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Human Metabolome Database Version 2.5

 

Showing metabocard for Deoxyribose 1-phosphate (HMDB01351)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:45
Accession Number HMDB01351
Secondary Accession Numbers Not Available
Common Name Deoxyribose 1-phosphate
Description Deoxyribose 1-phosphate is an intermediate in the metabolism of Pyrimidine. It is a substrate for Purine nucleoside phosphorylase and Thymidine phosphorylase.
Synonyms
  1. 2-deoxy-D-ribose-1-phosphate
  2. 2-deoxy-alpha-D-ribose 1-phosphate
  3. 2-deoxy-d-erythro-pentofuranose 1-phosphate
  4. 2-deoxy-d-ribose 1-phosphate
  5. 2-deoxyribofuranose 1-phosphate
  6. Deoxyribose 1-phosphate
  7. Deoxyribose 1-phosphic acid
  8. Deoxyribose-1-phosphate
  9. d-2-deoxy-ribofuranose 1-phosphate
  10. 2-deoxy-delta-ribose-1-phosphate
  11. 2-deoxy-alpha-delta-ribose 1-phosphate
  12. 2-deoxy-delta-erythro-pentofuranose 1-phosphate
  13. 2-deoxy-delta-ribose 1-phosphate
  14. delta-2-deoxy-ribofuranose 1-phosphate
Chemical IUPAC Name [4-hydroxy-5-(hydroxymethyl)oxolan-2-yl]oxyphosphonic acid
Chemical Formula C5H11O7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 214.110
Monoisotopic Molecular Weight 214.024246
Isomeric SMILES OC[C@H]1OC(C[C@@H]1O)OP(O)(O)=O
Canonical SMILES OCC1OC(CC1O)OP(O)(O)=O
KEGG Compound ID C00672 Link Image
BioCyc ID DEOXY-RIBOSE-1P Link Image
BiGG ID 35664 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01351 Link Image
Metagene Link HMDB01351 Link Image
METLIN ID 6182 Link Image
PubChem Compound 439287 Link Image
PubChem Substance 729740 Link Image
ChEBI ID 28542 Link Image
CAS Registry Number 17210-42-3
InChI Identifier InChI=1/C5H11O7P/c6-2-4-3(7)1-5(11-4)12-13(8,9)10/h3-7H,1-2H2,(H2,8,9,10)/t3-,4+,5?/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 37.6 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.14 [Predicted by ALOGPS]; -2.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pentose Phosphate Pathway SMP00031 Link Image map00030 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Holmberg I, Stal P, Hamberg M: Quantitative determination of 8-hydroxy-2'-deoxyguanosine in human urine by isotope dilution mass spectrometry: normal levels in hemochromatosis. Free Radic Biol Med. 1999 Jan;26(1-2):129-35. [PubMed Link Image]
Metabolic Enzymes
  1. Purine nucleoside phosphorylase
  2. Thymidine phosphorylase precursor
  3. Ribokinase
  4. cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
Enzyme 1 [top]
Enzyme 1 ID 5805
Enzyme 1 Name Purine nucleoside phosphorylase
Enzyme 1 Synonyms
  1. Inosine phosphorylase
  2. PNP
Enzyme 1 Gene Name NP
Enzyme 1 Protein Sequence >Purine nucleoside phosphorylase 
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
Enzyme 1 Number of Residues 289
Enzyme 1 Molecular Weight 32118
Enzyme 1 Theoretical pI 6.95
Enzyme 1 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 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • purine nucleoside + phosphate = purine + alpha-D-ribose 1-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 35565 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P00491 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PNPH_HUMAN Link Image
Enzyme 1 PDB ID 1RT9 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >870 bp 
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
Enzyme 1 GenBank Gene ID X00737 Link Image
Enzyme 1 GeneCard ID NP Link Image
Enzyme 1 GenAtlas ID NP Link Image
Enzyme 1 HGNC ID HGNC:7892 Link Image
Enzyme 1 Chromosome Location 14
Enzyme 1 Locus 14q13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5806
Enzyme 2 Name Thymidine phosphorylase precursor
Enzyme 2 Synonyms
  1. TdRPase
  2. TP
  3. Platelet-derived endothelial cell growth factor
  4. PD-ECGF
  5. Gliostatin
