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Human Metabolome Database Version 2.5

 

Showing metabocard for D-Ribose 5-phosphate (HMDB01548)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-07 04:01:20
Accession Number HMDB01548
Secondary Accession Numbers Not Available
Common Name D-Ribose 5-phosphate
Description D-Ribose 5-phosphate is an important intermediate metabolite in the Pentose phosphate pathway (KEGG, map00030) and in the Purine metabolism pathway (KEGG, map00230). The intracellular ribose 5-phosphate concentration is an important determinant of the rate of de novo purine synthesis. (PMID 6699001)
Synonyms
  1. D-Ribose 5-phosphate
  2. D-Ribose 5-phosphic acid
  3. D-ribose-5-P
  4. D-ribose-5-phosphate
  5. D-ribose-5-phosphorate
  6. D-ribose-5-phosphoric acid
  7. Ribose-5-phosphate
  8. ribose-5-P
  9. ribose-5-phosphorate
  10. ribose-5-phosphoric acid
  11. ribose-5P
Chemical IUPAC Name (2,3,4-trihydroxy-5-oxo-pentoxy)phosphonic acid
Chemical Formula C5H11O8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • hemiacetal
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
  • Component of Purine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 230.110
Monoisotopic Molecular Weight 230.019150
Isomeric SMILES OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O
Canonical SMILES OC1OC(COP(O)(O)=O)C(O)C1O
KEGG Compound ID C00117 Link Image
BioCyc ID RIBOSE-5P Link Image
BiGG ID 42420 Link Image
Wikipedia Link D-ribose-5-P Link Image
NuGOwiki Link HMDB01548 Link Image
Metagene Link HMDB01548 Link Image
METLIN ID 6315 Link Image
PubChem Compound 77982 Link Image
PubChem Substance 823373 Link Image
ChEBI ID 17797 Link Image
CAS Registry Number 3615-55-2
InChI Identifier InChI=1/C5H11O8P/c6-3-2(1-12-14(9,10)11)13-5(8)4(3)7/h2-8H,1H2,(H2,9,10,11)/t2-,3-,4-,5?/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 33.6 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.07 [Predicted by ALOGPS]; -3.9 [Predicted by PubChem via XLOGP]; -2.65 [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 1JCY 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
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 13.2 +/- 4.8 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 0.281 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]
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
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. 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]
  2. Wikipedia Link Image
Metabolic Enzymes
  1. Ribose-phosphate pyrophosphokinase III
  2. Ribose-phosphate pyrophosphokinase I
  3. Ribose-phosphate pyrophosphokinase II
  4. Transketolase-like protein 1
  5. Transketolase
  6. Ribokinase
  7. Phosphoglucomutase-1
  8. Ribose-5-phosphate isomerase
  9. Transketolase-like protein 2
  10. cDNA FLJ76204, highly similar to Homo sapiens transketolase
  11. cDNA FLJ76398, highly similar to Homo sapiens nudix
  12. CDNA FLJ14389 fis, clone HEMBA1002876
  13. cDNA, FLJ95330, Homo sapiens phosphoglucomutase 3 (PGM3), mRNA (Phosphoglucomutase 3, isoform CRA_d)
  14. Ribose-phosphate pyrophosphokinase
  15. Ribose-phosphate pyrophosphokinase
Enzyme 1 [top]
Enzyme 1 ID 5838
Enzyme 1 Name Ribose-phosphate pyrophosphokinase III
Enzyme 1 Synonyms
  1. Phosphoribosyl pyrophosphate synthetase III
  2. PRS-III
  3. Phosphoribosyl pyrophosphate synthetase 1-like 1
Enzyme 1 Gene Name PRPS1L1
Enzyme 1 Protein Sequence >Ribose-phosphate pyrophosphokinase III 
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGC
GEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTS
IADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAG
ATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAI
RRTHNGESVSYLFSHVPL
Enzyme 1 Number of Residues 318
Enzyme 1 Molecular Weight 34840
Enzyme 1 Theoretical pI 6.31
Enzyme 1 GO Classification
Function
  • catalytic activity
  • diphosphotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lipoate-protein ligase B activity
  • lipoate-protein ligase activity
  • ribose phosphate diphosphokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleoside monophosphate biosynthesis
  • nucleoside monophosphate metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 190522 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P21108 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PRPS3_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >957 bp 
ACGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCCCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGCGTGGAAATTGATGAGAGTGTGCGTGGAGAGGATGTCTACATCGTTCAGAGTGGTTGT
GGCGAAATCAACGACAGTCTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCTAGCCGAGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGACAGGATAAGAAG
GATAAGAGCCGGTCCCCAATCTCTGCCAAGCTTGTTGCAAATATGCTCTCTATAGCAGGT
GCGGATCATATCATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAACTTGTATGCAGAGCCAACTGTCCTGAAGTGGATAAGGGAGAATATCCCT
