We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Xanthosine (HMDB00299)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-07-27 12:44:33
Accession Number HMDB00299
Secondary Accession Numbers Not Available
Common Name Xanthosine
Description Biological Source: Prod. by guanine-free mutants of bacteria e.g. Bacillus subtilis, Aerobacter aerogenes. Also reported from seeds of Trifolium alexandrinum Physical Description: Prismatic cryst. (H2O) (Chemnetbase) The deamination product of guanosine Xanthosine monophosphate is an intermediate in purine metabolism, formed from IMP, and forming GMP.(Wikipedia) Xanthylic acid can be used in quantitative measurements of the Inosine monophosphate dehydrogenase enzyme activities in purine metabolism, as recommended to ensure optimal thiopurine therapy for children with acute lymphoblastic leukaemia (ALL). (PMID: 16725387)
Synonyms
  1. 3,9-Dihydro-9-D-ribofuranosyl-1H-purine-2,6-dione
  2. 3,9-Dihydro-9-b-D-ribofuranosyl-1H-purine-2,6-dione
  3. 9-D-Ribofuranosylxanthine
  4. 9-b-D-Ribofuranosylxanthine
  5. Xanthosine
  6. 3,9-Dihydro-9-delta-ribofuranosyl-1H-purine-2,6-dione
  7. 3,9-Dihydro-9-beta-delta-ribofuranosyl-1H-purine-2,6-dione
  8. 9-delta-Ribofuranosylxanthine
  9. 9-beta-delta-Ribofuranosylxanthine
Chemical IUPAC Name Xanthine-9b-D-ribofuranoside
Chemical Formula C10H12N4O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleoside Analogues
Sub Class
  • Miscellaneous nucleosides
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • phenol or hydroxyhetarene
  • aromatic compound
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 284.225
Monoisotopic Molecular Weight 284.075684
Isomeric SMILES OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC2=C1N=C(O)N=C2O
Canonical SMILES OCC1OC(C(O)C1O)N1C=NC2=C1N=C(O)N=C2O
KEGG Compound ID C01762 Link Image
BioCyc ID Not Available
BiGG ID 38352 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB00299 Link Image
Metagene Link HMDB00299 Link Image
METLIN ID 3408 Link Image
PubChem Compound 64959 Link Image
PubChem Substance 8189406 Link Image
ChEBI ID 18107 Link Image
CAS Registry Number 146-80-5
InChI Identifier InChI=1/C10H12N4O6/c15-1-3-5(16)6(17)9(20-3)14-2-11-4-7(14)12-10(19)13-8(4)18/h2-3,5-6,9,15-17H,1H2,(H2,12,13,18,19)/t3-,5-,6-,9-/m1/s1
Synthesis Reference Enei, Hitoshi; Sato, Katsuaki; Hirose, Yoshio. Xanthosine production by fermentation. Jpn. Kokai Tokkyo Koho (1975), 3 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 25.7 mg/mL [MEYLAN,WM et al. (1996)]; 27.8 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.60 [Predicted by ALOGPS]; -2.1 [Predicted by PubChem via XLOGP]; -1.80 [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 Not Available
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
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 5.08 +/- 0.30 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Urine
Value 0.59 +/- 0.36 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Liebich HM, Di Stefano C, Wixforth A, Schmid HR: Quantitation of urinary nucleosides by high-performance liquid chromatography. J Chromatogr A. 1997 Feb 28;763(1-2):193-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 0.99 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Liebich HM, Di Stefano C, Wixforth A, Schmid HR: Quantitation of urinary nucleosides by high-performance liquid chromatography. J Chromatogr A. 1997 Feb 28;763(1-2):193-7. [PubMed Link Image]
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Marti R, Nishigaki Y, Hirano M: Elevated plasma deoxyuridine in patients with thymidine phosphorylase deficiency. Biochem Biophys Res Commun. 2003 Mar 28;303(1):14-8. [PubMed Link Image]
  2. Dudley E, Lemiere F, Van Dongen W, Tuytten R, El-Sharkawi S, Brenton AG, Esmans EL, Newton RP: Analysis of urinary nucleosides. IV. Identification of urinary purine nucleosides by liquid chromatography/electrospray mass spectrometry. Rapid Commun Mass Spectrom. 2004;18(22):2730-8. [PubMed Link Image]
  3. Liebich HM, Di Stefano C, Wixforth A, Schmid HR: Quantitation of urinary nucleosides by high-performance liquid chromatography. J Chromatogr A. 1997 Feb 28;763(1-2):193-7. [PubMed 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. Inosine triphosphate pyrophosphatase
  6. Purine nucleoside phosphorylase
  7. Cytosolic 5'-nucleotidase III
  8. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  9. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
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 5668
Enzyme 5 Name Inosine triphosphate pyrophosphatase
