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Human Metabolome Database Version 2.5

 

Showing metabocard for 3-Phosphoglyceric acid (HMDB00807)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-01 10:58:18
Accession Number HMDB00807
Secondary Accession Numbers Not Available
Common Name 3-Phosphoglyceric acid
Description 3-phosphoglyceric acid (3PG) is a 3-carbon molecule that is a metabolic intermediate in both glycolysis and the Calvin cycle. This chemical is often termed PGA when referring to the Calvin cycle. In the Calvin cycle, two glycerate 3-phosphate molecules are reduced to form two molecules of glyceraldehyde 3-phosphate (GALP). (wikipedia)
Synonyms
  1. 3-(dihydrogen phosphate)Glycerate
  2. 3-(dihydrogen phosphate)Glyceric acid
  3. 3-Glycerophosphorate
  4. 3-Glycerophosphoric acid
  5. 3-P-D-glycerate
  6. 3-P-glycerate
  7. 3-PGA
  8. 3-Phosphoglycerate
  9. 3-Phosphoglyceric acid
  10. 3-pg
  11. 3-phospho-(R)-glycerate
  12. 3-phospho-D-glycerate
  13. 3-phospho-glycerate
  14. 3-phospho-glyceric acid
  15. D-Glycerate 3-phosphate
  16. G3P
  17. Glycerate 3-phosphate
  18. Glyceric acid 3-phosphate
  19. Phosphoglycerate
  20. glycerate-3-P
  21. D-(-)-3-Phosphoglyceric acid
Chemical IUPAC Name 2-hydroxy-3-phosphonooxy-propanoic acid
Chemical Formula C3H7O7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Glycerophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • phosphoric acid ester
  • alpha-hydroxyacid
Biofunction
  • Component of Glycine, serine and threonine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 186.057
Monoisotopic Molecular Weight 185.992935
Isomeric SMILES OC(COP(O)(O)=O)C(O)=O
Canonical SMILES OC(COP(O)(O)=O)C(O)=O
KEGG Compound ID C00597 Link Image
BioCyc ID G3P Link Image
BiGG ID 34230 Link Image
Wikipedia Link 3-Phosphoglycerate Link Image
NuGOwiki Link HMDB00807 Link Image
Metagene Link HMDB00807 Link Image
METLIN ID 150 Link Image
PubChem Compound 724 Link Image
PubChem Substance 8144701 Link Image
ChEBI ID 17050 Link Image
CAS Registry Number 820-11-1
InChI Identifier InChI=1/C3H7O7P/c4-2(3(5)6)1-10-11(7,8)9/h2,4H,1H2,(H,5,6)(H2,7,8,9)
Synthesis Reference Jakoby, Wm. B.; Brummond, Dewey O.; Ochoa, Severo. Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach-leaf enzymes. Journal of Biological Chemistry (1956), 218 811-22.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 21.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.26 [Predicted by ALOGPS]; -3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 13PK Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location
  • Blood
  • Cellular Cytoplasm
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 58.2 +/- 14.4 uM
Age Newborn:0-30 days 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 Blood
Value 47.2 +/- 7.4 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 45 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
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
General References