GAGTGGAAGAACTGCATTATTGTCTCGCCAGATGCTGGTGGAGCTAAAAGAGTGACCTCC
ATTGCAGACCAGTTGAATGTGGACTTTGCTTTGATTCATAAAGAACGGAAGAAGGCCAAT
GAAGTGGACTGCATAGTGCTAGTGGGAGATGTGAATGATCGTGTGGCTATCCTTGTAGAT
GACATGGCAGACACTTGTGTTACAATCTGCCTCGCAGCTGACAAACTTCTCTCAGCTGGA
GCAACCAGAGTTTATGCTATCTTGACTCATGGAATCTTTTCTGGCCCAGCCATTTCTCGC
ATCAACACTGCATGCTTTGAAGCAGTGGTAGTCACCAATACCATACCTCAAGATGAGAAG
ATGAAGCATTGCTCCAAAATACGAGTAATTGACATCTCCATGATCCTTGCAGAAGCCATA
AGGAGAACTCATAATGGGGAATCTGTTTCCTACCTGTTCAGCCATGTTCCTTTATAA
Enzyme 1 GenBank Gene ID M57423 Link Image
Enzyme 1 GeneCard ID PRPS1L1 Link Image
Enzyme 1 GenAtlas ID PRPS1L1 Link Image
Enzyme 1 HGNC ID HGNC:9463 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Taira M, Iizasa T, Shimada H, Kudoh J, Shimizu N, Tatibana M: A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon. J Biol Chem. 1990 Sep 25;265(27):16491-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5900
Enzyme 2 Name Ribose-phosphate pyrophosphokinase I
Enzyme 2 Synonyms
  1. Phosphoribosyl pyrophosphate synthetase I
  2. PRS-I
  3. PPRibP
Enzyme 2 Gene Name PRPS1
Enzyme 2 Protein Sequence >Ribose-phosphate pyrophosphokinase I 
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
Enzyme 2 Number of Residues 318
Enzyme 2 Molecular Weight 34835
Enzyme 2 Theoretical pI 6.98
Enzyme 2 GO Classification
Function
  • catalytic activity
  • diphosphotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lipoate-protein ligase B activity
  • lipoate-protein ligase activity
  • ribose phosphate diphosphokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleoside monophosphate biosynthesis
  • nucleoside monophosphate metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 35702 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P60891 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PRPS1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >957 bp 
ATGCCGAATATCAAAATCTTCAGCGGCAGTTCCCACCAGGACTTATCTCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAGTTCAGCAACCAGGAGACC
TGTGTGGAAATCGGTGAAAGTGTACGTGGAGAGGATGTCTACATTGTTCAGAGTGGTTGT
GGCGAAATCAATGACAATTTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCCAGCCGGGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGGCAGGATAAGAAG
GATAAGAGCCGGGCGCCAATCTCAGCCAAGCTTGTTGCAAATATGCTATCTGTAGCAGGT
GCAGATCATATTATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAATTTGTATGCAGAGCCGGCTGTCCTAAAGTGGATAAGGGAGAATATCTCT
GAGTGGAGGAACTGCACTATTGTCTCACCTGATGCTGGTGGAGCTAAGAGAGTGACCTCC
ATTGCAGACAGGCTGAATGTGGACTTTGCCTTGATTCACAAAGAACGGAAGAAGGCCAAT
GAAGTGGACCGCATGGTGCTTGTGGGAGATGTGAAGGATCGGGTGGCCATCCTTGTGGAT
GACATGGCTGACACTTGTGGCACAATCTGCCATGCAGCTGACAAACTTCTCTCAGCTGGC
GCCACCAGAGTTTATGCCATCTTGACTCATGGAATCTTCTCCGGTCCTGCTATTTCTCGC
ATCAACAACGCATGCTTTGAGGCAGTAGTAGTCACCAATACCATACCTCAGGAGGACAAG
ATGAAGCATTGCTCCAAAATACAGGTGATTGACATCTCTATGATCCTTGCAGAAGCCATC
AGGAGAACTCACAATGGAGAATCCGTTTCTTACCTATTCAGCCATGTCCCTTTATAA
Enzyme 2 GenBank Gene ID X15331 Link Image
Enzyme 2 GeneCard ID PRPS1 Link Image
Enzyme 2 GenAtlas ID PRPS1 Link Image
Enzyme 2 HGNC ID HGNC:9462 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Roessler BJ, Bell G, Heidler S, Seino S, Becker M, Palella TD: Cloning of two distinct copies of human phosphoribosylpyrophosphate synthetase cDNA. Nucleic Acids Res. 1990 Jan 11;18(1):193. [PubMed Link Image]
  2. Sonoda T, Taira M, Ishijima S, Ishizuka T, Iizasa T, Tatibana M: Complete nucleotide sequence of human phosphoribosyl pyrophosphate synthetase subunit I (PRS I) cDNA and a comparison with human and rat PRPS gene families. J Biochem (Tokyo). 1991 Feb;109(2):361-4. [PubMed Link Image]
  3. Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed Link Image]
  4. Becker MA, Smith PR, Taylor W, Mustafi R, Switzer RL: The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity. J Clin Invest. 1995 Nov;96(5):2133-41. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5904
Enzyme 3 Name Ribose-phosphate pyrophosphokinase II
Enzyme 3 Synonyms
  1. Phosphoribosyl pyrophosphate synthetase II
  2. PRS-II
  3. PPRibP
Enzyme 3 Gene Name PRPS2
Enzyme 3 Protein Sequence >Ribose-phosphate pyrophosphokinase II 
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGC
GEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRVTS
IADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATKVYAILTHGIFSGPAISRINNAAFEAVVVTNTIPQEDKMKHCTKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
Enzyme 3 Number of Residues 318
Enzyme 3 Molecular Weight 34770
Enzyme 3 Theoretical pI 6.60
Enzyme 3 GO Classification
Function
  • catalytic activity
  • diphosphotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lipoate-protein ligase B activity
  • lipoate-protein ligase activity
  • ribose phosphate diphosphokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleoside monophosphate biosynthesis
  • nucleoside monophosphate metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 35700 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P11908 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PRPS2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >957 bp 
