTCTTGGTTTGAACCTGGTCGCTTCCGGAGGGACTGCAAAAGCTCTC
AGGGATGCTGGTCTGGCAGTCAGAGATGTCTCTGAGTTGACGGGATTTCCTGAAATGTTG
GGGGGACGTGTGAAAACTTTGCATCCTGCAGTCCATGCTGGAATCCTAGCTCGTAATATT
CCAGAAGATAATGCTGACATGGCCAGACTTGATTTCAATCTTATAAGAGTTGTCGCCTGC
AATCTCTATCCCTTTGTAAAGACAGTGGCTTCTCCAGGTGTAACTGTTGAGGAGGCTGTG
GAGCAAATTGACATTGGTGGAGTAACCTTACTGAGAGCTGCAGCCAAAAACCACGCTCGA
GTGACAGTGGTGTGTGAACCAGAGGACTATGTGGTGGTGTCCACGGAGATGCAGAGCTCC
GAGAGTAAGGGCACCTCCTTGGAGACTAGACGCCAGTTAGCCTTGAAGGCATTCACTCAT
ACGGCACAATATGATGAAGCAATTTCAGATTATTTCAGGAAACAGTACAGCAAAGGCGTA
TCTCAGATGCCCTTGAGATATGGAATGAACCCACATCAGACCCCTGCCCAGCTGTACACA
CTGCAGCCCAAGCTTCCCATCACAGTTCTAAATGGAGCCCCTGGATTTATAAACTTGTGC
GATGCTTTGAACGCCTGGCAGCTGGTGAAGGAACTCAAGGAGGCTTTAGGTATTCCAGCC
GCTGCCTCTTTCAAACATGTCAGCCCAGCAGGTGCTGCTGTTGGAATTCCACTCAGTGAA
GATGAGGCCAAAGTCTGCATGGTTTATGATCTCTATAAAACCCTCACACCCATCTCAGCG
GCATATGCAAGAGCAAGAGGGGCTGATAGGATGTCTTCATTTGGTGATTTTGTTGCATTG
TCTGATGTTTGTGATGTACCAACTGCAAAAATTATTTCCAGAGAAGTATCTGATGGTATA
ATTGCCCCAGGATATGAAGAAGAAGCCTTGACAATACTTTCCAAAAAGAAAAATGGAAAC
TATTGTGTCCTTCAGATGGACCAATCTTACAAACCAGATGAAAATGAAGTTCGAACTCTC
TTTGGTCTTCATTTAAGCCAGAAGAGAAATAATGGTGTCGTCGACAAGTCATTATTTAGC
AATGTTGTTACCAAAAATAAAGATTTGCCAGAGTCTGCCCTCCGAGACCTCATCGTAGCC
ACCATTGCTGTCAAGTACACTCAGTCTAACTCTGTGTGCTACGCCAAGAACGGGCAGGTT
ATCGGCATTGGAGCAGGACAGCAGTCTCGTATACACTGCACTCGCCTTGCAGGAGATAAG
GCAAACTATTGGTGGCTTAGACACCATCCACAAGTGCTTTCGATGAAGTTTAAAACAGGA
GTGAAGAGAGCAGAAATCTCCAATGCCATCGATCAATATGTGACTGGAACCATTGGCGAG
GATGAAGATTTGATAAAGTGGAAGGCACTGTTTGAGGAAGTCCCTGAGTTACTCACTGAG
GCAGAGAAGAAGGAATGGGTTGAGAAACTGACTGAAGTTTCTATCAGCTCTGATGCCTTC
TTCCCTTTCCGAGATAACGTAGACAGAGCTAAAAGGAGTGGTGTGGCGTACATTGCGGCT
CCCTCCGGTTCTGCTGCTGACAAAGTTGTGATTGAGGCCTGCGACGAACTGGGAATCATC
CTCGCTCATACGAACCTTCGGCTCTTCCACCACTGA
Enzyme 18 GenBank Gene ID U37436 Link Image
Enzyme 18 GeneCard ID ATIC Link Image
Enzyme 18 GenAtlas ID ATIC Link Image
Enzyme 18 HGNC ID HGNC:794 Link Image
Enzyme 18 Chromosome Location 2
Enzyme 18 Locus 2q35
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Rayl EA, Moroson BA, Beardsley GP: The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping. J Biol Chem. 1996 Jan 26;271(4):2225-33. [PubMed Link Image]
  2. Yamauchi M, Seki N, Mita K, Saito T, Tsuji S, Hongo E, Morimyo M, Shiomi T, Koyama H, Ayusawa D: Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript. DNA Res. 1995 Dec 31;2(6):269-75. [PubMed Link Image]
  3. Sugita T, Aya H, Ueno M, Ishizuka T, Kawashima K: Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase. J Biochem (Tokyo). 1997 Aug;122(2):309-13. [PubMed Link Image]
  4. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6166
Enzyme 19 Name Adenylosuccinate synthetase isozyme 1
Enzyme 19 Synonyms
  1. IMP--aspartate ligase 1
  2. AdSS 1
  3. AMPSase 1
Enzyme 19 Gene Name ADSSL1
Enzyme 19 Protein Sequence >Adenylosuccinate synthetase isozyme 1
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 19 Number of Residues 457
Enzyme 19 Molecular Weight 50209
Enzyme 19 Theoretical pI 8.85
Enzyme 19 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
Enzyme 19 General Function Nucleotide transport and metabolism
Enzyme 19 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 19 Pathways
Enzyme 19 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 21303413 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 19 PDB ID 1MF1 Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1374 bp
ATGTCGGGGACCCGAGCCTCCAACGACCGGCCCCCCGGCGCAGGCGGCGTCAAGCGGGGG
CGGCTGCAGCAGGAGGCGGCGGCGACCGGCTCCCGCGTGACGGTGGTGCTGGGCGCGCAG
TGGGGGGACGAGGGCAAAGGCAAGGTGGTGGACCTGCTGGCCACGGACGCCGACATCATC