  1. Yu KT, Pendley C 2nd, Herczeg T, Pendleton RG: 2,3-Diphosphoglycerate phosphatase/synthase: a potential target for elevating the diphosphoglycerate level in human red blood cells. J Pharmacol Exp Ther. 1990 Jan;252(1):192-200. [PubMed Link Image]
  2. Uchida K, Kondoh K, Matuo Y: Recombinant M-, B- and MB-type isozymes of human phosphoglyceric acid mutase: their large-scale production and preparation of polyclonal antibodies specific to M- and B-type isozymes. Clin Chim Acta. 1995 Jun 15;237(1-2):43-58. [PubMed Link Image]
  3. Uchida K, Mori K, Matuo Y: [Phosphoglyceric acid mutase] Nippon Rinsho. 1995 May;53(5):1247-52. [PubMed Link Image]
  4. Nakai A, Shigematsu Y, Liu YY, Kikawa Y, Sudo M: Urinary sugar phosphates and related organic acids in fructose-1,6-diphosphatase deficiency. J Inherit Metab Dis. 1993;16(2):408-14. [PubMed Link Image]
  5. Sayed A, Matsuyama S, Inoue K, Alsina J, Cai F, Chen J, Inouye M: ATPase and GTPase activities copurifying with GTP-binding proteins in E. coli. J Mol Microbiol Biotechnol. 2000 Jul;2(3):261-3. [PubMed Link Image]
  6. Grisolia S, Salinas M, Wallace R, Singh GK: Influence of size, protein concentration, protein synthesis inhibitors,and carbon on clearance of enzymes and proteins from blood. Physiol Chem Phys. 1976;8(1):37-52. [PubMed Link Image]
  7. Mair J: Progress in myocardial damage detection: new biochemical markers for clinicians. Crit Rev Clin Lab Sci. 1997;34(1):1-66. [PubMed Link Image]
  8. 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]
  9. Glaus M, Schneider W: Iron release from transferrin induced by mixed ligand complexes of copper(II). Biol Met. 1989;2(3):185-90. [PubMed Link Image]
  10. Mayo Medical Laboratories 2005 Test Catalog
  11. Veech RL, Lawson JW, Cornell NW, Krebs HA: Cytosolic phosphorylation potential. J Biol Chem. 1979 Jul 25;254(14):6538-47. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Bisphosphoglycerate mutase
  2. Phosphoglycerate mutase 1
  3. Acylphosphatase-1
  4. D-3-phosphoglycerate dehydrogenase
  5. Phosphoglycerate kinase 1
  6. Glycerate kinase
Enzyme 1 [top]
Enzyme 1 ID 5498
Enzyme 1 Name Bisphosphoglycerate mutase
Enzyme 1 Synonyms
  1. 2,3-bisphosphoglycerate mutase, erythrocyte
  2. 2,3-bisphosphoglycerate synthase
  3. BPGM
  4. BPG-dependent PGAM
Enzyme 1 Gene Name BPGM
Enzyme 1 Protein Sequence >Bisphosphoglycerate mutase
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK
Enzyme 1 Number of Residues 259
Enzyme 1 Molecular Weight 30006
Enzyme 1 Theoretical pI 6.52
Enzyme 1 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 Specific Function Plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. Can also catalyze the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 29481 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P07738 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PMGE_HUMAN Link Image
Enzyme 1 PDB ID 1T8P Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >780 bp
ATGTCCAAGTACAAACTTATTATGTTAAGACATGGAGAGGGTGCTTGGAATAAGGAGAAC
CGTTTTTGTAGCTGGGTGGATCAGAAACTCAACAGCGAAGGAATGGAGGAAGCTCGGAAC
TGTGGGAAGCAACTCAAAGCGTTAAACTTTGAGTTTGATCTTGTATTCACATCTGTCCTT