ATGCCCAACATCGTGCTGTTCAGCGGCAGCTCGCATCAGGACCTATCCCAGCGCGTGGCC
GACCGCCTGGGCCTGGAGCTGGGCAAGGTGGTCACGAAGAAGTTCAGCAACCAGGAGACC
AGCGTGGAGATTGGTGAAAGCGTGAGAGGGGAAGATGTCTACATCATCCAGAGCGGCTGC
GGGGAAATTAACGACAACCTGATGGAACTCCTCATCATGATCAATGCCTGCAAGATTGCG
TCATCATCCAGAGTAACTGCCGTGATCCCGTGTTTCCCATACGCCCGACAAGATAAAAAG
GACAAGAGTCGTGCCCCAATTTCTGCAAAACTTGTGGCCAATATGCTGTCGGTGGCTGGG
GCGGATCACATCATCACCATGGACCTGCATGCTTCTCAGATACAGGGATTCTTTGATATT
CCTGTGGATAATTTGTATGCGGAGCCCGCAGTCCTGCAGTGGATTCGGGAAAACATTGCC
GAGTGGAAGAACTGTATCATTGTTTCACCTGACGCAGGGGGAGCCAAAAGGGTTACATCA
ATTGCAGACAGGTTGAATGTGGAATTTGCTTTGATCCACAAAGAGAGGAAGAAGGCGAAT
GAAGTGGACCGGATGGTCCTGGTGGGCGACGTGAAGGACCGTGTGGCCATCCTCGTGGAT
GACATGGCTGACACTTGCGGCACCATCTGCCATGCTGCGGACAAGCTGCTGTCAGCTGGA
GCCACCAAAGTGTATGCTATCCTTACCCATGGGATCTTCTCTGGACCAGCTATTTCCAGA
ATAAATAATGCCGCCTTTGAGGCTGTTGTCGTCACAAACACAATTCCGCAAGAGGACAAA
ATGAAACACTGCACCAAGATTCAGGTCATTGACATTTCCATGATCTTGGCCGAAGCAATC
CGAAGGACACACAATGGGGAATCCGTGTCCTACCTGTTCAGCCATGTCCCGCTATAA
Enzyme 3 GenBank Gene ID Y00971 Link Image
Enzyme 3 GeneCard ID PRPS2 Link Image
Enzyme 3 GenAtlas ID PRPS2 Link Image
Enzyme 3 HGNC ID HGNC:9465 Link Image
Enzyme 3 Chromosome Location X
Enzyme 3 Locus Xp22.3-p22.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Iizasa T, Taira M, Shimada H, Ishijima S, Tatibana M: Molecular cloning and sequencing of human cDNA for phosphoribosyl pyrophosphate synthetase subunit II. FEBS Lett. 1989 Feb 13;244(1):47-50. [PubMed Link Image]
  2. Iizasa T, Taira M, Shimada H, Tatibana M: Deduced amino acid sequence from human phosphoribosylpyrophosphate synthetase subunit II cDNA. Adv Exp Med Biol. 1989;253A:519-23. [PubMed Link Image]
  3. Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6080
Enzyme 4 Name Transketolase-like protein 1
Enzyme 4 Synonyms
  1. Transketolase 2
  2. TK 2
  3. Transketolase-related protein
Enzyme 4 Gene Name TKTL1
Enzyme 4 Protein Sequence >Transketolase-like protein 1 
MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVL
FFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRV
FCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAF
GWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRER
ADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALA
KLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFA
STFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIF
YPTDAVSTEHAVALAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVI
GAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEGRIITVEDHYPQG
GIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN
Enzyme 4 Number of Residues 596
Enzyme 4 Molecular Weight 65334
Enzyme 4 Theoretical pI 5.65
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring aldehyde or ketonic groups
  • transketolase activity
Process
—
Component
—
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1232175 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P51854 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name TKTL1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1623 bp 
ATGTCTGTGCTGTTCTTCTACATCATGAGGTACAAGCAGTCAGATCCAGAGAATCCGGAC
AACGACCGATTTGTCCTCGCAAAGAGACTGTCGTTTGTGGATGTGGCAACAGGATGGCTC
GGACAAGGACTGGGAGTTGCATGTGGAATGGCATATACTGGCAAGTACTTCGACAGGGCC
AGCTACCGGGTGTTCTGCCTCATGAGTGATGGCGAGTCCTCAGAAGGCTCTGTCTGGGAG
GCAATGGCCTTTGCTTCCTACTACAGTCTGGACAATCTTGTGGCAATCTTTGATGTGAAC
CGCCTGGGACACAGTGGTGCATTGCCCGCCGAGCACTGCATAAACATCTATCAGAGGCGC
TGCGAAGCCTTTGGGTGGAACACTTATGTGGTGGACGGCCGGGACGTGGAGGCACTGTGC
CAGGTATTCTGGCAGGCTTCTCAGGTGAAGCACAAGCCCACTGCTGTGGTGGCCAAGACC
TTCAAGGGCCGGGGCACCCCAAGTATTGAGGATGCAGAAAGTTGGCATGCAAAGCCAATG
CCGAGAGAAAGAGCAGATGCCATTATCAAATTAATTGAGAGCCAGATACAGACCAGCAGG
AATCTTGACCCACAGCCCCCCATTGAGGACTCACCTGAAGTCAACATCACAGATGTAAGG
ATGACCTCTCCACCTGATTACAGAGTTGGTGACAAGATAGCTACTCGGAAAGCATGCGGT
CTGGCTCTGGCTAAGCTGGGCTACGCGAACAACAGAGTCGTTGTGCTGGATGGTGACACC
AGGTACTCTACTTTCTCTGAGATATTCAACAAGGAGTACCCTGAGCGCTTCATCGAGTGC
TTTATGGCTGAACAAAACATGGTGAGCGTGGCTCTGGGCTGTGCCTCCCGTGGACGGACC
ATTGCTTTTGCTAGCACCTTTGCTGCCTTTCTGACTCGAGCATTTGATCACATCCGGATA
GGAGGCCTCGCTGAGAGCAACATCAACATTATTGGTTCCCACTGTGGGGTATCTGTTGGT
GACGATGGTGCTTCCCAGATGGCCCTGGAGGATATAGCCATGTTCCGAACCATTCCCAAG
TGCACGATCTTCTACCCAACTGATGCCGTCTCCACGGAGCATGCTGTTGCTCTGGCAGCC
AATGCCAAGGGGATGTGCTTCATTCGGACCACCCGACCAGAAACTATGGTTATTTACACC
CCACAAGAACGCTTTGAGATCGGACAGGCCAAGGTCCTCCGCCACTGTGTCAGTGACAAG
GTCACAGTTATTGGAGCTGGAATTACTGTGTATGAAGCCTTAGCAGCTGCTGATGAGCTT
TCGAAACAAGATATTTTTATCCGTGTCATCGACCTGTTTACCATTAAACCTCTGGATGTC
GCCACCATCGTCTCCAGTGCAAAAGCCACAGAGGGCCGGATCATTACAGTGGAGGATCAC
TACCCGCAAGGTGGCATCGGGGAAGCTGTCTGCGCAGCCGTCTCCATGGATCCTGACATT
CAGGTTCATTCGCTGGCAGTGTCGGGAGTGCCCCAGAGTGGGAAGTCCGAGGAATTGCTG
GATATGTATGGAATTAGTGCCAGACATATCATAGTGGCCGTGAAATGCATGTTGCTGAAC
TAA
Enzyme 4 GenBank Gene ID X91817 Link Image
Enzyme 4 GeneCard ID TKTL1 Link Image
Enzyme 4 GenAtlas ID TKTL1 Link Image
Enzyme 4 HGNC ID HGNC:11835 Link Image
