CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphoglycerate mutase-like
Functional Family Phosphoglycerate mutase

Enzyme Information

5.4.2.11
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
based on mapping to UniProt P18669
2-phospho-D-glycerate = 3-phospho-D-glycerate.
-!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1.
5.4.2.4
Bisphosphoglycerate mutase.
based on mapping to UniProt P18669
3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
-!- In the direction shown, the enzyme is phosphorylated by 3-phosphoglyceroyl phosphate to give phosphoenzyme and 3-phosphoglycerate. -!- The latter is rephosphorylated by the enzyme to yield 2,3- diphosphoglycerate, but this reaction is slowed down by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. -!- Also catalyzes, slowly, the reaction of EC 5.4.2.12. -!- Formerly EC 2.7.5.4.

UniProtKB Entries (1)

P18669
PGAM1_HUMAN
Homo sapiens
Phosphoglycerate mutase 1

PDB Structure

PDB 4GPI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation.
Hitosugi, T., Zhou, L., Fan, J., Elf, S., Zhang, L., Xie, J., Wang, Y., Gu, T.L., Aleckovic, M., Leroy, G., Kang, Y., Kang, H.B., Seo, J.H., Shan, C., Jin, P., Gong, W., Lonial, S., Arellano, M.L., Khoury, H.J., Chen, G.Z., Shin, D.M., Khuri, F.R., Boggon, T.J., Kang, S., He, C., Chen, J.
Nat Commun