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Human Metabolome Database Version 2.5

 

Showing metabocard for Glucose 1-phosphate (HMDB01586)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-20 22:13:08
Update Date 2010-04-13 00:22:10
Accession Number HMDB01586
Secondary Accession Numbers HMDB01306
Common Name Glucose 1-phosphate
Description The direct product of the reaction in which glycogen phosphorylase cleaves off a molecule of glucose from a greater glycogen structure. It cannot travel down many metabolic pathways and must be interconverted by the enzyme phosphoglucomutase in order to become glucose 6-phosphate. Free glucose 1-phosphate can also react with UTP to form UDP-glucose. It can then return to the greater glycogen structure via glycogen synthase.
Synonyms
  1. Cori ester
  2. D-Glucopyranose 1-phosphate
  3. D-Glucose-1-phosphate
  4. D-glucose 1-phosphate
  5. D-glucose-1-P
  6. Glucose 1-phosphate
  7. Glucose 1-phosphic acid
  8. Glucose monophosphate
  9. Glucose-1-phosphate
  10. a-D-Glucopyranosyl phosphate
  11. a-D-Glucose 1-phosphate
  12. glucose-1P
  13. alpha-d-glucose-1-phosphate
  14. delta-Glucopyranose 1-phosphate
  15. delta-Glucose-1-phosphate
  16. delta-glucose 1-phosphate
  17. delta-glucose-1-P
  18. alpha-delta-Glucopyranosyl phosphate
  19. alpha-delta-Glucose 1-phosphate
  20. alpha-delta-glucose-1-phosphate
  21. alpha-D-Glucopyranosyl phosphate
  22. alpha-D-Glucose 1-phosphate
Chemical IUPAC Name [(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyphosphonic acid
Chemical Formula C6H13O9P
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
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
  • Component of Starch and sucrose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 260.136
Monoisotopic Molecular Weight 260.029724
Isomeric SMILES OC[C@H]1OC(OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O
Canonical SMILES OCC1OC(OP(O)(O)=O)C(O)C(O)C1O
KEGG Compound ID C00103 Link Image
BioCyc ID GLC-1-P Link Image
BiGG ID 33865 Link Image
Wikipedia Link Glucose 1-phosphate Link Image
NuGOwiki Link HMDB01586 Link Image
Metagene Link HMDB01586 Link Image
METLIN ID 6331 Link Image
PubChem Compound 65533 Link Image
PubChem Substance 841543 Link Image
ChEBI ID 29042 Link Image
CAS Registry Number 59-56-3
InChI Identifier InChI=1/C6H13O9P/c7-1-2-3(8)4(9)5(10)6(14-2)15-16(11,12)13/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5-,6?/m1/s1
Synthesis Reference Weinhausel, Andreas; Nidetzky, Bernd; Kysela, Christian; Kulbe, Klaus D. Application of Escherichia coli maltodextrin-phosphorylase for the continuous production of glucose-1-phosphate. Enzyme and Microbial Technology (1995), 17(2), 140-6.
Melting Point (Experimental) Not Available
Experimental Water Solubility 1000.0 mg/mL [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 32.3 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.00 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP]; -3.79 [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 Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
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 (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Galactose Metabolism SMP00043 Link Image map00052 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Lactose Synthesis SMP00444 Link Image
Nucleotide Sugars Metabolism SMP00010 Link Image map00520 Link Image
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References
  1. Kamei A: Glycation and insolubility of human lens protein. Chem Pharm Bull (Tokyo). 1992 Oct;40(10):2787-91. [PubMed Link Image]
  2. Bollaert PE, Levy B, Nace L, Laterre PF, Larcan A: Hemodynamic and metabolic effects of rapid correction of hypophosphatemia in patients with septic shock. Chest. 1995 Jun;107(6):1698-701. [PubMed Link Image]
  3. Reinken L, Obladen M, Dockx-Reinken F, Lindemann C: [The effect of osteopenia prevention in very small premature infants on hormonal parameters of calcium metabolism and bone mineralization] Klin Padiatr. 1989 May-Jun;201(3):177-82. [PubMed Link Image]
  4. Nakashima H, Suo H, Ochiai J, Sugie H, Kawamura Y: [A case of adult onset phosphoglucomutase deficiency] Rinsho Shinkeigaku. 1992 Jan;32(1):42-7. [PubMed Link Image]
  5. Yamada Y, Kono N, Nakajima H, Shimizu T, Kiyokawa H, Kawachi M, Ono A, Nishimura T, Kuwajima M, Tarui S: Low glucose-1, 6-bisphosphate and high fructose-2, 6-bisphosphate concentrations in muscles of patients with glycogenosis types VII and V. Biochem Biophys Res Commun. 1991 Apr 15;176(1):7-10. [PubMed Link Image]
  6. Leuzzi R, Fulceri R, Marcolongo P, Banhegyi G, Zammarchi E, Stafford K, Burchell A, Benedetti A: Glucose 6-phosphate transport in fibroblast microsomes from glycogen storage disease type 1b patients: evidence for multiple glucose 6-phosphate transport systems. Biochem J. 2001 Jul 15;357(Pt 2):557-62. [PubMed Link Image]
  7. Kamei A, Kato M: Contribution of glycation to human lens coloration. Chem Pharm Bull (Tokyo). 1991 May;39(5):1272-6. [PubMed Link Image]
  8. Mahadevan-Jansen A, Mitchell MF, Ramanujam N, Malpica A, Thomsen S, Utzinger U, Richards-Kortum R: Near-infrared Raman spectroscopy for in vitro detection of cervical precancers. Photochem Photobiol. 1998 Jul;68(1):123-32. [PubMed Link Image]
  9. Kodentsova VM, Glinka EIu: [Changes in kinetic properties of pyridoxal-dependent enzymes during dietary vitamin B6 deficiency in rats] Ukr Biokhim Zh. 1990 Jan-Feb;62(1):44-9. [PubMed Link Image]