Enzyme 5 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 5 Gene Name ITPA
Enzyme 5 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 5 Number of Residues 194
Enzyme 5 Molecular Weight 21446
Enzyme 5 Theoretical pI 5.34
Enzyme 5 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • A nucleoside triphosphate + H2O = a nucleotide + diphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 13398328 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
Enzyme 5 GenBank Gene ID AF219116 Link Image
Enzyme 5 GeneCard ID ITPA Link Image
Enzyme 5 GenAtlas ID ITPA Link Image
Enzyme 5 HGNC ID HGNC:6176 Link Image
Enzyme 5 Chromosome Location 20
Enzyme 5 Locus 20p
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5805
Enzyme 6 Name Purine nucleoside phosphorylase
Enzyme 6 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 6 Gene Name NP
Enzyme 6 Protein Sequence >Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 6 Number of Residues 289
Enzyme 6 Molecular Weight 32118
Enzyme 6 Theoretical pI 6.95
Enzyme 6 GO Classification
Function
  • catalytic activity
  • purine-nucleoside phosphorylase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 35565 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 6 PDB ID 1RT9 Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 6 GenBank Gene ID X00737 Link Image
Enzyme 6 GeneCard ID NP Link Image
Enzyme 6 GenAtlas ID NP Link Image
Enzyme 6 HGNC ID HGNC:7892 Link Image
Enzyme 6 Chromosome Location 14
Enzyme 6 Locus 14q13.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed Link Image]
  2. Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed Link Image]
  3. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  4. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed Link Image]
  5. Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed Link Image]
  6. Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 8749
Enzyme 7 Name Cytosolic 5'-nucleotidase III
Enzyme 7 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 7 Gene Name NT5C3
Enzyme 7 Protein Sequence >Cytosolic 5'-nucleotidase III
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 7 Number of Residues 336
Enzyme 7 Molecular Weight 37949
Enzyme 7 Theoretical pI 7.15
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-32
Enzyme 7 Transmembrane Regions
  • 13-35
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 11245474 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >861 bp
ATGATGCCAGAATTCCAGAAAAGTTCAGTTCGAATCAAGAACCCTACAAGAGTAGAAGAA
ATTATCTGTGGTCTTATCAAAGGAGGAGCTGCCAAACTTCAGATAATAACGGACTTTGAT
ATGACACTCAGTAGATTTTCATATAAAGGGAAAAGATGCCCAACATGTCATAATATCATT
GACAACTGTAAGCTGGTTACAGATGAATGTAGAAAAAAGTTATTGCAACTAAAGGAAAAA
TACTACGCTATTGAAGTTGATCCTGTTCTTACTGTAGAAGAGAAGTACCCTTATATGGTG
GAATGGTATACTAAATCACATGGTTTGCTTGTTCAGCAAGCTTTACCAAAAGCTAAACTT
AAAGAAATTGTGGCAGAATCTGACGTTATGCTCAAAGAAGGATATGAGAATTTCTTTGAT
AAGCTCCAACAACATAGCATCCCCGTGTTCATATTTTCGGCTGGAATCGGCGATGTACTA
GAGGAAGTTATTCGTCAAGCTGGTGTTTATCATCCCAATGTCAAAGTTGTGTCCAATTTT
ATGGATTTTGATGAAACTGGGGTGCTCAAAGGATTTAAAGGAGAACTAATTCATGTATTT
AACAAACATGATGGTGCCTTGAGGAATACAGAATATTTCAATCAACTAAAAGACAATAGT
AACATAATTCTTCTGGGAGACTCCCAAGGAGACTTAAGAATGGCAGATGGAGTGGCCAAT
GTTGAGCACATTCTGAAAATTGGATATCTAAATGATAGAGTGGATGAGCTTTTAGAAAAG
TACATGGACTCTTATGATATTGTTTTAGTACAAGATGAATCATTAGAAGTAGCCAACTCT
ATTTTACAGAAGATTCTATAA
Enzyme 7 GenBank Gene ID AF312735 Link Image
Enzyme 7 GeneCard ID NT5C3 Link Image
Enzyme 7 GenAtlas ID NT5C3 Link Image
Enzyme 7 HGNC ID HGNC:17820 Link Image
Enzyme 7 Chromosome Location 7
Enzyme 7 Locus 7p14.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15061
Enzyme 8 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name Not Available
Enzyme 8 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 8 Number of Residues 561
Enzyme 8 Molecular Weight 64960
Enzyme 8 Theoretical pI 6.05
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158256766 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID AK291667 Link Image
Enzyme 8 GeneCard ID A8K6K2 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs Not Available
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16422
Enzyme 9 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name Not Available
Enzyme 9 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 9 Number of Residues 574
Enzyme 9 Molecular Weight 63396
Enzyme 9 Theoretical pI 7.04
Enzyme 9 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 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK314661 Link Image
Enzyme 9 GeneCard ID B2RBH2 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs Not Available
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available