AGCCGCTGCCAGGGGGGCAACAACGCCGGCCACACGGTGGTGGTGGATGGGAAAGAGTAC
GACTTCCACCTGCTGCCCAGCGGCATCATCAACACCAAGGCCGTGTCCTTCATTGGCAAC
GGGGTGGTCATCCACTTGCCAGGCTTGTTTGAGGAAGCAGAGAAGAATGAAAAGAAAGGC
CTGAAGGACTGGGAGAAGAGGCTCATCATCTCTGACAGAGCCCACCTTGTGTTTGATTTT
CACCAGGCTGTCGACGGACTTCAGGAAGTGCAGCGCCAGGCACAAGAGGGGAAGAATATA
GGCACCACCAAGAAGGGAATCGGACCAACCTACTCTTCCAAAGCTGCCCGGACAGGCCTC
CGCATCTGCGACCTCCTGTCAGATTTTGATGAGTTTTCCTCCAGATTCAAGAACCTGGCC
CACCAGCACCAGTCGATGTTCCCCACCCTGGAAATAGACATTGAAGGCCAACTCAAAAGG
CTCAAGGGCTTTGCTGAGCGGATCAGACCCATGGTCCGAGATGGTGTTTACTTTATGTAT
GAGGCACTCCACGGCCCCCCCAAGAAGATCCTGGTGGAGGGTGCCAACGCCGCCCTCCTC
GACATTGACTTCGGGACCTACCCCTTTGTGACTTCATCCAACTGCACCGTGGGCGGTGTG
TGCACGGGCCTGGGCATCCCCCCGCAGAACATAGGTGACGTGTATGGCGTGGTGAAAGCC
TATACCACACGTGTGGGCATCGGGGCCTTCCCCACCGAGCAGATCAACGAGATTGGAGGC
CTGCTGCAGACCCGCGGCCACGAGTGGGGAGTGACCACAGGCAGGAAGAGGCGCTGCGGC
TGGCTCGACCTGATGATTCTAAGATATGCTCACATGGTCAACGGATTCACTGCGCTGGCC
CTGACGAAGCTGGACATCCTGGACGTACTGGGTGAGGTTAAAGTCGGTGTCTCATACAAG
CTGAACGGGAAAAGGATTCCCTATTTCCCAGCTAACCAGGAGATGCTTCAGAAGGTCGAA
GTTGAGTATGAAACGCTGCCTGGGTGGAAAGCAGACACCACAGGCGCCAGGAGGTGGGAG
GACCTGCCCCCACAGGCCCAGAACTACATCCGCTTTGTGGAGAATCACGTGGGAGTCGCA
GTCAAATGGGTTGGTGTTGGCAAGTCAAGAGAGTCGATGATCCAGCTGTTTTAG
Enzyme 19 GenBank Gene ID AY037159 Link Image
Enzyme 19 GeneCard ID ADSSL1 Link Image
Enzyme 19 GenAtlas ID ADSSL1 Link Image
Enzyme 19 HGNC ID HGNC:20093 Link Image
Enzyme 19 Chromosome Location 14
Enzyme 19 Locus 14q32.33
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 8749
Enzyme 20 Name Cytosolic 5'-nucleotidase III
Enzyme 20 Synonyms
  1. cN-III
  2. Pyrimidine 5'- nucleotidase 1
  3. P5'N-1
  4. P5N-1
  5. PN-I
  6. Uridine 5'-monophosphate hydrolase 1
  7. p36
Enzyme 20 Gene Name NT5C3
Enzyme 20 Protein Sequence >Cytosolic 5'-nucleotidase III
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 20 Number of Residues 336
Enzyme 20 Molecular Weight 37949
Enzyme 20 Theoretical pI 7.15
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-32
Enzyme 20 Transmembrane Regions
  • 13-35
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 11245474 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >861 bp
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 20 GenBank Gene ID AF312735 Link Image
Enzyme 20 GeneCard ID NT5C3 Link Image
Enzyme 20 GenAtlas ID NT5C3 Link Image
Enzyme 20 HGNC ID HGNC:17820 Link Image
Enzyme 20 Chromosome Location 7
Enzyme 20 Locus 7p14.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  4. Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 8772
Enzyme 21 Name ENTPD4 protein
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name ENTPD4
Enzyme 21 Protein Sequence >ENTPD4 protein
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTEEVAKNLLAEFNLG
CDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPC
LPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEF
YGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKY
QCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRKIGMLII
PCSGGCPKLCCAVWQPPPYGATKHLQCAAWN
Enzyme 21 Number of Residues 571
Enzyme 21 Molecular Weight 64854
Enzyme 21 Theoretical pI 8.13
Enzyme 21 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-46
Enzyme 21 Transmembrane Regions
  • 35-54
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 21759777 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8NE73 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name Q8NE73_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1716 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTGGGA
TGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGGTTT
GGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAAAAG
AACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCCTGC
CTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGAGGG
ACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAACGAG
ACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAATTC
TATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGACTAC
AATGCTGCTAAATTTACTAAAGCTGCAAAGGATTATTGTGCAACAAAGTGGTCCATTTTG
CGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAGTAT
CAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCTGTC
AACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACCCTT
GGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGGAAAATAGGGATGCTGATAATA
CCTTGCTCAGGGGGTTGTCCAAAGCTGTGTTGTGCAGTATGGCAGCCACCACCATATGGG
GCCACCAAACACTTGCAATGTGCTGCTTGGAATTGA
Enzyme 21 GenBank Gene ID BC034477 Link Image
Enzyme 21 GeneCard ID ENTPD4 Link Image
Enzyme 21 GenAtlas ID ENTPD4 Link Image
Enzyme 21 HGNC ID HGNC:14573 Link Image
Enzyme 21 Chromosome Location 8
Enzyme 21 Locus 8p21.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 13095
Enzyme 22 Name IMP
Enzyme 22 Synonyms
  1. Inosine monophosphatedehydrogenase 1
Enzyme 22 Gene Name IMPDH1
Enzyme 22 Protein Sequence >IMP
MEGPLTPPPLQGGGAAAVPEPGARQHPGHETAAQRYSARLLQAGYEPESPRLDLATHPTT
PRSELSSVVLLAGVGVQMDRLRRASMADYLISGGTGYVPEDGLTAQQLFASADGLTYNDF
LILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNC
TPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLV
GIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDC
DELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDS
SQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQE
VMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTE
APGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQK
FVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
Enzyme 22 Number of Residues 599
Enzyme 22 Molecular Weight 64321
Enzyme 22 Theoretical pI 7.03
Enzyme 22 GO Classification
Function
  • IMP dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • GMP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 22 General Function Nucleotide transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID A4D0Z6 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name A4D0Z6_HUMAN Link Image
Enzyme 22 PDB ID 1JCN Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence Not Available
Enzyme 22 GenBank Gene ID CH236947 Link Image
Enzyme 22 GeneCard ID A4D0Z6 Link Image
Enzyme 22 GenAtlas ID IMPDH1 Link Image
Enzyme 22 HGNC ID HGNC:6052 Link Image
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 13379
Enzyme 23 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 23 Synonyms
  1. NTPDase 8
  2. NTPDase8
  3. E-NTPDase 8
Enzyme 23 Gene Name ENTPD8
Enzyme 23 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 23 Number of Residues 495
Enzyme 23 Molecular Weight 53904
Enzyme 23 Theoretical pI 4.96
Enzyme 23 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085] ALL_REAC R00085
  • (other) R00086 R00122 R00155 R00159 R00328 R00335 R00514 R00569 R00719 R00961 R02092 R02095
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 9-29 472-492
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 59003409 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCCGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTGCAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 23 GenBank Gene ID AY903953 Link Image
Enzyme 23 GeneCard ID Q5MY95 Link Image
Enzyme 23 GenAtlas ID ENTPD8 Link Image
Enzyme 23 HGNC ID HGNC:24860 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 15061
Enzyme 24 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name Not Available