  10. Gannon MC, Khan MA, Nuttall FQ: Glucose appearance rate after the ingestion of galactose. Metabolism. 2001 Jan;50(1):93-8. [PubMed Link Image]
  11. Chen YT, Kato T: Liver-specific glucose-6-phosphatase is not present in human placenta. J Inherit Metab Dis. 1985;8(2):92-4. [PubMed Link Image]
  12. Krause EG, Will H, Bohm M, Wollenberger A: The assay of glycogen phosphorylase in human blood serum and its application to the diagnosis of myocardial infarction. Clin Chim Acta. 1975 Jan 20;58(2):145-54. [PubMed Link Image]
  13. Suzuki K, Kayamori Y, Katayama Y: Development of an enzymatic method for the assay of serum magnesium using phosphoglucomutase and glucose-6-phosphate dehydrogenase. Clin Biochem. 1991 Jun;24(3):249-53. [PubMed Link Image]
  14. Lang A, Groebe H, Hellkuhl B, von Figura K: A new variant of galactosemia: galactose-1-phosphate uridylytransferase sensitive to product inhibition by glucose 1-phosphate. Pediatr Res. 1980 May;14(5):729-34. [PubMed Link Image]
  15. Gella FJ, Cusso R: Glycogen phosphorylase from normal and leukemic human leucocytes: kinetic parameters of the active form. Rev Esp Fisiol. 1980 Mar;36(1):1-6. [PubMed Link Image]
  16. Pezzarossa A, Cavazzini G, Coscelli C, Butturini U: [Modifications induced by glucose-1-phosphate on carbohydrate utilization curve after venous loading. Results in normal subjects (preliminary note)] Boll Soc Ital Biol Sper. 1972 Jun 30;48(12):318-21. [PubMed Link Image]
  17. Lai K, Elsas LJ: Structure-function analyses of a common mutation in blacks with transferase-deficiency galactosemia. Mol Genet Metab. 2001 Sep-Oct;74(1-2):264-72. [PubMed Link Image]
  18. Palombi M, Bochicchio O, Gargiulo M, Sammarco M: [Alternative therapy of deep venous thrombosis in patients at hemorrhagic risk] Minerva Chir. 1994 Mar;49(3):189-94. [PubMed Link Image]
  19. Arthur PG, Kent JC, Hartmann PE: Microanalysis of the metabolic intermediates of lactose synthesis in human milk and plasma using bioluminescent methods. Anal Biochem. 1989 Feb 1;176(2):449-56. [PubMed Link Image]
  20. Lederer B, Van Hoof F, Van den Berghe G, Hers H: Glycogen phosphorylase and its converter enzymes in haemolysates of normal human subjects and of patients with type VI glycogen-storage disease. A study of phosphorylase kinase deficiency. Biochem J. 1975 Apr;147(1):23-35. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  2. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  3. Glycogen phosphorylase, liver form
  4. Glycogen phosphorylase, muscle form
  5. Glycogen phosphorylase, brain form
  6. UTP--glucose-1-phosphate uridylyltransferase 2
  7. Galactose-1-phosphate uridylyltransferase
  8. Uridine diphosphate glucose pyrophosphatase
  9. Phosphoglucomutase-1
  10. Phosphoglucomutase-2
  11. cDNA FLJ77760, highly similar to Homo sapiens glucosidase, beta; acid
  12. Glucose 1,6-bisphosphate synthase
  13. cDNA, FLJ95330, Homo sapiens phosphoglucomutase 3 (PGM3), mRNA (Phosphoglucomutase 3, isoform CRA_d)
  14. Galactose-1-phosphate uridylyltransferase
Enzyme 1 [top]
Enzyme 1 ID 5351
Enzyme 1 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 1 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 1 Gene Name ENPP1
Enzyme 1 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 1 Number of Residues 925
Enzyme 1 Molecular Weight 104925
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 77-97
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189650 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2622 bp
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 1 GenBank Gene ID M57736 Link Image
Enzyme 1 GeneCard ID ENPP1 Link Image
Enzyme 1 GenAtlas ID ENPP1 Link Image
Enzyme 1 HGNC ID HGNC:3356 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6q22-q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5426
Enzyme 2 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Enzyme 2 Synonyms
  1. E- NPP 3
  2. Phosphodiesterase I/nucleotide pyrophosphatase 3
  3. Phosphodiesterase I beta
  4. PD-Ibeta
  5. CD203c antigen[Includes: Alkaline phosphodiesterase I
  6. NPPase]
Enzyme 2 Gene Name ENPP3
Enzyme 2 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
Enzyme 2 Number of Residues 875
Enzyme 2 Molecular Weight 100097
Enzyme 2 Theoretical pI 6.55
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-38
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 2465540 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14638 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENPP3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2628 bp
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
Enzyme 2 GenBank Gene ID AF005632 Link Image
Enzyme 2 GeneCard ID ENPP3 Link Image
Enzyme 2 GenAtlas ID ENPP3 Link Image
Enzyme 2 HGNC ID HGNC:3358 Link Image
Enzyme 2 Chromosome Location 6
Enzyme 2 Locus 6q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5606
Enzyme 3 Name Glycogen phosphorylase, liver form
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name PYGL
Enzyme 3 Protein Sequence >Glycogen phosphorylase, liver form
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTV
RDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEA
DDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVN
TMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKL
PWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFP
KDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKF
QNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQ
ENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFV
PRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPA
TDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVA
ALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEA
YVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNE
SNKVNGN
Enzyme 3 Number of Residues 847
Enzyme 3 Molecular Weight 97150
Enzyme 3 Theoretical pI 7.17
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-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 183353 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P06737 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PYGL_HUMAN Link Image
Enzyme 3 PDB ID 1L7X Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2544 bp
ATGGGCGAACCGCTGACAGACCAGGAGAAGCGGCGGCAGATCAGCATCCGCGGCATCGTG
GGCGTGGAGAACGTGGCAGAGCTGAAGAAGAGTTTCAACCGGCACCTGCACTTCACGCTG
GTCAAGGACCGCAACGTGGCCACCACCCGCGACTACTACTTCGCGCTGGCGCACACGGTG
CGGGACCACCTGGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTACGACAAGTGCCCC
AAGAGGGAATATTACCTCTCTCTGGAATTTTACATGGGCCGAACATTACAGAACACCATG
ATCAACCTCGGTCTGCAAAATGCCTGTGATGAGGCCATTTACCAGCTTGGATTGGATATA
GAAGAGTTAGAAGAAATTGAAGAAGATGCTGGACTTGGCAATGGTGGTCTTGGGAGACTT
GCTGCCTGCTTCTTGGATTCCATGGCAACCCTGGGACTTGCAGCCTATGGATACGGCATT
CGGTATGAATATGGGATTTTCAATCAGAAGATCCGAGATGGATGGCAGGTAGAAGAAGCA
GATGATTGGCTCAGATATGGAAACCCTTGGGAGAAGTCCCGCCCAGAATTCATGCTGCCT
GTGCACTTCTATGGAAAAGTAGAACACACCAACACCGGGACCAAGTGGATTGACACTCAA
GTGGTCCTGGCTCTGCCATATGACACCCCCGAGCCCGGCTACATGAATAACACTGTCAAC
ACCATGCGCCTCTGGTCTGCTCGGGCACCAAATGACTTTAACCTCAGAGACTTTAATGTT
GGAGACTACATTCAGGCTGTGCTGGACCGAAACCTGGCCGAGAACATCTCCCGGGTCCTC
TATCCCAATGACAATTTTTTTGAAGGGAAGGAGCTAAGATTGAAGCAGGAATACTTTGTG
GTGGCTGCAACCTTGCAAGATATCATCCGCCGTTTCAAAGCCTCCAAGTTTGGCTCCACC
CGTGGTCAAGGAACTGTGTTTGATGCCTTCCCGGATCAGGTGGCCATCCAGCTGAATGAT
ACTCACCCTCGCATCGCGATCCCTGAGCTGATGAGGATTTTTGTGGATATTGAAAAACTG
CCCTGGTCCAAGGCATGGGAGCTCAACCAGAAGACCTTCGCCTACACCAACCACACAGTG
CTCCCGGAAGCCCTGGAGCGCTGGCCCGTGGACCTGGTGGAGAAGCTGCTCCCTCGACAT
TTGGAAATCATTTATGAGATAAATCAGAAGCATTTAGATAGAATTGTGGCCTTGTTTCCT
AAAGATGTGGACCCTCTGAGAAGGATGTCTCTGATAGAAGAGGAAGGAAGCAAAAGGATC
AACATGGCCCATCTCTGCATTGTCGGTTCCCATGCTGTGAATGGCGTGGCTAAAATCCAC
TCAGACATCGTGAAGACTAAAGTATTCAAGGACTTCAGTGAGCTAGAACCTGACAAGTTT
CAGAATAAAACCAATGGGATCACTCCAAGGCGCTGGCTCCTACTCTGCAACCCAGGACTT
GCAGAGCTCATAGCAGAGAAAATTGGAGAAGACTATGTGAAAGACCTGAGCCAGCTGACG
AAGCTCCACAGCTTCCTGGGTGATGATGTCTTCCTCCGGGAACTCGCCAAGGTGAAGCAG
GAGAATAAGCTGAAGTTTTCTCAGTTCCTGGAGACGGAGTACAAAGTGAAGATCAACCCA
TCCTCCATGTTTGATGTCCAGGTGAAGAGGATACATGAGTACAAGCGACAGCTCTTGAAC
TGTCTGCATGTGATCACGATGTACAACCGCATTAAGAAAGACCCTAAGAAGTTATTCGTG
CCAAGGACAGTTATCATTGGTGGTAAAGCTGCCCCAGGATATCACATGGCCAAAATGATC
ATAAAGCTGATCACTTCAGTGGCAGATGTGGTGAACAATGACCCTATGGTTGGAAGCAAG
TTGAAAGTCATCTTCTTGGAGAACTACAGAGTATCTCTTGCTGAAAAAGTCATTCCAGCC
ACAGATCTGTCAGAGCAGATTTCCACTGCAGGCACCGAAGCCTCGGGGACAGGCAATATG
AAGTTCATGCTAAATGGGGCCCTAACTATCGGGACCATGGATGGGGCCAATGTGGAAATG
GCAGAAGAAGCTGGGGAAGAGAACCTGTTCATCTTTGGCATGAGCATAGATGATGTGGCT
GCTTTGGACAAGAAAGGGTACGAGGCAAAAGAATACTATGAGGCACTTCCAGAGCTGAAG
CTGGTCATTGATCAAATTGACAATGGCTTTTTTTCTCCCAAGCAGCCTGACCTCTTCAAA
GATATCATCAACATGCTATTTTATCATGACAGGTTTAAAGTCTTTGCAGACTACGAAGCC
TATGTCAAGTGTCAAGATAAAGTGAGTCAGCTGTACATGAATCCAAAGGCCTGGAACACA
ATGGTACTCAAAAACATAGCTGCCTCGGGGAAATTCTCCAGTGACCGAACAATTAAAGAA
TATGCCCAAAACATCTGGAACGTGGAACCTTCAGATCTAAAGATTTCTCTATCCAATGAA
TCTAACAAAGTCAATGGAAATTGA
Enzyme 3 GenBank Gene ID M14636 Link Image
Enzyme 3 GeneCard ID PYGL Link Image
Enzyme 3 GenAtlas ID PYGL Link Image
Enzyme 3 HGNC ID HGNC:9725 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q21-q22
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Newgard CB, Nakano K, Hwang PK, Fletterick RJ: Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8132-6. [PubMed Link Image]
  2. Chang S, Rosenberg MJ, Morton H, Francomano CA, Biesecker LG: Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI. Hum Mol Genet. 1998 May;7(5):865-70. [PubMed Link Image]
  3. Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW: Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. [PubMed Link Image]
  4. Gorin FA, Mullinax RL, Ignacio PC, Neve RL, Kurnit DM: McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues. J Neurogenet. 1987 Dec;4(6):293-308. [PubMed Link Image]
  5. Rath VL, Ammirati M, Danley DE, Ekstrom JL, Gibbs EM, Hynes TR, Mathiowetz AM, McPherson RK, Olson TV, Treadway JL, Hoover DJ: Human liver glycogen phosphorylase inhibitors bind at a new allosteric site. Chem Biol. 2000 Sep;7(9):677-82. [PubMed Link Image]
  6. Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J: Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core. Mol Cell. 2000 Jul;6(1):139-48. [PubMed Link Image]
  7. Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL: Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase. Chem Biol. 2002 Aug;9(8):915-24. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5610
Enzyme 4 Name Glycogen phosphorylase, muscle form
Enzyme 4 Synonyms
  1. Myophosphorylase
Enzyme 4 Gene Name PYGM
Enzyme 4 Protein Sequence >Glycogen phosphorylase, muscle form
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI
Enzyme 4 Number of Residues 842
Enzyme 4 Molecular Weight 97093
Enzyme 4 Theoretical pI 7.03
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-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 190784 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P11217 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PYGM_HUMAN Link Image
Enzyme 4 PDB ID 1XL1 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2529 bp
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGGTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAGGATCTACTACCTGTCTTTAGAGTTCTATATGGGACGGACGCTACAGAACACCATG