AATCGGTCCATTCACACAGCCTGGCTGATCCTGGAAGAGCTAGGCCAGGAATGGGTGCCT
GTGGAAAGCTCCTGGCGTCTAAATGAGCGTCACTATGGGGCCTTGATCGGTCTCAACAGG
GAGCAGATGGCTTTGAATCATGGTGAAGAACAAGTGAGGCTCTGGAGAAGAAGCTACAAT
GTAACCCCGCCTCCCATTGAGGAGTCTCATCCTTACTACCAAGAAATCTACAACGACCGG
AGGTATAAAGTATGCGATGTGCCCTTGGATCAACTGCCACGGTCGGAAAGCTTAAAGGAT
GTTCTGGAGAGACTCCTTCCCTATTGGAATGAAAGGATTGCTCCCGAAGTATTACGTGGC
AAAACCATTCTGATATCTGCTCATGGAAATAGCAGTAGGGCACTCCTAAAACACCTGGAA
GGTATCTCAGATGAAGACATCATCAACATTACTCTTCCTACTGGAGTCCCCATTCTTCTG
GAATTGGATGAAAACCTGCGTGCTGTTGGGCCTCATCAGTTCCTGGGTGACCAAGAGGCG
ATCCAAGCAGCCATTAAGAAAGTAGAAGATCAAGGAAAAGTGAAACAAGCTAAAAAATAG
Enzyme 1 GenBank Gene ID X04327 Link Image
Enzyme 1 GeneCard ID BPGM Link Image
Enzyme 1 GenAtlas ID BPGM Link Image
Enzyme 1 HGNC ID HGNC:1093 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q31-q34
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Joulin V, Peduzzi J, Romeo PH, Rosa R, Valentin C, Dubart A, Lapeyre B, Blouquit Y, Garel MC, Goossens M, et al.: Molecular cloning and sequencing of the human erythrocyte 2,3-bisphosphoglycerate mutase cDNA: revised amino acid sequence. EMBO J. 1986 Sep;5(9):2275-83. [PubMed Link Image]
  2. Cohen-Solal M, Joulin V, Romeo PH, Rosa R, Valentin C, Garel MC, Rosa J: Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and revised amino acid sequence. Biomed Biochim Acta. 1987;46(2-3):S126-30. [PubMed Link Image]
  3. Joulin V, Garel MC, Le Boulch P, Valentin C, Rosa R, Rosa J, Cohen-Solal M: Isolation and characterization of the human 2,3-bisphosphoglycerate mutase gene. J Biol Chem. 1988 Oct 25;263(30):15785-90. [PubMed Link Image]
  4. Stafforini DM, Rollins EN, Prescott SM, McIntyre TM: The platelet-activating factor acetylhydrolase from human erythrocytes. Purification and properties. J Biol Chem. 1993 Feb 25;268(6):3857-65. [PubMed Link Image]
  5. Craescu CT, Schaad O, Garel MC, Rosa R, Edelstein S: Structural modeling of the human erythrocyte bisphosphoglycerate mutase. Biochimie. 1992 Jun;74(6):519-26. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5501
Enzyme 2 Name Phosphoglycerate mutase 1
Enzyme 2 Synonyms
  1. Phosphoglycerate mutase isozyme B
  2. PGAM-B
  3. BPG-dependent PGAM 1
Enzyme 2 Gene Name PGAM1
Enzyme 2 Protein Sequence >Phosphoglycerate mutase 1
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQ
KRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYD
VPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKR
VLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVR
KAMEAVAAQGKAKK
Enzyme 2 Number of Residues 254
Enzyme 2 Molecular Weight 28804
Enzyme 2 Theoretical pI 7.22
Enzyme 2 GO Classification
Function
  • catalytic activity
  • intramolecular transferase activity
  • intramolecular transferase activity, phosphotransferases
  • isomerase activity
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 Specific Function Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 551174 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P18669 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PGAM1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >765 bp