Enzyme 24 Protein Sequence >cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
Enzyme 24 Number of Residues 561
Enzyme 24 Molecular Weight 64960
Enzyme 24 Theoretical pI 6.05
Enzyme 24 GO Classification Not Available
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function Not Available
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 158256766 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1686 bp
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 24 GenBank Gene ID AK291667 Link Image
Enzyme 24 GeneCard ID A8K6K2 Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs Not Available
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15072
Enzyme 25 Name Adenosine monophosphate deaminase (Isoform E) (Adenosine monophosphate deaminase (Isoform E), isoform CRA_b) (cDNA FLJ76195, highly similar to Homo sapiens adenosine monophosphate deaminase (isoform E) (AMPD3),mRNA)
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name AMPD3
Enzyme 25 Protein Sequence >Adenosine monophosphate deaminase (Isoform E) (Adenosine monophosphate deaminase (Isoform E), isoform CRA_b) (cDNA FLJ76195, highly similar to Homo sapiens adenosine monophosphate deaminase (isoform E) (AMPD3),mRNA)
MALSSEPAEMPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQ
KEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTP
VVTGATSLPTPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYH
RFPRITSQYLGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFV
YDNKKMLEHQEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEML
NEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKRGR
KITLRQVFDGLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENY
LGGEYFARMVKEVARELEESKYQYSEPRLSIYGRSPEEWPNLAYWFIQHKVYSPNMRWII
QVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESK
HSDHMFSDKSPNPDVWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAG
SITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREF
LHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEK
QKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTN
Enzyme 25 Number of Residues 776
Enzyme 25 Molecular Weight 89729
Enzyme 25 Theoretical pI 6.84
Enzyme 25 GO Classification
Function
  • AMP deaminase activity
  • catalytic activity
  • deaminase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 116496603 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID A0AUX0 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name A0AUX0_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2331 bp
ATGGCCCTGTCGTCCGAACCCGCTGAGATGCCGCGGCAGTTTCCCAAGCTGAACATCTCT
GAAGTGGATGAGCAAGTCCGGCTCCTGGCGGAGAAGGTGTTTGCTAAAGTGCTCCGAGAA
GAGGACAGCAAAGATGCCCTGTCCCTGTTCACTGTCCCAGAGGACTGCCCCATCGGGCAA
AAGGAAGCCAAGGAGAGGGAGCTGCAGAAGGAGCTGGCAGAGCAGAAGTCTGTGGAGACC
GCAAAAAGAAAGAAAAGTTTCAAGATGATTCGGTCCCAGTCCCTGTCTCTGCAAATGCCG
CCACAGCAAGATTGGAAGGGCCCCCCGGCAGCCAGTCCGGCCATGTCTCCCACAACCCCT
GTGGTCACTGGAGCCACTTCCCTGCCCACGCCAGCACCCTATGCCATGCCTGAGTTCCAG
CGGGTCACCATCAGCGGAGATTACTGTGCCGGGATCACTTTGGAGGACTATGAGCAGGCA
GCCAAGAGTCTGGCCAAGGCCCTAATGATCCGGGAGAAGTATGCGCGGCTCGCCTACCAC
CGCTTCCCGCGGATCACATCCCAGTACCTGGGTCATCCGCGGGCGGATACTGCACCTCCG
GAAGAGGGCCTTCCAGACTTCCACCCTCCTCCACTGCCCCAGGAAGACCCCTACTGCCTG
GATGATGCACCCCCCAACCTGGATTACTTGGTCCACATGCAGGGGGGCATCCTCTTTGTG
TATGATAACAAGAAGATGCTGGAGCACCAGGAGCCGCACAGCCTACCCTACCCCGACCTG
GAGACCTACACGGTGGACATGAGCCACATCCTGGCTCTCATCACCGATGGCCCCACGAAA
ACCTATTGTCACCGGCGACTGAACTTTCTGGAATCCAAGTTCAGCCTTCATGAGATGTTA
AACGAAATGTCCGAGTTCAAAGAGTTGAAGAGTAACCCCCACCGGGACTTCTATAACGTG
AGAAAGGTGGACACACACATCCATGCGGCCGCCTGCATGAACCAAAAGCATCTGCTGCGC
TTCATCAAGCACACATACCAGACGGAGCCTGACAGGACTGTGGCAGAGAAGCGGGGCCGG