GTGAACCTGGCCTTAGAGAATGCCTGTGACGAGGCCACCTACCAGCTGGGCCTGGACATG
GAGGAGCTGGAGGAAATTGAGGAGGATGCGGGGCTGGGCAACGGGGGCCTGGGCCGGCTG
GCAGCCTGCTTTCTTGACTCCATGGCAACACTGGGCCTGGCTGCCTATGGCTACGGGATT
CGCTATGAGTTTGGGATTTTTAACCAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCC
GATGACTGGCTTCGCTACGGCAACCCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCT
GTGCACTTCTACGGCCATGTGGAGCACACCAGCCAGGGTGCCAAGTGGGTGGACACACAG
GTGGTACTGGCCATGCCCTACGATACCCCGGTGCCTGGCTATCGCAACAATGTTGTCAAC
ACCATGCGCCTCTGGTCTGCCAAGGCTCCCAATGACTTCAACCTCAAGGACTTCAATGTC
GGTGGCTACATCCAGGCTGTGTTGGACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTG
TACCCCAATGATAATTTCTTCGAAGGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTG
GTGGCTGCCACCCTCCAGGACATCATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGT
GATCCCGTGCGCACGAACTTCGATGCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGAC
ACCCACCCCTCCCTGGCCATCCCCGAGCTGATGAGGATCCTGGTGGACCTGGAACGGATG
GACTGGGACAAGGCGTGGGATGTGACAGTGAGGACCTGTGCCTACACCAACCACACGGTG
CTGCCCGAGGCCCTGGAGCGCTGGCCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCAC
CTCCAGATCATCTACGAGATCAACCAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCA
GGGGACGTAGACCGGCTGCGGCGCATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATC
AACATGGCACACCTGTGCATCGCGGGGTCGCACGCCGTCAACGGTGTGGCCCGCATCCAC
TCGGAGATCCTCAAGAAGACCATCTTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTC
CAGAATAAGACCAACGGCATCACCCCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTG
GCAGAGGTCATTGCTGAGCGCATCGGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGC
AAACTGCTCTCCTTTGTGGATGATGAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAG
GAAAACAAGTTGAAGTTTGCTGCCTACCTAGAGAGGGAATACAAAGTCCACATCAACCCC
AACTCACTCTTCGACATCCAGGTGAAGCGGATTCACGAATATAAACGACAGCTCCTCAAC
TGCCTCCATGTCATCACCCTGTACAACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTG
CCTCGGACTGTGATGATTGGAGGGAAGGCTGCACCTGGGTACCACATGGCCAAGATGATC
ATCAGACTCGTCACAGCCATCGGGGATGTGGTCAACCATGACCCGGCAGTGGGTGACCGC
CTCCGTGTCATCTTCCTGGAGAACTACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCT
GCAGACCTCTCTGAGCAGATCTCCACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATG
AAGTTCATGCTCAACGGGGCTCTGACCATTGGCACCATGGACGGGGCCAATGTGGAGATG
GCAGAAGAGGCGGGAGAGGAAAACTTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGAT
AAGCTTGACCAAAGAGGGTACAATGCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGG
CAGGTCATTGAGCAGCTGAGCAGTGGCTTCTTCTCCCCCAAACAACCCGACCTGTTCAAG
GACATTGTCAATATGCTCATGCACCATGACCGGTTTAAAGTCTTCGCAGATTATGAAGAC
TACATTAAATGCCAGGAGAAAGTCAGCGCCTGGTACAAGAACCCAAGAGAGTGGACGCGG
ATGGTGATCCGGAACATAGCCACTTCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAG
TATGCCCGGGAGATCTGGGGTGTGGAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAG
GCCATCTGA
Enzyme 4 GenBank Gene ID M32598 Link Image
Enzyme 4 GeneCard ID PYGM Link Image
Enzyme 4 GenAtlas ID PYGM Link Image
Enzyme 4 HGNC ID HGNC:9726 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q12-q13.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [PubMed Link Image]
  2. Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [PubMed Link Image]
  3. Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [PubMed Link Image]
  4. Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [PubMed Link Image]
  5. Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [PubMed Link Image]
  6. Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve. 1995;3:S23-7. [PubMed Link Image]
  7. Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [PubMed Link Image]
  8. Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [PubMed Link Image]
  9. Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [PubMed Link Image]
  10. Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [PubMed Link Image]
  11. Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [PubMed Link Image]
  12. Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [PubMed Link Image]
  13. Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [PubMed Link Image]
  14. Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [PubMed Link Image]
  15. Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [PubMed Link Image]
  16. Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5612
Enzyme 5 Name Glycogen phosphorylase, brain form
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name PYGB
Enzyme 5 Protein Sequence >Glycogen phosphorylase, brain form
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
Enzyme 5 Number of Residues 843
Enzyme 5 Molecular Weight 96697
Enzyme 5 Theoretical pI 6.85
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • phosphorylase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
  • vitamin binding
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties
Enzyme 5 Pathways
Enzyme 5 Reactions
  • (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-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 307200 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P11216 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PYGB_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2592 bp
ATGGGCGAACCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGAATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCAAGGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGGCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGCTTCAGCACCTGCCCCAC
CCAGAGTGGGAGTCAGGTGGAGCCACCTGCTGGGCTCCCCCAGAACTTTGCACACATCTT
GCTATGTATTAG
Enzyme 5 GenBank Gene ID J03544 Link Image
Enzyme 5 GeneCard ID PYGB Link Image
Enzyme 5 GenAtlas ID PYGB Link Image
Enzyme 5 HGNC ID HGNC:9723 Link Image