ATGGCCGCCTACAAACTGGTGCTGATCCGGCACGGCGAGAGCGCATGGAACCTGGAGAAC
CGCTTCAGCGGCTGGTACGACGCCGACCTGAGCCCGGCGGGCCACGAGGAGGCGAAGCGC
GGCGGGCAGGCGCTACGAGATGCTGGCTATGAGTTTGACATCTGCTTCACCTCAGTGCAG
AAGAGAGCGATCCGGACCCTCTGGACAGTGCTAGATGCCATTGATCAGATGTGGCTGCCA
GTGGTGAGGACTTGGCGCCTCAATGAGCGGCACTATGGGGGTCTAACCGGTCTCAATAAA
GCAGAAACTGCTGCAAAGCATGGTGAGGCCCAGGTGAAGATCTGGAGGCGCTCCTATGAT
GTCCCACCACCTCCGATGGAGCCCGACCATCCTTTCTACAGCAACATCAGTAAGGATCGC
AGGTATGCAGACCTCACAGAAGATCAGCTACCCTCCTGTGAGAGTCTGAAGGATACTATT
GCCAGAGCTCTGCCCTTCTGGAATGAAGAAATAGTTCCCCAGATCAAGGAGGGGAAACGT
GTACTGATTGCAGCCCATGGCAACAGCCTCCGGGGCATTGTCAAGCATCTGGAGGGTCTC
TCTGAAGAGGCTATCATGGAGCTGAACCTGCCGACTGGTATTCCCATTGTCTATGAATTG
GACAAGAACTTGAAGCCTATCAAGCCCATGCAGTTTCTGGGGGATGAAGAGACGGTGCGC
AAAGCCATGGAAGCTGTGGCTGCCCAGGGCAAGGCCAAGAAGTGA
Enzyme 2 GenBank Gene ID J04173 Link Image
Enzyme 2 GeneCard ID PGAM1 Link Image
Enzyme 2 GenAtlas ID PGAM1 Link Image
Enzyme 2 HGNC ID HGNC:8888 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Sakoda S, Shanske S, DiMauro S, Schon EA: Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family. J Biol Chem. 1988 Nov 15;263(32):16899-905. [PubMed Link Image]
  2. Blouquit Y, Calvin MC, Rosa R, Prome D, Prome JC, Pratbernou F, Cohen-Solal M, Rosa J: Sequence of the human erythrocyte phosphoglycerate mutase by microsequencer and mass spectrometry. J Biol Chem. 1988 Nov 15;263(32):16906-10. [PubMed Link Image]
  3. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5825
Enzyme 3 Name Acylphosphatase-1
Enzyme 3 Synonyms
  1. Acylphosphate phosphohydrolase 1
  2. Acylphosphatase, organ-common type isozyme
  3. Acylphosphatase, erythrocyte isozyme
Enzyme 3 Gene Name ACYP1
Enzyme 3 Protein Sequence >Acylphosphatase-1
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
Enzyme 3 Number of Residues 99
Enzyme 3 Molecular Weight 11261
Enzyme 3 Theoretical pI 9.94
Enzyme 3 GO Classification
Function
  • acylphosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Process
Component
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function Its physiological role is not yet clear
Enzyme 3 Pathways
Enzyme 3 Reactions
  • An acylphosphate + H2O = a carboxylate + 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 1834464 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P07311 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ACYP1_HUMAN Link Image
Enzyme 3 PDB ID 2ACY Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >300 bp
ATGGCAGAGGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCAATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA
Enzyme 3 GenBank Gene ID X84194 Link Image
Enzyme 3 GeneCard ID ACYP1 Link Image
Enzyme 3 GenAtlas ID ACYP1 Link Image
Enzyme 3 HGNC ID HGNC:179 Link Image
Enzyme 3 Chromosome Location 14
Enzyme 3 Locus 14q24.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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]
  2. Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed Link Image]
  3. Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6210