Enzyme 4 Chromosome Location X
Enzyme 4 Locus Xq28
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Coy JF, Dubel S, Kioschis P, Thomas K, Micklem G, Delius H, Poustka A: Molecular cloning of tissue-specific transcripts of a transketolase-related gene: implications for the evolution of new vertebrate genes. Genomics. 1996 Mar 15;32(3):309-16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6085
Enzyme 5 Name Transketolase
Enzyme 5 Synonyms
  1. TK
Enzyme 5 Gene Name TKT
Enzyme 5 Protein Sequence >Transketolase 
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKS
QDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDV
ATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVA
ILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIA
KTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIAN
IRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFI
ECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVS
IGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAII
YNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPL
DRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAE
LLKMFGIDRDAIAQAVRGLITKA
Enzyme 5 Number of Residues 623
Enzyme 5 Molecular Weight 67878
Enzyme 5 Theoretical pI 7.73
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring aldehyde or ketonic groups
  • transketolase activity
Process
—
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 5 Pathways
Enzyme 5 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-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 37267 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P29401 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name TKT_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1872 bp 
ATGGAGAGCTACCACAAGCCTGACCAGCAGAAGCTGCAGGCCTTGAAGGACACGGCCAAC
CGCCTACGTATCAGCTCCATCCAGGCCTCCTCTGCGGCGGGCTCTGGCCACCCCACGTCA
TGCTGCAGCGCCGCAGTGATCATGGCTGTCCTCTTTTTCCACACCATGCGCTACAAGTCC
CAGGACCCCCGGAATCCGCACAATGACCGCTTTGTGCTCTCCAAGGGCCATGCAGCTCCC
ATCCTCTACGCGGTCTGGGCTGAAGCTGGTTTCCTGGCCGAGGCGGAGCTGCTGAACCTG
AGGAAGATCAGCTCCGACTTGGACGGGCACCCGGTCCCGAAACAAGCTTTCACCGACGTG
GCCACTGGCTCCCTGGGCCAGGGCCTCGGGGCCGCTTGTGGGATGGCCTACACCGGCAAA
TACTTCGACAAGGCCAGCTACCGAGTCTATTGCTTGCTGGGAGATGGGGAGCTGTCAGAG
GGCTCTGTATGGGAGGCCATGGCCTTCGCCAGCATCTATAAGCTGGACAACCTTGTGGCC
ATTCTAGACATCAATCGCCTGGGCCAGAGTGACCCGGCCCCGCTGCAGCACCAGATGGAC
ATCTACCAGAAGCGGTGCGAGGCCTTCGGTTGGCATGCCATCATCGTGGATGGACACAGC
GTGGAGGAGCTGTGCAAGGCCTTTGGCCAGGCCAAGCACCAGCCAACAGCCATCATTGCC
AAGACCTTCAAGGGCCGAGGGATCACGGGGGTAGAAGATAAGGAGTCTTGGCATGGGAAG
CCCCTCCCCAAAAACATGGCTGAGCAGATCATCCAGGAGATCTACAGCCAGATCCAGAGC
AAAAAGAAGATCCTGGCAACCCCTCCACAGGAGGACGCACCCTCAGTGGACATTGCCAAC
ATCCGCATGCCCAGCCTGCCCAGCTACAAAGTTGGGGACAAGATAGCCACCCGCAAGGCC
TACGGGCAGGCACTGGCCAAGCTGGGCCATGCCAGTGACCGCATCATCGCCCTGGATGGG
GACACCAAAAATTCCACCTTCTCGGAGATCTTCAAAAAGGAGCACCCGGACCGCTTCATC
GAGTGCTACATTGCCGAGCAGAACATGGTGAGCATCGCGGTGGGCTGTGCCACCCGCAAC
AGGACGGTGCCCTTCTGCAGCACTTTTGCAGCCTTCTTCACGCGGGCCTTTGACCAGATT
CGCATGGCGGCCATCTCCGAGAGCAACATCAACCTCTGCGGCTCCCACTGCGGCGTTTCC
ATCGGGGAAGACGGGGCCTCCCAGATGGCCCTAGAAGATCTGGCTATGTTTCGGTCAGTC
CCCACATCAACTGTCTTTTACCCAAGTGATGGCGTTGCTACAGAGAAGGCAGTGGAACTA
GCCGCCAATACAAAGGGTATCTGCTTCATCCGGACCAGCCGCCCAGAAAATGCCATCATC
TATAACAACAATGAGGACTTCCAGGTCGGACAAGCCAAGGTGGTCCTGAAGAGCAAGGAT
GACCAGGTGACCGTTATCGGGGCTGGGGTGACCCTGCACGAGGCCTTGGCCGCTGCCGAA
CTGCTGAAGAAAGAAAAGATCAACATCCGCGTGCTGGACCCCTTCACCATCAAGCCCCTG
GACAGAAAACTCATTCTCGACAGCGCTCGTGCCACCAAGGGCAGGATCCTCACCGTGGAG
GACCATTATTATGAAGGTGGCATTGGTGAGGCTGTGTCCAGTGCAGTAGTGGGCGAGCCT
GGCATCACTGTCACCCACCTGGCAGTTAACCGGGTACCAAGAAGTGGGAAGCCAGCTGAG
CTGCTGAAGATGTTTGGTATCGACAGGGATGCCATTGCACAAGCTGTGAGGGGCCTCATC
ACCAAGGCCTAG
Enzyme 5 GenBank Gene ID X67688 Link Image
Enzyme 5 GeneCard ID TKT Link Image
Enzyme 5 GenAtlas ID TKT Link Image
Enzyme 5 HGNC ID HGNC:11834 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p14.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. McCool BA, Plonk SG, Martin PR, Singleton CK: Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals. J Biol Chem. 1993 Jan 15;268(2):1397-404. [PubMed Link Image]
  2. 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]
  3. Abedinia M, Layfield R, Jones SM, Nixon PF, Mattick JS: Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase. Biochem Biophys Res Commun. 1992 Mar 31;183(3):1159-66. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6377
Enzyme 6 Name Ribokinase
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name RBKS
Enzyme 6 Protein Sequence >Ribokinase 
MAASGEPQRQWQEEVAAVVVVGSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCV
QAARLGAMTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNI
IVIVAGANLLLNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAP
AIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEG
CVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAV
SVQAAGTQSSYPYKKDLPLTLF
Enzyme 6 Number of Residues 322
Enzyme 6 Molecular Weight 34143
Enzyme 6 Theoretical pI 4.68