Enzyme 5 Chromosome Location 20
Enzyme 5 Locus 20p11.2-p11.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed Link Image]
  2. Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6363
Enzyme 6 Name UTP--glucose-1-phosphate uridylyltransferase 2
Enzyme 6 Synonyms
  1. UDP- glucose pyrophosphorylase 2
  2. UDPGP 2
  3. UGPase 2
Enzyme 6 Gene Name UGP2
Enzyme 6 Protein Sequence >UTP--glucose-1-phosphate uridylyltransferase 2
MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTASSHEFEHTKKDLDGFRK
LFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTS
MGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNH
CRVKIYTFNQSRYPRINKESLLPVAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFI
GEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEG
KLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLD
GGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSE
KREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIA
NHGDRIDIPPGAVLENKIVSGNLRILDH
Enzyme 6 Number of Residues 508
Enzyme 6 Molecular Weight 56941
Enzyme 6 Theoretical pI 8.40
Enzyme 6 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Plays a central role as a glucosyl donor in cellular metabolic pathways
Enzyme 6 Pathways
Enzyme 6 Reactions
  • UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 881394 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q16851 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name UGPA2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1494 bp
ATGTCTCAAGATGGTGCTTCTCAGTTCCAAGAAGTCATTCGGCAAGAGCTAGAATTATCT
GTGAAGAAGGAACTAGAAAAAATACTCACCACAGCATCATCACATGAATTTGAGCACACC
AAAAAAGACCTGGATGGATTTCGGAAGCTATTTCATAGATTTTTGCAAGAAAAGGGGCCT
TCTGTGGATTGGGGAAAAATCCAGAGACCCCCTGAAGATTCGATTCAACCCTATGAAAAG
ATAAAGGCCAGGGGCCTGCCTGATAATATATCTTCCGTGTTGAACAAACTAGTGGTGGTG
AAACTCAATGGTGGTTTGGGAACCAGCATGGGCTGCAAAGGCCCTAAAAGTCTGATTGGT
GTGAGGAATGAGAATACCTTTCTGGATCTGACTGTTCAGCAAATTGAACATTTGAACAAA
ACCTACAATACAGATGTCCCTCTTGTTTTAATGAACTCTTTTAACACGGATGAAGATACC
AAAAAAATACTACAGAAGTACAATCATTGTCGTGTGAAAATCTACACTTTCAATCAAAGC
AGGTACCCGAGGATTAATAAAGAATCTTTACGGCCTGTAGCAAAGGACGTGTCTTACTCA
GGGGAAAATACAGAAGCTTGGTACCCTCCAGGTCATGGTGATATTTACGCCAGTTTCTAC
AACTCTGGATTGCTTGATACCTTTATAGGAGAAGGCAAAGAGTATATTTTTGTGTCTAAC
ATAGATAATCTGGGTGCCACAGTGGATCTGTATATTCTTAATCATCTAATCAACCCACCC
AATGGAAAACGCTGTGAATTTGTCATGGAAGTCACAAATAAAACACGTGCAGATGTAAAG
GGCGGGACACTCACTCAATATGAAGGCAAACTGAGACTGGTGGAAATTGCTCAAGTGCCA
AAAGCACATGTTGACGAGTTCAAGTCTGTATCAAAGTTCAAAATATTTAATACAAACAAC
CTATGGATTTCTCTTGCAGCAGTTAAAAGACTGCAGGAGCAAAATGCCATTGACATGGAA
ATCATTGTGAATGCAAAGACTTTGGATGGAGGCCTGAATGTCATTCAATTAGAAACTGCA
GTAGGGGCTGCCATCAAAAGCTTTGAGAATTCTCTAGGTATTAATGTGCCAAGGAGCCGT
TTTCTGCCTGTCAAAACCACATCAGATCTCTTGCTGGTGATGTCAAACCTCTATAGTCTT
AATGCAGGATCTCTGACAATGAGTGAAAAGCGGGAATTTCCTACAGTGCCCTTGGTTAAA
TTAGGCAGTTCTTTTACGAAGGTTCAAGATTATCTAAGAAGATTTGAAAGTATACCAGAT
ATGCTTGAATTGGATCACCTCACAGTTTCAGGAGATGTGACATTTGGAAAAAATGTTTCA
TTAAAGGGAACGGTTATCATCATTGCAAATCATGGTGACAGAATTGATATCCCACCTGGA
GCAGTATTAGAGAACAAGATAGTGTCTGGAAACCTTCGCATCTTGGACCACTGA
Enzyme 6 GenBank Gene ID U27460 Link Image
Enzyme 6 GeneCard ID UGP2 Link Image
Enzyme 6 GenAtlas ID UGP2 Link Image
Enzyme 6 HGNC ID HGNC:12527 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2p14-p13
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Duggleby RG, Chao YC, Huang JG, Peng HL, Chang HY: Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli. Eur J Biochem. 1996 Jan 15;235(1-2):173-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6381
Enzyme 7 Name Galactose-1-phosphate uridylyltransferase
Enzyme 7 Synonyms
  1. Gal-1-P uridylyltransferase
  2. UDP-glucose--hexose-1-phosphate uridylyltransferase
Enzyme 7 Gene Name GALT
Enzyme 7 Protein Sequence >Galactose-1-phosphate uridylyltransferase
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQ
LLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAK
SARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC
SNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWL
VLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGW
HGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA
LPEVHYHLGQKDRETATIA
Enzyme 7 Number of Residues 379
Enzyme 7 Molecular Weight 43364
Enzyme 7 Theoretical pI 6.99
Enzyme 7 GO Classification
Function
  • UDP-glucose:hexose-1-phosphate uridylyltransferase activity
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose
Enzyme 7 Pathways
Enzyme 7 Reactions
  • UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDPgalactose
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 182951 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P07902 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GALT_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1140 bp
ATGTCGCGCAGTGGAACCGATCCTCAGCAACGCCAGCAGGCGTCAGAGGCGGACGCCGCA
GCAGCAACCTTCCGGGCAAACGACCATCAGCATATCCGCTACAACCCGCTGCAGGATGAG
TGGGTGCTGGTGTCAGCTCACCGCATGAAGCGGCCCTGGCAGGGTCAAGTGGAGCCCCAG
CTTCTGAAGACAGTGCCCCGCCATGACCCTCTCAACCCTCTGTGTCCTGGGGCCATCCGA
GCCAACGGAGAGGTGAATCCCCAGTACGATAGCACCTTCCTGTTTGACAACGACTTCCCA
GCTCTGCAGCCTGATGCCCCCAGTCCAGGACCCAGTGATCATCCCCTTTTCCAAGCAAAG
TCTGCTCGAGGAGTCTGTAAGGTCATGTGCTTCCACCCCTGGTCGGATGTAACGCTGCCA
CTCATGTCGGTCCCTGAGATCCGGGCTGTTGTTGATGCATGGGCCTCAGTCACAGAGGAG
CTGGGTGCCCAGTACCCTTGGGTGCAGATCTTTGAAAACAAAGGTGCCATGATGGGCTGT
TCTAACCCCCACCCCCACTGCCAGGTATGGGCCAGCAGTTTCCTGCCAGATATTGCCCAG
CGTGAGGAGCGATCTCAGCAGGCCTATAAGAGTCAGCATGGAGAGCCCCTGCTAATGGAG
TACAGCCGCCAGGAGCTACTCAGGAAGGAACGTCTGGTCCTAACCAGTGAGCACTGGTTA
GTACTGGTCCCCTTCTGGGCAACATGGCCCTACCAGACACTGCTGCTGCCCGTCGGCCAT
GTGCGGCGGCTACCTGAGCTGACCCCTGCTGAGCGTGATGATCTAGCCTCCATCATGAAG