Enzyme 4 Name D-3-phosphoglycerate dehydrogenase
Enzyme 4 Synonyms
  1. 3-PGDH
Enzyme 4 Gene Name PHGDH
Enzyme 4 Protein Sequence >D-3-phosphoglycerate dehydrogenase
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVT
ADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQ
IPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISP
EVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIV
DEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIA
VQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQG
TSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGE
CLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPT
MIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
Enzyme 4 Number of Residues 533
Enzyme 4 Molecular Weight 56651
Enzyme 4 Theoretical pI 6.70
Enzyme 4 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphoglycerate dehydrogenase activity
Process
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function 3-phospho-D-glycerate + NAD(+) = 3- phosphonooxypyruvate + NADH
Enzyme 4 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 4 Reactions
  • 3-phosphoglycerate + NAD+ = 3-phosphohydroxypyruvate + NADH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2674062 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O43175 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SERA_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1602 bp
ATGGCTTTTGCAAATCTGCGGAAAGTGCTCATCAGTGACAGCCTGGACCCTTGCTGCCGG
AAGATCTTGCAAGAGGGAGGGCTGCAGGTGGTGGAAAAGCAGAACCTTAGCAAAGAGGAG
CTGATAGCGGAGCTGCAGGACTGTGAAGGCCTTATTGTTCGCTCTGCCACCAAGGTGACC
GCTGATGTCATCAACGCAGCTGAGAAACTCCAGGTGGTGGGCAGGGCTGGCACAGGTGTG
GACAATGTGGATCTGGAGGCCGCAACAAGGAAGGGCATCTTGGTTATGAACACCCCCAAT
GGGAACAGCCTCAGTGCCGCAGAACTCACTTGTGGAATGATCATGTGCCTGGCCAGGCAG
ATTCCCCAGGCGACGGCTTCGATGAAGGACGGCAAATGGGAGCGGAAGAAGTTCATGGGA
ACAGAGCTGAATGGAAAGACCCTGGGAATTCTTGGCCTGGGCAGGATTGGGAGAGAGGTA
GCTACCCGGATGCAGTCCTTTGGGATGAAGACTATAGGGTATGACCCCATCATTTCCCCA
GAGGTCTCGGCCTCCTTTGGTGTTCAGCAGCTGCCCCTGGAGGAGATCTGGCCTCTCTGT
GATTTCATCACTGTGCACACTCCTCTCCTGCCCTCCACGACAGGCTTGCTGAATGACAAC
ACCTTTGCCCAGTGCAAGAAGGGGGTGCGTGTGGTGAACTGTGCCCGTGGAGGGATCGTG
GACGAAGGCGCCCTGCTCCGGGCCCTGCAGTCTGGCCAGTGTGCCGGGGCTGCACTGGAC
GTGTTTACGGAAGAGCCGCCACGGGACCGGGCCTTGGTGGACCATGAGAATGTCATCAGC
TGTCCCCACCTGGGTGCCAGCACCAAGGAGGCTCAGAGCCGCTGTGGGGAGGAAATTGCT
GTTCAGTTCGTGGACATGGTGAAGGGGAAATCTCTCACGGGGGTTGTGAATGCCCAGGCC
CTTACCAGTGCCTTCTCTCCACACACCAAGCCTTGGATTGGTCTGGCAGAAGCTCTGGGG
ACACTGATGCGAGCCTGGGCTGGGTCCCCCAAAGGGACCATCCAGGTGATAACACAGGGA
ACATCCCTGAAGAATGCTGGGAACTGCCTAAGCCCCGCAGTCATTGTCGGCCTCCTGAAA
GAGGCTTCCAAGCAGGCGGATGTGAACTTGGTGAACGCTAAGCTGCTGGTGAAAGAGGCT
GGCCTCAATGTCACCACCTCCCACAGCCCTGCTGCACCAGGGGAGCAAGGCTTCGGGGAA
TGCCTCCTGGCCGTGGCCCTGGCAGGCGCCCCTTACCAGGCTGTGGGCTTGGTCCAAGGC
ACTACACCTGTACTGCAGGGGCTCAATGGAGCTGTCTTCAGGCCAGAAGTGCCTCTCCGC
AGGGACCTGCCCCTGCTCCTATTCCGGACTCAGACCTCTGACCCTGCAATGCTGCCTACC
ATGATTGGCCTCCTGGCAGAGGCAGGCGTGCGGCTGCTGTCCTACCAGACTTCACTGGTG
TCAGATGGGGAGACCTGGCACGTCATGGGCATCTCCTCCTTGCTGCCCAGCCTGGAAGCG
TGGAAGCAGCATGTGACTGAAGCCTTCCAGTTCCACTTCTAA