Enzyme 2 Gene Name ECGF1
Enzyme 2 Protein Sequence >Thymidine phosphorylase precursor 
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
Enzyme 2 Number of Residues 482
Enzyme 2 Molecular Weight 49956
Enzyme 2 Theoretical pI 5.19
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base metabolism
Component
—
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Catalyzes the reversible phosphorolysis of thymidine. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis
Enzyme 2 Pathways
Enzyme 2 Reactions
  • thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-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 189701 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P19971 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name TYPH_HUMAN Link Image
Enzyme 2 PDB ID 1UOU Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1449 bp 
ATGGCAGCCTTGATGACCCCGGGAACCGGGGCCCCACCCGCGCCTGGTGACTTCTCCGGG
GAAGGGAGCCAGGGACTTCCCGACCCTTCGCCAGAGCCCAAGCAGCTCCCGGAGCTGATC
CGCATGAAGCGAGACGGAGGCCGCCTGAGCGAAGCGGACATCAGGGGCTTCGTGGCCGCT
GTGGTGAATGGGAGCGCGCAGGGCGCACAGATCGGGGCCATGCTGATGGCCATCCGACTT
CGGGGCATGGATCTGGAGGAGACCTCGGTGCTGACCCAGGCCCTGGCTCAGTCGGGACAG
CAGCTGGAGTGGCCAGAGGCCTGGCGCCAGCAGCTTGTGGACAAGCATTCCACAGGGGGT
GTGGGTGACAAGGTCAGCCTGGTCCTCGCACCTGCCCTGGCGGCATGTGGCTGCAAGGTG
CCAATGATCAGCGGACGTGGTCTGGGGCACACAGGAGGCACCTTGGATAAGCTGGAGTCT
ATTCCTGGATTCAATGTCATCCAGAGCCCAGAGCAGATGCAAGTGCTGCTGGACCAGGCG
GGCTGCTGTATCGTGGGTCAGAGTGAGCAGCTGGTTCCTGCGGACGGAATCCTATATGCA
GCCAGAGATGTGACAGCCACCGTGGACAGCCTGCCACTCATCACAGCCTCCATTCTCAGT
AAGAAACTCGTGGAGGGGCTGTCCGCTCTGGTGGTGGACGTTAAGTTCGGAGGGGCCGCC
GTCTTCCCCAACCAGGAGCAGGCCCGGGAGCTGGCAAAGACGCTGGTTGGCGTGGGAGCC
AGCCTAGGGCTTCGGGTCGCGGCAGCGCTGACCGCCATGGACAAGCCCCTGGGTCGCTGC
GTGGGCCACGCCCTGGAGGTGGAGGAGGCGCTGCTCTGCATGGACGGCGCAGGCCCGCCA
GACTTAAGGGACCTGGTCACCACGCTCGGGGGCGCCCTGCTCTGGCTCAGCGGACACGCG
GGGACTCAGGCTCAGGGCGCTGCCCGGGTGGCCGCGGCGCTGGACGACGGCTCGGCCCTT
GGCCGCTTCGAGCGGATGCTGGCGGCGCAGGGCGTGGATCCCGGTCTGGCCCGAGCCCTG
TGCTCGGGAAGTCCCGCAGAACGCCGGCAGCTGCTGCCTCGCGCCCGGGAGCAGGAGGAG
CTGCTGGCGCCCGCAGATGGCACCGTGGAGCTGGTCCGGGCGCTGCCGCTGGCGCTGGTG
CTGCACGAGCTCGGGGCCGGGCGCAGCCGCGCTGGGGAGCCGCTCCGCCTGGGGGTGGGC
GCAGAGCTGCTGGTCGACGTGGGTCAGAGGCTGCGCCGTGGGACCCCCTGGCTCCGCGTG
CACCGGGACGGCCCCGCGCTCAGCGGCCCGCAGAGCCGCGCCCTGCAGGAGGCGCTCGTA
CTCTCCGACCGCGCGCCATTCGCCGCCCCCTCGCCCTTCGCAGAGCTCGTTCTGCCGCCG
CAGCAATAA
Enzyme 2 GenBank Gene ID M63193 Link Image
Enzyme 2 GeneCard ID ECGF1 Link Image
Enzyme 2 GenAtlas ID ECGF1 Link Image
Enzyme 2 HGNC ID HGNC:3148 Link Image
Enzyme 2 Chromosome Location 22
Enzyme 2 Locus 22q13|22q13.33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Ishikawa F, Miyazono K, Hellman U, Drexler H, Wernstedt C, Hagiwara K, Usuki K, Takaku F, Risau W, Heldin CH: Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor. Nature. 1989 Apr 13;338(6216):557-62. [PubMed Link Image]
  2. Furukawa T, Yoshimura A, Sumizawa T, Haraguchi M, Akiyama S, Fukui K, Ishizawa M, Yamada Y: Angiogenic factor. Nature. 1992 Apr 23;356(6371):668. [PubMed Link Image]
  3. Asai K, Nakanishi K, Isobe I, Eksioglu YZ, Hirano A, Hama K, Miyamoto T, Kato T: Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. J Biol Chem. 1992 Oct 5;267(28):20311-6. [PubMed Link Image]
  4. Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH: Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. [PubMed Link Image]
  5. Nishino I, Spinazzola A, Hirano M: Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. Science. 1999 Jan 29;283(5402):689-92. [PubMed Link Image]
  6. Gamez J, Ferreiro C, Accarino ML, Guarner L, Tadesse S, Marti RA, Andreu AL, Raguer N, Cervera C, Hirano M: Phenotypic variability in a Spanish family with MNGIE. Neurology. 2002 Aug 13;59(3):455-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6377
Enzyme 3 Name Ribokinase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name RBKS