AAGCTCTTGACCAAGTATGACAACCTCTTTGAGACGTCCTTTCCCTACTCCATGGGCTGG
CATGGGGCTCCCACAGGATCAGAGGCTGGGGCCAACTGGAACCATTGGCAGCTGCACGCT
CATTACTACCCTCCGCTCCTGCGCTCTGCCACTGTCCGGAAATTCATGGTTGGCTACGAA
ATGCTTGCTCAGGCTCAGAGGGACCTCACCCCTGAGCAGGCTGCAGAGAGACTAAGGGCA
CTTCCTGAGGTTCATTACCACCTGGGGCAGAAGGACAGGGAGACAGCAACCATCGCCTGA
Enzyme 7 GenBank Gene ID M60091 Link Image
Enzyme 7 GeneCard ID GALT Link Image
Enzyme 7 GenAtlas ID GALT Link Image
Enzyme 7 HGNC ID HGNC:4135 Link Image
Enzyme 7 Chromosome Location 9
Enzyme 7 Locus 9p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Reichardt JK, Berg P: Cloning and characterization of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol Biol Med. 1988 Apr;5(2):107-22. [PubMed Link Image]
  2. Flach JE, Reichardt JK, Elsas LJ 2nd: Sequence of a cDNA encoding human galactose-1-phosphate uridyl transferase. Mol Biol Med. 1990 Aug;7(4):365-9. [PubMed Link Image]
  3. Leslie ND, Immerman EB, Flach JE, Florez M, Fridovich-Keil JL, Elsas LJ: The human galactose-1-phosphate uridyltransferase gene. Genomics. 1992 Oct;14(2):474-80. [PubMed Link Image]
  4. Reichardt JK: Genetic basis of galactosemia. Hum Mutat. 1992;1(3):190-6. [PubMed Link Image]
  5. Tyfield L, Reichardt J, Fridovich-Keil J, Croke DT, Elsas LJ 2nd, Strobl W, Kozak L, Coskun T, Novelli G, Okano Y, Zekanowski C, Shin Y, Boleda MD: Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene. Hum Mutat. 1999;13(6):417-30. [PubMed Link Image]
  6. Reichardt JK, Packman S, Woo SL: Molecular characterization of two galactosemia mutations: correlation of mutations with highly conserved domains in galactose-1-phosphate uridyl transferase. Am J Hum Genet. 1991 Oct;49(4):860-7. [PubMed Link Image]
  7. Reichardt JK, Woo SL: Molecular basis of galactosemia: mutations and polymorphisms in the gene encoding human galactose-1-phosphate uridylyltransferase. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2633-7. [PubMed Link Image]
  8. Reichardt JK, Levy HL, Woo SL: Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase. Biochemistry. 1992 Jun 23;31(24):5430-3. [PubMed Link Image]
  9. Reichardt JK, Belmont JW, Levy HL, Woo SL: Characterization of two missense mutations in human galactose-1-phosphate uridyltransferase: different molecular mechanisms for galactosemia. Genomics. 1992 Mar;12(3):596-600. [PubMed Link Image]
  10. Reichardt JK, Novelli G, Dallapiccola B: Molecular characterization of the H319Q galactosemia mutation. Hum Mol Genet. 1993 Mar;2(3):325-6. [PubMed Link Image]
  11. Lin HC, Kirby LT, Ng WG, Reichardt JK: On the molecular nature of the Duarte variant of galactose-1-phosphate uridyl transferase (GALT). Hum Genet. 1994 Feb;93(2):167-9. [PubMed Link Image]
  12. Elsas LJ, Langley S, Steele E, Evinger J, Fridovich-Keil JL, Brown A, Singh R, Fernhoff P, Hjelm LN, Dembure PP: Galactosemia: a strategy to identify new biochemical phenotypes and molecular genotypes. Am J Hum Genet. 1995 Mar;56(3):630-9. [PubMed Link Image]
  13. Fridovich-Keil JL, Langley SD, Mazur LA, Lennon JC, Dembure PP, Elsas JL 2nd: Identification and functional analysis of three distinct mutations in the human galactose-1-phosphate uridyltransferase gene associated with galactosemia in a single family. Am J Hum Genet. 1995 Mar;56(3):640-6. [PubMed Link Image]
  14. Sommer M, Gathof BS, Podskarbi T, Giugliani R, Kleinlein B, Shin YS: Mutations in the galactose-1-phosphate uridyltransferase gene of two families with mild galactosaemia variants. J Inherit Metab Dis. 1995;18(5):567-76. [PubMed Link Image]
  15. Ashino J, Okano Y, Suyama I, Yamazaki T, Yoshino M, Furuyama J, Lin HC, Reichardt JK, Isshiki G: Molecular characterization of galactosemia (type 1) mutations in Japanese. Hum Mutat. 1995;6(1):36-43. [PubMed Link Image]
  16. Shin YS, Gathof BS, Podskarbi T, Sommer M, Giugliani R, Gresser U: Three missense mutations in the galactose-1-phosphate uridyltransferase gene of three families with mild galactosaemia. Eur J Pediatr. 1996 May;155(5):393-7. [PubMed Link Image]
  17. Maceratesi P, Sangiuolo F, Novelli G, Ninfali P, Magnani M, Reichardt JK, Dallapiccola B: Three new mutations (P183T, V150L, 528insG) and eleven sequence polymorphisms in Italian patients with galactose-1-phosphate uridyltransferase (GALT) deficiency. Hum Mutat. 1996;8(4):369-72. [PubMed Link Image]
  18. Ninfali P, Bresolin N, Dallapiccola B, Novelli G: Molecular basis of galactose-1-phosphate uridyltransferase deficiency involving skeletal muscle. J Neurol. 1996 Jan;243(1):102-3. [PubMed Link Image]
  19. Greber-Platzer S, Guldberg P, Scheibenreiter S, Item C, Schuller E, Patel N, Strobl W: Molecular heterogeneity of classical and Duarte galactosemia: mutation analysis by denaturing gradient gel electrophoresis. Hum Mutat. 1997;10(1):49-57. [PubMed Link Image]
  20. Seyrantepe V, Ozguc M, Coskun T, Ozalp I, Reichardt JK: Identification of mutations in the galactose-1-phosphate uridyltransferase (GALT) gene in 16 Turkish patients with galactosemia, including a novel mutation of F294Y. Mutation in brief no. 235. Online. Hum Mutat. 1999;13(4):339. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6386
Enzyme 8 Name Uridine diphosphate glucose pyrophosphatase
Enzyme 8 Synonyms
  1. UDPG pyrophosphatase
  2. UGPPase
  3. Nucleoside diphosphate-linked moiety X motif 14
  4. Nudix motif 14
Enzyme 8 Gene Name NUDT14
Enzyme 8 Protein Sequence >Uridine diphosphate glucose pyrophosphatase
MERIEGASVGRCAASPYLRPLTLHYRQNGAQKSWDFMKTHDSVTVLLFNSSRRSLVLVKQ