Enzyme 4 GenBank Gene ID AF006043 Link Image
Enzyme 4 GeneCard ID PHGDH Link Image
Enzyme 4 GenAtlas ID PHGDH Link Image
Enzyme 4 HGNC ID HGNC:8923 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1p12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Cho HM, Jun DY, Bae MA, Ahn JD, Kim YH: Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene. Gene. 2000 Mar 7;245(1):193-201. [PubMed Link Image]
  2. Klomp LW, de Koning TJ, Malingre HE, van Beurden EA, Brink M, Opdam FL, Duran M, Jaeken J, Pineda M, Van Maldergem L, Poll-The BT, van den Berg IE, Berger R: Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency--a neurometabolic disorder associated with reduced L-serine biosynthesis. Am J Hum Genet. 2000 Dec;67(6):1389-99. Epub 2000 Oct 27. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6824
Enzyme 5 Name Phosphoglycerate kinase 1
Enzyme 5 Synonyms
  1. Primer recognition protein 2
  2. PRP 2
  3. Cell migration-inducing gene 10 protein
Enzyme 5 Gene Name PGK1
Enzyme 5 Protein Sequence >Phosphoglycerate kinase 1
MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVL
MSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLE
NLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVN
LPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGM
AFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQ
ATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVV
KATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI
Enzyme 5 Number of Residues 417
Enzyme 5 Molecular Weight 44615
Enzyme 5 Theoretical pI 8.27
Enzyme 5 GO Classification
Function
  • catalytic activity
  • kinase activity
  • phosphoglycerate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 Specific Function In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl 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 35435 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P00558 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PGK1_HUMAN Link Image
Enzyme 5 PDB ID 1VJD Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1254 bp
ATGTCGCTTTCTAACAAGCTGACGCTGGACAAGCTGGACGTTAAAGGGAAGCGGGTCGTT
ATGAGAGTCGACTTCAATGTTCCTATGAAGAACAACCAGATAACAAACAACCAGAGGATT
AAGGCTGCTGTCCCAAGCATCAAATTCTGCTTGGACAATGGAGCCAAGTCGGTAGTCCTT
ATGAGCCACCTAGGCCGGCCTGATGGTGTGCCCATGCCTGACAAGTACTCCTTAGAGCCA
GTTGCTGTAGAACTCAAATCTCTGCTGGGCAAGGATGTTCTGTTCTTGAAGGACTGTGTA
GGCCCAGAAGTGGAGAAAGCCTGTGCCAACCCAGCTGCTGGGTCTGTCATCCTGCTGGAG
AACCTCCGCTTTCATGTGGAGGAAGAAGGGAAGGGAAAAGATGCTTCTGGGAACAAGGTT
AAAGCCGAGCCAGCCAAAATAGAAGCTTTCCGAGCTTCACTTTCCAAGCTAGGGGATGTC
TATGTCAATGATGCTTTTGGCACTGCTCACAGAGCCCACAGCTCCATGGTAGGAGTCAAT
CTGCCACAGAAGGCTGGTGGGTTTTTGATGAAGAAGGAGCTGAACTACTTTGCAAAGGCC
TTGGAGAGCCCAGAGCGACCCTTCCTGGCCATCCTGGGCGGAGCTAAAGTTGCAGACAAG
ATCCAGCTCATCAATAATATGCTGGACAAAGTCAATGAGATGATTATTGGTGGTGGAATG
GCTTTTACCTTCCTTAAGGTGCTCAACAACATGGAGATTGGCACTTCTCTGTTTGATGAA
GAGGGAGCCAAGATTGTCAAAGACCTAATGTCCAAAGCTGAGAAGAATGGTGTGAAGATT
ACCTTGCCTGTTGACTTTGTCACTGCTGACAAGTTTGATGAGAATGCCAAGACTGGCCAA
GCCACTGTGGCTTCTGGCATACCTGCTGGCTGGATGGGCTTGGACTGTGGTCCTGAAAGC
AGCAAGAAGTATGCTGAGGCTGTCACTCGGGCTAAGCAGATTGTGTGGAATGGTCCTGTG