Enzyme 6 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 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function ATP + D-ribose = ADP + D-ribose 5-phosphate
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + D-ribose = ADP + D-ribose 5-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 10799803 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9H477 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name RBSK_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >969 bp 
ATGGCGGCGTCTGGGGAACCCCAGAGGCAGTGGCAAGAGGAGGTGGCGGCGGTGGTAGTG
GTGGGCTCCTGCATGACCGACCTGGTCAGTCTTACTTCTCGTTTGCCAAAAACTGGAGAA
ACCATCCATGGACATAAGTTTTTTATTGGCTTTGGAGGGAAAGGTGCCAACCAGTGTGTC
CAAGCTGCTCGGCTTGGAGCAATGACGTCCATGGTGTGTAAGGTTGGCAAAGATTCTTTT
GGCAATGATTATATAGAAAACTTAAAACAGAATGATATTTCTACAGAATTTACATATCAG
ACTAAAGATGCTGCTACAGGAACTGCTTCTATAATTGTCAATAATGAAGGCCAGAATATC
ATTGTCATAGTGGCTGGAGCAAATTTACTTTTGAATACGGAGGATCTGAGGGCAGCAGCC
AATGTCATTAGCAGAGCCAAAGTCATGGTCTGCCAGCTCGAAATAACTCCAGCAACTTCT
TTGGAAGCCCTAACAATGGCCCGCAGGAGTGGAGTGAAAACCTTGTTCAATCCAGCCCCT
GCCATTGCTGACCTGGATCCCCAGTTCTACACCCTCTCAGATGTGTTCTGCTGCAATGAA
AGTGAGGCTGAGATTTTAACTGGCCTCACGGTGGGCAGCGCTGCAGATGCTGGGGAGGCT
GCATTAGTGCTCTTGAAAAGGGGCTGCCAGGTGGTAATCATTACCTTAGGGGCTGAAGGA
TGTGTGGTGCTGTCACAGACAGAACCTGAGCCAAAGCACATTCCCACAGAGAAAGTCAAG
GCTGTGGATACCACGGGTGCTGGTGACAGCTTTGTGGGAGCTCTGGCCTTCTACCTGGCT
TACTATCCAAATCTGTCCTTGGAAGACATGCTCAACAGATCCAATTTCATTGCAGCAGTC
AGTGTCCAGGCTGCAGGAACACAGTCATCTTACCCTTACAAAAAAGACCTTCCGCTTACT
CTGTTTTGA
Enzyme 6 GenBank Gene ID AJ404857 Link Image
Enzyme 6 GeneCard ID RBKS Link Image
Enzyme 6 GenAtlas ID RBKS Link Image
Enzyme 6 HGNC ID HGNC:30325 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2p23.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6399
Enzyme 7 Name Phosphoglucomutase-1
Enzyme 7 Synonyms
  1. Glucose phosphomutase 1
  2. PGM 1
Enzyme 7 Gene Name PGM1
Enzyme 7 Protein Sequence >Phosphoglucomutase-1 
MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVG
GDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNP
GGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENK
FKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEE
LGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKH
GFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWK
FFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKY
GRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPV
DGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLI
SIALKVSQLQERTGRTAPTVIT
Enzyme 7 Number of Residues 562
Enzyme 7 Molecular Weight 61450
Enzyme 7 Theoretical pI 6.72
Enzyme 7 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Carbohydrate transport and metabolism
Enzyme 7 Specific Function This enzyme participates in both the breakdown and synthesis of glucose
Enzyme 7 Pathways
Enzyme 7 Reactions
  • alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 189926 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P36871 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PGM1_HUMAN Link Image
Enzyme 7 PDB ID 1C47 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1689 bp 
ATGGTGAAGATCGTGACAGTTAAGACCCAGGCGTACCAGGACCAGAAGCCGGGCACGAGC
GGGCTGCGGAAGCGGGTGAAGGTGTTCCAGAGCAGCGCCAACTACGCGGAGAACTTCATC
CAGAGTATCATCTCCACCGTGGAGCCGGCGCAGCGGCAGGAGGCCACGCTGGTGGTGGGC
GGGGACGGCCGGTTCTACATGAAGGAGGCCATCCAGCTCATCGCTCGCATCGCTGCCGCC
AACGGGATCGGTCGCTTGGTTATCGGACAGAATGGAATCCTCTCCACCCCTGCTGTATCC
TGCATCATTAGAAAAATCAAAGCCATTGGTGGGATCATTCTGACAGCCAGTCACAACCCA
GGGGGCCCCAATGGAGATTTTGGAATCAAATTCAATATTTCTAATGGAGGTCCTGCTCCA
GAAGCAATAACTGATAAAATTTTCCAAATCAGCAAGACAATTGAAGAATATGCAGTTTGC
CCTGACCTGAAAGTAGACCTTGGTGTTCTGGGAAAGCAGCAGTTTGACTTGGAAAATAAG
TTCAAACCCTTCACAGTGGAAATTGTGGATTCGGTAGAAGCTTATGCTACAATGCTGAGA
AGCATCTTTGATTTCAGTGCACTGAAAGAACTACTTTCTGGGCCAAACCGACTGAAGATC
TGTATTGATGCTATGCATGGAGTTGTGGGACCGTATGTAAAGAAGATCCTCTGTGAAGAA
CTCGGTGCCCCTGCGAACTCGGCAGTTAACTGCGTTCCTCTGGAGGACTTTGGAGGCCAC
CACCCTGACCCCAACCTCACCTATGCAGCTGACCTGGTGGAGACCATGAAGTCAGGAGAG
CATGATTTTGGGGCTGCCTTTGATGGAGATGGGGATCGAAACATGATTCTGGGCAAGCAT
GGGTTCTTTGTGAACCCTTCAGACTCTGTGGCTGTCATTGCTGCCAACATCTTCAGCATT
CCGTATTTCCAGCAGACTGGGGTCCGCGGCTTTGCACGGAGCATGCCCACGAGTGGTGCT
CTGGACCGGGTGGCTAGTGCTACAAAGATTGCTTTGTATGAGACCCCAACTGGCTGGAAG
TTTTTTGGGAATTTGATGGACGCGAGCAAACTGTCCCTTTGTGGGGAGGAGAGCTTCGGG
ACCGGTTCTGACCACATCCGTGAGAAAGATGGACTGTGGGCTGTCCTTGCCTGGCTCTCC
ATCCTAGCCACCCGCAAGCAGAGTGTGGAGGACATTCTCAAAGATCATTGGCAAAAGCAT
GGCCGGAATTTCTTCACCAGGTATGATTACGAGGAGGTGGAAGCTGAGGGCGCAAACAAA
ATGATGAAGGACTTGGAGGCCCTGATGTTTGATCGCTCCTTTGTGGGGAAGCAGTTCTCA
GCAAATGACAAAGTTTACACTGTGGAGAAGGCCGATAACTTTGAATACAGCGACCCAGTG
GATGGAAGCATTTCAAGAAATCAGGGCTTGCGCCTCATTTTCACAGATGGTTCTCGAATC
GTCTTCCGACTGAGCGGCACTGGGAGTGCCGGGGCCACCATTCGGCTGTACATCGATAGC
TATGAGAAGGACGTTGCCAAGATTAACCAGGACCCCCAGGTCATGTTGGCCCCCCTTATT
TCCATTGCTCTGAAAGTGTCCCAGCTGCAGGAGAGGACGGGACGCACTGCACCCACTGTC
ATCACCTAA
Enzyme 7 GenBank Gene ID M83088 Link Image
Enzyme 7 GeneCard ID PGM1 Link Image
Enzyme 7 GenAtlas ID PGM1 Link Image