FRPAVYAGEVERRFPGSLAAVDQDGPRELQPALPGSAGVTVELCAGLVDQPGLSLEEVAC
KEAWEECGYHLAPSDLRRVATYWSGVGLTGSRQTMFYTEVTDAQRSGPGGGLVEEGELIE
VVHLPLEGAQAFADDPDIPKTLGVIFGVSWFLSQVAPNLDLQ
Enzyme 8 Number of Residues 222
Enzyme 8 Molecular Weight 24119
Enzyme 8 Theoretical pI 4.69
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
Process
Component
Enzyme 8 General Function Replication, recombination and repair
Enzyme 8 Specific Function Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP- mannose
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID O95848 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NUD14_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AF111170 Link Image
Enzyme 8 GeneCard ID NUDT14 Link Image
Enzyme 8 GenAtlas ID NUDT14 Link Image
Enzyme 8 HGNC ID HGNC:20141 Link Image
Enzyme 8 Chromosome Location 14
Enzyme 8 Locus 14q32.33
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Deng Y, Madan A, Banta AB, Friedman C, Trask BJ, Hood L, Li L: Characterization, chromosomal localization, and the complete 30-kb DNA sequence of the human Jagged2 (JAG2) gene. Genomics. 2000 Jan 1;63(1):133-8. [PubMed Link Image]
  2. Yagi T, Baroja-Fernandez E, Yamamoto R, Munoz FJ, Akazawa T, Hong KS, Pozueta-Romero J: Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Biochem J. 2003 Mar 1;370(Pt 2):409-15. [PubMed Link Image]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6399
Enzyme 9 Name Phosphoglucomutase-1
Enzyme 9 Synonyms
  1. Glucose phosphomutase 1
  2. PGM 1
Enzyme 9 Gene Name PGM1
Enzyme 9 Protein Sequence >Phosphoglucomutase-1
MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVG
GDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNP
GGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENK
FKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEE
LGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKH
GFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWK
FFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKY
GRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPV
DGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLI
SIALKVSQLQERTGRTAPTVIT
Enzyme 9 Number of Residues 562
Enzyme 9 Molecular Weight 61450
Enzyme 9 Theoretical pI 6.72
Enzyme 9 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 9 General Function Carbohydrate transport and metabolism
Enzyme 9 Specific Function This enzyme participates in both the breakdown and synthesis of glucose
Enzyme 9 Pathways
Enzyme 9 Reactions
  • alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 189926 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P36871 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PGM1_HUMAN Link Image
Enzyme 9 PDB ID 1C47 Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID M83088 Link Image
Enzyme 9 GeneCard ID PGM1 Link Image
Enzyme 9 GenAtlas ID PGM1 Link Image
Enzyme 9 HGNC ID HGNC:8905 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p31
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 9329
Enzyme 10 Name Phosphoglucomutase-2
Enzyme 10 Synonyms
  1. Glucose phosphomutase 2
  2. PGM 2
Enzyme 10 Gene Name PGM2
Enzyme 10 Protein Sequence >Phosphoglucomutase-2
MAAPEGSGLGEDARLDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTA
GLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHPSSGGSSRRF
ARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDN
GAQIISPHDKGISQAIEENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCFHR
SVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGK
GVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWK
EKNQDRSALKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVL
FAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKAS
YFICHDQETIKKLFENLRNYDGKNNYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSK
SSQMITFTFANGGVATMRTSGTEPKIKYYAELCAPPGNSDPEQLKKELNELVSAIEEHFF
QPQKYNLQPKAD
Enzyme 10 Number of Residues 612
Enzyme 10 Molecular Weight 68284
Enzyme 10 Theoretical pI Not Available
Enzyme 10 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function This enzyme participates in both the breakdown and synthesis of glucose
Enzyme 10 Pathways
Enzyme 10 Reactions
  • D-Glucose 1-phosphate <==> D-Glucose 6-phosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 12052930 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q96G03 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PGM2_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 AL136705 Link Image
Enzyme 10 GeneCard ID Not Available
Enzyme 10 GenAtlas ID PGM2 Link Image
Enzyme 10 HGNC ID HGNC:8906 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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]
  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]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 13108
Enzyme 11 Name cDNA FLJ77760, highly similar to Homo sapiens glucosidase, beta; acid
Enzyme 11 Synonyms
  1. includes glucosylceramidase, mRNA
Enzyme 11 Gene Name Not Available
Enzyme 11 Protein Sequence >cDNA FLJ77760, highly similar to Homo sapiens glucosidase, beta; acid
MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNAT
YCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGF
GGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDD
FQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQP
GDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIA
RDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAK
ATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDW
NLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQK
NDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
Enzyme 11 Number of Residues 536
