Hmdb loader
Identification
HMDB Protein ID HMDBP00266
Secondary Accession Numbers
  • 5498
  • HMDBP09155
Name Bisphosphoglycerate mutase
Synonyms
  1. 2,3-bisphosphoglycerate mutase, erythrocyte
  2. 2,3-bisphosphoglycerate synthase
  3. BPG-dependent PGAM
  4. BPGM
  5. 2,3-diphosphoglycerate mutase
  6. DPGM
Gene Name BPGM
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.
Pathways
  • Fanconi-bickel syndrome
  • Fructose-1,6-diphosphatase deficiency
  • Gluconeogenesis
  • Glycine, serine and threonine metabolism
  • Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
  • Glycogenosis, Type IA. Von gierke disease
  • Glycogenosis, Type IB
  • Glycogenosis, Type IC
  • Glycogenosis, Type VII. Tarui disease
  • Glycolysis
  • Glycolysis / Gluconeogenesis
  • Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
  • Triosephosphate isomerase
Reactions
Glyceric acid 1,3-biphosphate → 2,3-Diphosphoglyceric acid details
2-Phospho-D-glyceric acid → 3-Phosphoglyceric acid details
2,3-Diphosphoglyceric acid + Water → 3-Phosphoglyceric acid + Phosphate details
GO Classification
Biological Process
glycolysis
respiratory gaseous exchange
erythrocyte development
carbohydrate metabolic process
Function
catalytic activity
isomerase activity
intramolecular transferase activity
intramolecular transferase activity, phosphotransferases
Molecular Function
bisphosphoglycerate 2-phosphatase activity
bisphosphoglycerate mutase activity
phosphoglycerate mutase activity
Process
metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
glucose catabolic process
glycolysis
Cellular Location Not Available
Gene Properties
Chromosome Location 7
Locus 7q33
SNPs BPGM
Gene Sequence
>780 bp
ATGTCCAAGTACAAACTTATTATGTTAAGACATGGAGAGGGTGCTTGGAATAAGGAGAAC
CGTTTTTGTAGCTGGGTGGATCAGAAACTCAACAGCGAAGGAATGGAGGAAGCTCGGAAC
TGTGGGAAGCAACTCAAAGCGTTAAACTTTGAGTTTGATCTTGTATTCACATCTGTCCTT
AATCGGTCCATTCACACAGCCTGGCTGATCCTGGAAGAGCTAGGCCAGGAATGGGTGCCT
GTGGAAAGCTCCTGGCGTCTAAATGAGCGTCACTATGGGGCCTTGATCGGTCTCAACAGG
GAGCAGATGGCTTTGAATCATGGTGAAGAACAAGTGAGGCTCTGGAGAAGAAGCTACAAT
GTAACCCCGCCTCCCATTGAGGAGTCTCATCCTTACTACCAAGAAATCTACAACGACCGG
AGGTATAAAGTATGCGATGTGCCCTTGGATCAACTGCCACGGTCGGAAAGCTTAAAGGAT
GTTCTGGAGAGACTCCTTCCCTATTGGAATGAAAGGATTGCTCCCGAAGTATTACGTGGC
AAAACCATTCTGATATCTGCTCATGGAAATAGCAGTAGGGCACTCCTAAAACACCTGGAA
GGTATCTCAGATGAAGACATCATCAACATTACTCTTCCTACTGGAGTCCCCATTCTTCTG
GAATTGGATGAAAACCTGCGTGCTGTTGGGCCTCATCAGTTCCTGGGTGACCAAGAGGCG
ATCCAAGCAGCCATTAAGAAAGTAGAAGATCAAGGAAAAGTGAAACAAGCTAAAAAATAG
Protein Properties
Number of Residues 259
Molecular Weight 30004.98
Theoretical pI 6.543
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Bisphosphoglycerate mutase
MSKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVL
NRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYN
VTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRG
KTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEA
IQAAIKKVEDQGKVKQAKK
GenBank ID Protein 16877598
UniProtKB/Swiss-Prot ID P07738
UniProtKB/Swiss-Prot Entry Name PMGE_HUMAN
PDB IDs
GenBank Gene ID BC017050
GeneCard ID BPGM
GenAtlas ID BPGM
HGNC ID HGNC:1093
References
General References
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  5. 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:3036106 ]
  6. 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:2844822 ]
  7. Fujita T, Suzuki K, Tada T, Yoshihara Y, Hamaoka R, Uchida K, Matuo Y, Sasaki T, Hanafusa T, Taniguchi N: Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro. J Biochem. 1998 Dec 1;124(6):1237-44. [PubMed:9832630 ]
  8. 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:8440681 ]
  9. 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:1387804 ]
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