Enzyme 7 HGNC ID HGNC:8905 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p31
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Whitehouse DB, Putt W, Lovegrove JU, Morrison K, Hollyoake M, Fox MF, Hopkinson DA, Edwards YH: Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct mapping of this highly polymorphic marker on human chromosome 1. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):411-5. [PubMed Link Image]
  2. Putt W, Ives JH, Hollyoake M, Hopkinson DA, Whitehouse DB, Edwards YH: Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon. Biochem J. 1993 Dec 1;296 ( Pt 2):417-22. [PubMed Link Image]
  3. Takahashi N, Neel JV: Intragenic recombination at the human phosphoglucomutase 1 locus: predictions fulfilled. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10725-9. [PubMed Link Image]
  4. March RE, Putt W, Hollyoake M, Ives JH, Lovegrove JU, Hopkinson DA, Edwards YH, Whitehouse DB: The classical human phosphoglucomutase (PGM1) isozyme polymorphism is generated by intragenic recombination. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10730-3. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6934
Enzyme 8 Name Ribose-5-phosphate isomerase
Enzyme 8 Synonyms
  1. Phosphoriboisomerase
Enzyme 8 Gene Name RPIA
Enzyme 8 Protein Sequence >Ribose-5-phosphate isomerase 
MSKAEEAKKLAGRAAVENHVRNNQVLGIGSGSTIVHAVQRIAERVKQENLNLVCIPTSFQ
ARQLILQYGLTLSDLDRHPEIDLAIDGADEVDADLNLIKGGGGCLTQEKIVAGYASRFIV
IADFRKDSKNLGDQWHKGIPIEVIPMAYVPVSRAVSQKFGGVVELRMAVNKAGPVVTDNG
NFILDWKFDRVHKWSEVNTAIKMIPGVVDTGLFINMAERVYFGMQDGSVNMREKPFC
Enzyme 8 Number of Residues 237
Enzyme 8 Molecular Weight 26091
Enzyme 8 Theoretical pI 7.56
Enzyme 8 GO Classification
Function
  • catalytic activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
  • ribose-5-phosphate isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • pentose-phosphate shunt
  • pentose-phosphate shunt, non-oxidative branch
  • physiological process
Component
—
Enzyme 8 General Function Carbohydrate transport and metabolism
Enzyme 8 Specific Function D-ribose 5-phosphate = D-ribulose 5-phosphate
Enzyme 8 Pathways
Enzyme 8 Reactions
  • D-ribose 5-phosphate = D-ribulose 5-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 114325416 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P49247 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name RPIA_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >936 bp 
ATGCAGCGCCCCGGGCCCTTCAGCACCCTCTACGGGCGGGTCTTGGCCCCGCTGCCCGGG
AGGGCCGGGGGCGCGGCCTCCGGCGGAGGAGGGAACAGCTGGGACCTCCCGGGTTCCCAC
GTGCGGCTGCCGGGGCGTGCACAGTCTGGGACCCGTGGCGGTGCTGGCAACACAAGCACC
AGCTGCGGGGACTCCAACAGCATCTGCCCGGCCCCCTCCACGATGTCCAAGGCCGAGGAG
GCCAAGAAGCTGGCGGGCCGCGCGGCTGTGGAGAACCACGTGAGGAATAACCAAGTGCTG
GGAATTGGAAGTGGTTCTACAATTGTCCATGCTGTGCAGCGAATAGCTGAAAGGGTGAAG
CAAGAGAATCTGAACCTCGTCTGTATTCCCACTTCCTTCCAGGCCCGCCAGCTCATCCTG
CAGTATGGCTTGACCCTCAGTGATCTGGATCGACACCCAGAGATCGACCTTGCCATCGAT
GGTGCTGATGAAGTAGATGCTGATCTCAATCTCATCAAGGGTGGCGGAGGCTGCCTGACC
CAGGAGAAGATTGTGGCTGGCTATGCTAGTCGCTTCATCGTGATCGCTGATTTCAGGAAA
GATTCGAAGAATCTCGGGGATCAGTGGCACAAGGGAATCCCCATCGAGGTCATCCCAATG
GCCTATGTCCCAGTGAGCCGAGCTGTGAGCCAGAAGTTTGGGGGCGTGGTTGAACTTCGA
ATGGCTGTCAACAAGGCTGGTCCTGTGGTGACAGATAATGGGAATTTTATCTTGGACTGG
AAGTTTGACCGGGTACACAAATGGAGTGAAGTGAATACAGCTATCAAAATGATCCCAGGT
GTGGTGGACACAGGCCTATTCATCAACATGGCTGAGAGAGTCTACTTTGGGATGCAGGAT
GGCTCAGTGAACATGAGGGAGAAGCCTTTCTGTTGA
Enzyme 8 GenBank Gene ID BC015529 Link Image
Enzyme 8 GeneCard ID RPIA Link Image
Enzyme 8 GenAtlas ID RPIA Link Image
Enzyme 8 HGNC ID HGNC:10297 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Apel TW, Scherer A, Adachi T, Auch D, Ayane M, Reth M: The ribose 5-phosphate isomerase-encoding gene is located immediately downstream from that encoding murine immunoglobulin kappa. Gene. 1995 Apr 24;156(2):191-7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 12873
Enzyme 9 Name Transketolase-like protein 2
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name TKTL2
Enzyme 9 Protein Sequence >Transketolase-like protein 2 
MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYK
QTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVD
VATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLV
AVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPT
AIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQI
SITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHP
ERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSH
CGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTSQPE
TAVIYTPQENFEIGQAKVVRHGVNDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFT
IKPLDAATIISSAKATGGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVPQRG
KTSELLDMFGISTRHIIAAVTLTLMK
Enzyme 9 Number of Residues 626
Enzyme 9 Molecular Weight 67878
Enzyme 9 Theoretical pI Not Available
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring aldehyde or ketonic groups
  • transketolase activity
Process
—
Component
—
Enzyme 9 General Function Energy production and conversion