AAGATCACCCTGCGGCAGGTGTTTGACGGCCTGCACATGGACCCCTACGACCTCACTGTG
GACTCACTGGATGTCCACGCGGGCCGGCAGACATTCCACCGCTTTGACAAGTTCAACTCC
AAATACAACCCTGTGGGGGCCAGTGAGCTGCGTGACCTGTATTTGAAAACTGAAAACTAT
CTGGGAGGAGAGTACTTTGCTCGGATGGTCAAGGAGGTTGCCCGGGAGCTGGAGGAGAGC
AAGTACCAGTACTCAGAGCCACGGCTCTCCATCTACGGCCGCAGTCCTGAGGAGTGGCCC
AACCTGGCCTACTGGTTCATCCAGCACAAGGTCTACTCTCCCAACATGCGCTGGATCATC
CAGGTGCCCCGGATTTATGACATATTTAGGTCAAAGAAGCTGCTGCCAAACTTTGGGAAG
ATGCTGGAGAACATCTTCCTGCCCCTTTTCAAGGCCACTATCAACCCCCAAGATCATCGA
GAGCTTCACCTCTTCCTTAAATATGTGACGGGGTTTGACAGCGTGGATGATGAGTCCAAG
CACAGCGACCACATGTTTTCCGACAAGAGCCCAAACCCGGACGTCTGGACCAGTGAGCAG
AACCCACCCTACAGCTACTACCTGTACTACATGTATGCCAACATCATGGTGCTCAACAAC
CTCCGCAGGGAGCGCGGCCTGAGCACGTTCCTGTTCCGGCCGCACTGTGGGGAAGCCGGC
TCCATCACCCACCTGGTGTCTGCCTTCCTCACTGCTGACAACATTTCCCACGGGCTGCTC
CTCAAGAAGAGTCCGGTATTGCAGTATCTCTACTACCTTGCTCAGATCCCCATTGCCATG
TCTCCTCTTAGCAACAACAGTTTGTTCCTCGAATATTCCAAGAACCCTCTGAGGGAATTC
CTACACAAGGGACTGCATGTTTCTCTTTCCACCGATGACCCCATGCAGTTCCACTACACG
AAGGAAGCACTTATGGAAGAATATGCCATTGCAGCTCAAGTGTGGAAGCTGAGCACCTGC
GACCTGTGTGAGATCGCCAGGAACAGCGTGCTGCAGAGCGGCCTCTCGCATCAGGAAAAG
CAAAAGTTTCTGGGACAAAATTATTATAAAGAAGGACCTGAAGGAAATGATATTCGAAAG
ACAAATGTGGCTCAGATCCGGATGGCATTCCGATATGAGACCTTATGCAATGAGCTCAGC
TTCCTGTCTGATGCTATGAAATCAGAAGAGATCACCGCCTTGACCAACTAG
Enzyme 25 GenBank Gene ID BC126118 Link Image
Enzyme 25 GeneCard ID A0AUX0 Link Image
Enzyme 25 GenAtlas ID AMPD3 Link Image
Enzyme 25 HGNC ID HGNC:470 Link Image
Enzyme 25 Chromosome Location 11
Enzyme 25 Locus 11p15
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15232
Enzyme 26 Name Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name DKFZp761J1915
Enzyme 26 Protein Sequence >Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
MQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYIKWHRATATQAFFSITRA
APGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQFTRPPRETPTLTHETFKA
LKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLKATAGLRLLPGEKAQKLL
QKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLKTPGGSSVGMLDLGGGST
QIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLMSARLAILGGVEGQPAKD
GKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARVSEVLQNRVHRTEEVKHV
DFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLETQPQSSPFSCMDLTYVS
LLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQKSPAS
Enzyme 26 Number of Residues 467
Enzyme 26 Molecular Weight 51160
Enzyme 26 Theoretical pI 9.14
Enzyme 26 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 50949564 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q8N3H3 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name Q8N3H3_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1404 bp
ATGCAGCCGCAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGC
CTGCGGGTGGCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTT
GCCTACATCAAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCA
GCCCCGGGGGCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGG
CACGAGGTCTTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTC
TTCCAGTTCACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCA
CTGAAGCCAGGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGG
GAACTACTGGATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTG
GTCCTCAAGGCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTG
CAGAAGGTGAAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCC
ATCATGAACGGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGC
AGCTTGAAAACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACT
CAGATCGCCTTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTG
ACGGCACTGCGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTC
GGGCTGATGTCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGAT
GGAAAGGAGTTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCA
GAAGTCACGTACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCT
GCCAGAGTGTCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTG
GACTTCTATGCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCG
GAGAAGGGAGGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGG
ACCCTGGAGACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGC
CTGCTACTCCAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATT
GACAATGTTGAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAAC
AGACAGAAGAGTCCAGCCTCATAG
Enzyme 26 GenBank Gene ID AL834158 Link Image
Enzyme 26 GeneCard ID Q8N3H3 Link Image
Enzyme 26 GenAtlas ID DKFZp761J1915 Link Image
Enzyme 26 HGNC ID HGNC:3368 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15233
Enzyme 27 Name Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name ENTPD5
Enzyme 27 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 27 Number of Residues 428
Enzyme 27 Molecular Weight 47518
Enzyme 27 Theoretical pI 6.29
Enzyme 27 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 120660392 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID A1L4C5 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name A1L4C5_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACCTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 27 GenBank Gene ID BC130485 Link Image
Enzyme 27 GeneCard ID A1L4C5 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location 14
Enzyme 27 Locus 14q24
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16422
Enzyme 28 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name Not Available
Enzyme 28 Protein Sequence >cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
Enzyme 28 Number of Residues 574
Enzyme 28 Molecular Weight 63396
Enzyme 28 Theoretical pI 7.04
Enzyme 28 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide catabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 28 General Function Nucleotide transport and metabolism
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK314661 Link Image
Enzyme 28 GeneCard ID B2RBH2 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs Not Available
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16437
Enzyme 29 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name ENTPD3
Enzyme 29 Protein Sequence >cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 29 Number of Residues 529
Enzyme 29 Molecular Weight 59106
Enzyme 29 Theoretical pI 6.40
Enzyme 29 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 29 General Function Not Available
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AK313322 Link Image
Enzyme 29 GeneCard ID B2R8D0 Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 16506
Enzyme 30 Name Adenylosuccinate synthetase
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name ADSS
Enzyme 30 Protein Sequence >Adenylosuccinate synthetase
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Enzyme 30 Number of Residues 456
Enzyme 30 Molecular Weight 50098
Enzyme 30 Theoretical pI 6.52
Enzyme 30 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
Enzyme 30 General Function Nucleotide transport and metabolism
Enzyme 30 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID B1AQM5 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name B1AQM5_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AL591594 Link Image
Enzyme 30 GeneCard ID B1AQM5 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available