GGGGTATTTGAATGGGAAGCTTTTGCCCGGGGAACCAAAGCTCTCATGGATGAGGTGGTG
AAAGCCACTTCTAGGGGCTGCATCACCATCATAGGTGGTGGAGACACTGCCACTTGCTGT
GCCAAATGGAACACGGAGGATAAAGTCAGCCATGTGAGCACTGGGGGTGGTGCCAGTTTG
GAGCTCCTGGAAGGTAAAGTCCTTCCTGGGGTGGATGCTCTCAGCAATATTTAG
Enzyme 5 GenBank Gene ID V00572 Link Image
Enzyme 5 GeneCard ID PGK1 Link Image
Enzyme 5 GenAtlas ID PGK1 Link Image
Enzyme 5 HGNC ID HGNC:8896 Link Image
Enzyme 5 Chromosome Location X
Enzyme 5 Locus Xq13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Michelson AM, Markham AF, Orkin SH: Isolation and DNA sequence of a full-length cDNA clone for human X chromosome-encoded phosphoglycerate kinase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):472-6. [PubMed Link Image]
  2. Michelson AM, Blake CC, Evans ST, Orkin SH: Structure of the human phosphoglycerate kinase gene and the intron-mediated evolution and dispersal of the nucleotide-binding domain. Proc Natl Acad Sci U S A. 1985 Oct;82(20):6965-9. [PubMed Link Image]
  3. Singer-Sam J, Keith DH, Tani K, Simmer RL, Shively L, Lindsay S, Yoshida A, Riggs AD: Sequence of the promoter region of the gene for human X-linked 3-phosphoglycerate kinase] Gene. 1984 Dec;32(3):409-17. [PubMed Link Image]
  4. Pfeifer GP, Steigerwald SD, Mueller PR, Wold B, Riggs AD: Genomic sequencing and methylation analysis by ligation mediated PCR. Science. 1989 Nov 10;246(4931):810-3. [PubMed Link Image]
  5. Huang IY, Welch CD, Yoshida A: Complete amino acid sequence of human phosphoglycerate kinase. Cyanogen bromide peptides and complete amino acid sequence. J Biol Chem. 1980 Jul 10;255(13):6412-20. [PubMed Link Image]
  6. Jindal HK, Vishwanatha JK: Functional identity of a primer recognition protein as phosphoglycerate kinase. J Biol Chem. 1990 Apr 25;265(12):6540-3. [PubMed Link Image]
  7. Yoshida A: Hematologically important mutations: molecular abnormalities of phosphoglycerate kinase. Blood Cells Mol Dis. 1996;22(3):265-7. [PubMed Link Image]
  8. Yoshida A, Twele TW, Dave V, Beutler E: Molecular abnormality of a phosphoglycerate kinase variant (PGK-Alabama). Blood Cells Mol Dis. 1995;21(3):179-81. [PubMed Link Image]
  9. Cohen-Solal M, Valentin C, Plassa F, Guillemin G, Danze F, Jaisson F, Rosa R: Identification of new mutations in two phosphoglycerate kinase (PGK) variants expressing different clinical syndromes: PGK Creteil and PGK Amiens. Blood. 1994 Aug 1;84(3):898-903. [PubMed Link Image]
  10. Ookawara T, Dave V, Willems P, Martin JJ, de Barsy T, Matthys E, Yoshida A: Retarded and aberrant splicings caused by single exon mutation in a phosphoglycerate kinase variant. Arch Biochem Biophys. 1996 Mar 1;327(1):35-40. [PubMed Link Image]
  11. Valentin C, Birgens H, Craescu CT, Brodum-Nielsen K, Cohen-Solal M: A phosphoglycerate kinase mutant (PGK Herlev; D285V) in a Danish patient with isolated chronic hemolytic anemia: mechanism of mutation and structure-function relationships. Hum Mutat. 1998;12(4):280-7. [PubMed Link Image]