Enzyme 9 Specific Function Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate [RN:R07246] ALL_REAC R07246 > R01641
  • (other) R01067 R01830 R06590 R06861 R06863
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 16552972 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9H0I9 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name TKTL2_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 AK057325 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID TKTL2 Link Image
Enzyme 9 HGNC ID HGNC:25313 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 13080
Enzyme 10 Name cDNA FLJ76204, highly similar to Homo sapiens transketolase
Enzyme 10 Synonyms
  1. Wernicke- Korsakoff syndrome
  2. TKT, mRNA
  3. Transketolase
  4. Wernicke-Korsakoff syndrome, isoform CRA_a
Enzyme 10 Gene Name TKT
Enzyme 10 Protein Sequence >cDNA FLJ76204, highly similar to Homo sapiens transketolase 
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKS
QDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDV
ATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVA
ILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIA
KTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIAN
IRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFI
ECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVS
IGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAII
YNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPL
DRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAE
LLKMFGIDRDAIAQAVRGLITKA
Enzyme 10 Number of Residues 623
Enzyme 10 Molecular Weight 67878
Enzyme 10 Theoretical pI 7.73
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Energy production and conversion
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 158259931 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID A8K089 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name A8K089_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK289454 Link Image
Enzyme 10 GeneCard ID A8K089 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 13090
Enzyme 11 Name cDNA FLJ76398, highly similar to Homo sapiens nudix
Enzyme 11 Synonyms
  1. nucleoside diphosphate linked moiety X-type motif 5
  2. NUDT5, mRNA
  3. Nudix
  4. Nucleoside diphosphate linked moiety X-type motif 5, isoform CRA_c
Enzyme 11 Gene Name NUDT5
Enzyme 11 Protein Sequence >cDNA FLJ76398, highly similar to Homo sapiens nudix 
MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTAD
GVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYK
GDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQ
RLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF
Enzyme 11 Number of Residues 219
Enzyme 11 Molecular Weight 24328
Enzyme 11 Theoretical pI 4.59
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Replication, recombination and repair
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function Not Available
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 158255698 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID A8K516 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name A8K516_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK291131 Link Image
Enzyme 11 GeneCard ID A8K516 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 15073
Enzyme 12 Name CDNA FLJ14389 fis, clone HEMBA1002876
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name Not Available
Enzyme 12 Protein Sequence >CDNA FLJ14389 fis, clone HEMBA1002876 
MAGRLLGKALAAVSLSLALASVTIRSSRCRGIQAFRNSFSSSWFHLNTNVMSGSNGSKEN
SHNKARTSPYPGSKVERSQVPNEKVGWLVEWQDYKPVEYTAVSVLAGPRWADPQISESNF
SPKFNEKDGHVERKSKNGLYEIENGRPRNPAGRTGLVGRGLLGRWGPNHAADPIITRWKR
DSSGNKIMHPVSGKHILQFVAIKRKDCGEWAIPGGMVDPGEKISATLKREFGEEALNSLQ
KTSAEKREIEEKLHKLFSQDHLVIYKGYVDDPRNTDNACMETEAVNYHDETGEIMDNLML
EAGDDAGKVKWVDINDKLKLYASHSQFIKLVAEKRDAHWSEDSEADCHAL
Enzyme 12 Number of Residues 350
Enzyme 12 Molecular Weight 39042
Enzyme 12 Theoretical pI 8.32
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 14041880 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q96KB3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q96KB3_HUMAN Link Image
Enzyme 12 PDB ID 1QVJ Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1053 bp 
ATGGCGGGACGCCTCCTGGGAAAGGCTTTAGCCGCGGTGTCTCTCTCTCTGGCCTTGGCC
TCTGTGACTATCAGGTCCTCGCGCTGCCGCGGCATCCAGGCGTTCAGAAACTCGTTTTCA
TCTTCTTGGTTTCATCTTAATACCAACGTCATGTCTGGTTCTAATGGTTCCAAAGAAAAT
TCTCACAATAAGGCTCGGACGTCTCCTTACCCAGGTTCAAAAGTTGAACGAAGCCAGGTT
CCTAATGAGAAAGTGGGCTGGCTTGTTGAGTGGCAAGACTATAAGCCTGTGGAATACACT
GCAGTCTCTGTCTTGGCTGGACCCAGGTGGGCAGATCCTCAGATCAGTGAAAGTAATTTT
TCTCCCAAGTTTAACGAAAAGGATGGGCATGTTGAGAGAAAGAGCAAGAATGGCCTGTAT
GAGATTGAAAATGGAAGACCGAGAAATCCTGCAGGACGGACTGGACTGGTGGGCCGGGGG
CTTTTGGGGCGATGGGGCCCAAATCACGCTGCAGATCCCATTATAACCAGATGGAAAAGG
GATAGCAGTGGAAATAAAATCATGCATCCTGTTTCTGGGAAGCATATCTTACAATTTGTT
GCAATAAAAAGGAAAGACTGTGGAGAATGGGCAATCCCAGGGGGGATGGTGGATCCAGGA
GAGAAGATTAGTGCCACACTGAAAAGAGAATTTGGTGAGGAAGCTCTCAACTCCTTACAG
AAAACCAGTGCTGAGAAGAGAGAAATAGAGGAAAAGTTGCACAAACTCTTCAGCCAAGAC