Enzyme 11 Molecular Weight 59717
Enzyme 11 Theoretical pI 7.66
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
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 158257254 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID A8K796 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name A8K796_HUMAN Link Image
Enzyme 11 PDB ID 1Y7V Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK291911 Link Image
Enzyme 11 GeneCard ID A8K796 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 Not Available
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 14947
Enzyme 12 Name Glucose 1,6-bisphosphate synthase
Enzyme 12 Synonyms
  1. Phosphoglucomutase-2-like 1
  2. PMMLP
Enzyme 12 Gene Name PGM2L1
Enzyme 12 Protein Sequence >Glucose 1,6-bisphosphate synthase
MAENTEGDLNSNLLHAPYHTGDPQLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDR
LCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGQ
VTSSCSSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKE
DNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLVDTSPLKRDPLQDICRRYM
EDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFST
VKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAAL
FGWWMFDCWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRII
DLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYE
KYGYHISKTSYFLCYEPPTIKSIFERLRNFDSPKEYPKFCGTFAILHVRDITTGYDSSQP
NKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDQSDTALLEEELKK
LIDALIENFLQPSKNGLIWRSV
Enzyme 12 Number of Residues 622
Enzyme 12 Molecular Weight 70456
Enzyme 12 Theoretical pI 7.17
Enzyme 12 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities
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 5688958 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q6PCE3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PGM2L_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1869 bp
ATGGCTGAAAACACAGAGGGGGATCTGAACTCCAACCTGCTCCACGCCCCCTACCACACC
GGGGACCCTCAGCTGGACACGGCCATCGGGCAGTGGCTCCGCTGGGATAAGAATCCCAAA
ACAAAAGAGCAGATTGAAAACCTGTTACGGAATGGGATGAACAAGGAGCTGCGAGATCGT
CTTTGTTGCCGAATGACTTTTGGGACTGCAGGACTTCGTTCTGCCATGGGGGCAGGGTTT
TGCTATATTAATGACCTTACAGTAATACAGTCAACACAGGGGATGTACAAATACCTTGAG
AGATGTTTCTCAGACTTCAAGCAGAGAGGCTTTGTGGTTGGGTATGACACTCGGGGTCAA
GTAACTAGCAGCTGCAGCAGCCAGAGGCTTGCTAAACTCACTGCTGCAGTCTTGCTGGCC
AAAGATGTTCCTGTGTACCTTTTTTCAAGATATGTTCCTACACCTTTTGTACCATATGCA
GTTCAGAAGCTCAAAGCAGTTGCAGGTGTGATGATTACTGCCTCTCACAACCGCAAGGAA
GACAATGGATACAAGGTTTACTGGGAAACTGGTGCTCAGATCACATCTCCTCATGATAAA
GAAATTCTAAAATGTATAGAAGAATGTGTGGAACCCTGGAATGGTTCCTGGAATGATAAT
TTAGTGGATACCAGCCCGCTGAAGAGAGACCCTCTGCAGGACATTTGCAGGAGATACATG
GAAGATCTGAAAAAGATCTGTTTTTACAGGGAGTTAAACTCGAAGACCACCTTGAAATTT
GTGCACACATCTTTTCATGGGGTCGGACATGACTATGTGCAGTTGGCTTTTAAAGTGTTT
GGTTTTAAGCCTCCAATTCCAGTACCAGAACAAAAAGATCCTGATCCAGACTTTTCTACC
GTTAAATGTCCAAATCCTGAAGAAGGAGAATCTGTGCTGGAACTTTCCTTGAGACTGGCA
GAGAAAGAAAATGCCCGGGTAGTGCTAGCCACAGATCCTGATGCAGACAGACTGGCAGCA
GCAGAACTTCAGGAGAATGGTTGTTGGAAAGTTTTCACAGGGAATGAGTTGGCAGCTTTG
TTTGGATGGTGGATGTTTGATTGCTGGAAGAAAAATAAATCAAGAAATGCTGATGTGAAG
AACGTTTATATGTTAGCCACCACAGTCTCTTCTAAAATTCTGAAGGCAATTGCACTTAAA
GAAGGATTTCATTTTGAAGAAACATTACCAGGTTTTAAATGGATTGGAAGTAGGATAATA
GACCTCCTGGAAAATGGGAAAGAAGTCCTTTTTGCATTTGAAGAGTCTATTGGTTTTCTC
TGTGGAACTTCAGTTTTGGATAAAGATGGGGTGAGTGCAGCTGTTGTGGTTGCTGAGATG
GCATCTTACCTGGAAACCATGAATATAACATTGAAACAGCAACTGGTTAAGGTTTATGAA
AAATATGGTTATCATATTTCAAAAACTTCCTATTTCTTGTGTTATGAACCACCTACCATC
AAAAGTATATTTGAAAGGCTTCGTAATTTTGATTCTCCAAAAGAATATCCAAAATTTTGT
GGAACATTTGCTATATTGCATGTACGGGACGTTACCACTGGATATGACAGTAGCCAGCCT
AATAAGAAATCAGTGCTGCCTGTGAGTAAAAACAGCCAAATGATTACATTTACTTTTCAA
AATGGCTGTGTTGCTACCCTTCGGACAAGTGGAACAGAACCAAAGATAAAGTATTATGCA
GAGATGTGTGCGTCACCTGACCAGAGTGACACTGCTTTACTGGAGGAAGAACTGAAGAAA
CTCATTGATGCTCTGATAGAGAATTTTCTTCAGCCTAGTAAGAATGGACTGATCTGGCGT
TCTGTTTAG
Enzyme 12 GenBank Gene ID AB019210 Link Image
Enzyme 12 GeneCard ID Q6PCE3 Link Image
Enzyme 12 GenAtlas ID PGM2L1 Link Image
Enzyme 12 HGNC ID HGNC:20898 Link Image
Enzyme 12 Chromosome Location 11
Enzyme 12 Locus 11q13.4
Enzyme 12 SNPs SNPJam Report Link Image
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 16941
Enzyme 14 Name Galactose-1-phosphate uridylyltransferase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name GALT
Enzyme 14 Protein Sequence >Galactose-1-phosphate uridylyltransferase
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQ
LLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAK
SARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGC
SNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWL
VLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGW
HGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRA
LPEVHYHLGQKDRETATIA
Enzyme 14 Number of Residues 379
Enzyme 14 Molecular Weight 43364
Enzyme 14 Theoretical pI 6.99
Enzyme 14 GO Classification
Function
  • UDP-glucose:hexose-1-phosphate uridylyltransferase activity
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • galactose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 14 General Function Energy production and conversion
Enzyme 14 Specific Function UDP-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-galactose
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
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 Q5VZ81 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q5VZ81_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 AL162231 Link Image
Enzyme 14 GeneCard ID Q5VZ81 Link Image
Enzyme 14 GenAtlas ID GALT Link Image
Enzyme 14 HGNC ID HGNC:4135 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