Enzyme 3 Protein Sequence >Ribokinase 
MAASGEPQRQWQEEVAAVVVVGSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCV
QAARLGAMTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNI
IVIVAGANLLLNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAP
AIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEG
CVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAV
SVQAAGTQSSYPYKKDLPLTLF
Enzyme 3 Number of Residues 322
Enzyme 3 Molecular Weight 34143
Enzyme 3 Theoretical pI 4.68
Enzyme 3 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, alcohol group as acceptor
  • ribokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • D-ribose metabolism
  • alcohol metabolism
  • cellular metabolism
  • metabolism
  • monosaccharide metabolism
  • pentose metabolism
  • physiological process
Component
—
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function ATP + D-ribose = ADP + D-ribose 5-phosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + D-ribose = ADP + D-ribose 5-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 10799803 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9H477 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name RBSK_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >969 bp 
ATGGCGGCGTCTGGGGAACCCCAGAGGCAGTGGCAAGAGGAGGTGGCGGCGGTGGTAGTG
GTGGGCTCCTGCATGACCGACCTGGTCAGTCTTACTTCTCGTTTGCCAAAAACTGGAGAA
ACCATCCATGGACATAAGTTTTTTATTGGCTTTGGAGGGAAAGGTGCCAACCAGTGTGTC
CAAGCTGCTCGGCTTGGAGCAATGACGTCCATGGTGTGTAAGGTTGGCAAAGATTCTTTT
GGCAATGATTATATAGAAAACTTAAAACAGAATGATATTTCTACAGAATTTACATATCAG
ACTAAAGATGCTGCTACAGGAACTGCTTCTATAATTGTCAATAATGAAGGCCAGAATATC
ATTGTCATAGTGGCTGGAGCAAATTTACTTTTGAATACGGAGGATCTGAGGGCAGCAGCC
AATGTCATTAGCAGAGCCAAAGTCATGGTCTGCCAGCTCGAAATAACTCCAGCAACTTCT
TTGGAAGCCCTAACAATGGCCCGCAGGAGTGGAGTGAAAACCTTGTTCAATCCAGCCCCT
GCCATTGCTGACCTGGATCCCCAGTTCTACACCCTCTCAGATGTGTTCTGCTGCAATGAA
AGTGAGGCTGAGATTTTAACTGGCCTCACGGTGGGCAGCGCTGCAGATGCTGGGGAGGCT
GCATTAGTGCTCTTGAAAAGGGGCTGCCAGGTGGTAATCATTACCTTAGGGGCTGAAGGA
TGTGTGGTGCTGTCACAGACAGAACCTGAGCCAAAGCACATTCCCACAGAGAAAGTCAAG
GCTGTGGATACCACGGGTGCTGGTGACAGCTTTGTGGGAGCTCTGGCCTTCTACCTGGCT
TACTATCCAAATCTGTCCTTGGAAGACATGCTCAACAGATCCAATTTCATTGCAGCAGTC
AGTGTCCAGGCTGCAGGAACACAGTCATCTTACCCTTACAAAAAAGACCTTCCGCTTACT
CTGTTTTGA
Enzyme 3 GenBank Gene ID AJ404857 Link Image
Enzyme 3 GeneCard ID RBKS Link Image
Enzyme 3 GenAtlas ID RBKS Link Image
Enzyme 3 HGNC ID HGNC:30325 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p23.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16421
Enzyme 4 Name cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name Not Available
Enzyme 4 Protein Sequence >cDNA, FLJ95575, highly similar to Homo sapiens endothelial cell growth factor 1 (platelet-derived) (ECGF1), mRNA 
MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAA
VVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGG
VGDKVSLVLAPALAACGCKVPVISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQA
GCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAA
VFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPP
DLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARAL
CSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVG
AELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPP
QQ
Enzyme 4 Number of Residues 482
Enzyme 4 Molecular Weight 49924
Enzyme 4 Theoretical pI 5.19
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base metabolism
Component
—
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID B2RBL3 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name B2RBL3_HUMAN Link Image
Enzyme 4 PDB ID 1UOU Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AK314716 Link Image
Enzyme 4 GeneCard ID B2RBL3 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs Not Available
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available