CACCTAGTGATATATAAGGGATATGTTGATGATCCTCGAAACACTGATAATGCATGTATG
GAGACAGAAGCTGTGAACTACCATGACGAAACAGGTGAGATAATGGATAATCTTATGCTA
GAAGCTGGAGATGATGCTGGAAAAGTGAAATGGGTGGACATCAATGATAAACTGAAGCTT
TATGCCAGTCACTCTCAATTCATCAAACTTGTGGCTGAGAAACGAGATGCACACTGGAGC
GAGGACTCTGAAGCTGACTGCCATGCGTTGTAG
Enzyme 12 GenBank Gene ID AK027295 Link Image
Enzyme 12 GeneCard ID Q96KB3 Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID HGNC:8056 Link Image
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
Enzyme 12 SNPs Not Available
Enzyme 12 General References Not Available
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16641
Enzyme 13 Name cDNA, FLJ95330, Homo sapiens phosphoglucomutase 3 (PGM3), mRNA (Phosphoglucomutase 3, isoform CRA_d)
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name PGM3
Enzyme 13 Protein Sequence >cDNA, FLJ95330, Homo sapiens phosphoglucomutase 3 (PGM3), mRNA (Phosphoglucomutase 3, isoform CRA_d) 
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVM
VTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQD
AFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATI
EGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDG
SKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDK
IATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKA
QEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAI
SDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEA
INDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQP
GF
Enzyme 13 Number of Residues 542
Enzyme 13 Molecular Weight 59853
Enzyme 13 Theoretical pI 6.21
Enzyme 13 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID B2RB65 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name B2RB65_HUMAN Link Image
Enzyme 13 PDB ID 1WJW Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence Not Available
Enzyme 13 GenBank Gene ID AK314512 Link Image
Enzyme 13 GeneCard ID B2RB65 Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus Not Available
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16926
Enzyme 14 Name Ribose-phosphate pyrophosphokinase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name PRPS2
Enzyme 14 Protein Sequence >Ribose-phosphate pyrophosphokinase 
MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGC
GEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENIAEWKNCIIVSPDAGGAKRYHA
GYTLQISPSADWFFLFRCIR
Enzyme 14 Number of Residues 200
Enzyme 14 Molecular Weight 22149
Enzyme 14 Theoretical pI 6.51
Enzyme 14 GO Classification
Function
  • catalytic activity
  • diphosphotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lipoate-protein ligase B activity
  • lipoate-protein ligase activity
  • ribose phosphate diphosphokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside monophosphate biosynthesis
  • nucleoside monophosphate metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 14 General Function Nucleotide transport and metabolism
Enzyme 14 Specific Function ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function Not Available
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID A6NMS2 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A6NMS2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AC005859 Link Image
Enzyme 14 GeneCard ID A6NMS2 Link Image
Enzyme 14 GenAtlas ID PRPS2 Link Image
Enzyme 14 HGNC ID HGNC:9465 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References Not Available
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16927
Enzyme 15 Name Ribose-phosphate pyrophosphokinase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name Not Available
Enzyme 15 Protein Sequence >Ribose-phosphate pyrophosphokinase 
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSEAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
Enzyme 15 Number of Residues 318
Enzyme 15 Molecular Weight 34865
Enzyme 15 Theoretical pI 6.78
Enzyme 15 GO Classification
Function
  • catalytic activity
  • diphosphotransferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lipoate-protein ligase B activity
  • lipoate-protein ligase activity
  • ribose phosphate diphosphokinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside metabolism
  • nucleoside monophosphate biosynthesis
  • nucleoside monophosphate metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 15 General Function Nucleotide transport and metabolism
Enzyme 15 Specific Function ATP + D-ribose 5-phosphate = AMP + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q53FW2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q53FW2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AK223169 Link Image
Enzyme 15 GeneCard ID Q53FW2 Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID HGNC:9462 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs Not Available
Enzyme 15 General References
  1. Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed Link Image]
  2. Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available