  12. Maeda M, Yoshida A: Molecular defect of a phosphoglycerate kinase variant (PGK-Matsue) associated with hemolytic anemia: Leu----Pro substitution caused by T/A----C/G transition in exon 3. Blood. 1991 Mar 15;77(6):1348-52. [PubMed Link Image]
  13. Maeda M, Bawle EV, Kulkarni R, Beutler E, Yoshida A: Molecular abnormalities of a phosphoglycerate kinase variant generated by spontaneous mutation. Blood. 1992 May 15;79(10):2759-62. [PubMed Link Image]
  14. Fujii H, Krietsch WK, Yoshida A: A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK Munchen) associated with enzyme deficiency. J Biol Chem. 1980 Jul 10;255(13):6421-3. [PubMed Link Image]
  15. Huang IY, Fujii H, Yoshida A: Structure and function of normal and variant human phosphoglycerate kinase. Hemoglobin. 1980;4(5-6):601-9. [PubMed Link Image]
  16. Fujii H, Kanno H, Hirono A, Shiomura T, Miwa S: A single amino acid substitution (157 Gly----Val) in a phosphoglycerate kinase variant (PGK Shizuoka) associated with chronic hemolysis and myoglobinuria. Blood. 1992 Mar 15;79(6):1582-5. [PubMed Link Image]
  17. Fujii H, Chen SH, Akatsuka J, Miwa S, Yoshida A: Use of cultured lymphoblastoid cells for the study of abnormal enzymes: molecular abnormality of a phosphoglycerate kinase variant associated with hemolytic anemia. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2587-90. [PubMed Link Image]
  18. Fujii H, Yoshida A: Molecular abnormality of phosphoglycerate kinase-Uppsala associated with chronic nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5461-5. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 13044
Enzyme 6 Name Glycerate kinase
Enzyme 6 Synonyms
  1. HBeAg-binding protein 4
Enzyme 6 Gene Name GLYCTK
Enzyme 6 Protein Sequence >Glycerate kinase
MAAALQVLPRLARAPLHPLLWRGSVARLASSMALAEQARQLFESAVGAVLPGPMLHRALS
LDPGGRQLKVRDRNFQLRQNLYLVGFGKAVLGMAAAAEELLGQHLVQGVISVPKGIRAAM
ERAGKQEMLLKPHSRVQVFEGAEDNLPDRDALRAALAIQQLAEGLTADDLLLVLISGGGS
ALLPAPIPPVTLEEKQTLTRLLAARGATIQELNTIRKALSQLKGGGLAQAAYPAQVVSLI
LSDVVGDPVEVIASGPTVASSHNVQDCLHILNRYGLRAALPRSVKTVLSRADSDPHGPHT
CGHVLNVIIGSNVLALAEAQRQAEALGYQAVVLSAAMQGDVKSMAQFYGLLAHVARTRLT
PSMAGASVEEDAQLHELAAELQIPDLQLEEALETMAWGRGPVCLLAGGEPTVQLQGSGRG
GRNQELALRVGAELRRWPLGPIDVLFLSGGTDGQDGPTEAAGAWVTPELASQAAAEGLDI
ATFLAHNDSHTFFCCLQGGAHLLHTGMTGTNVMDTHLLFLRPR
Enzyme 6 Number of Residues 523
Enzyme 6 Molecular Weight 55253
Enzyme 6 Theoretical pI 6.72
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function ATP + (R)-glycerate = ADP + 3-phospho-(R)- glycerate
Enzyme 6 Pathways
  • Glycerolipid Metabolism (map00561 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
Enzyme 6 Reactions
  • ATP + (R)-glycerate = ADP + 3-phospho-(R)-glycerate [RN:R01514] ALL_REAC R01514
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 31616511 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q8IVS8 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GLCTK_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AY295075 Link Image
Enzyme 6 GeneCard ID Q8IVS8 Link Image
Enzyme 6 GenAtlas ID GLYCTK Link Image
Enzyme 6 HGNC ID HGNC:24247 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available