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Information on EC 5.4.2.11 - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and Organism(s) Danio rerio

for references in articles please use BRENDA:EC5.4.2.11
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EC Tree
IUBMB Comments
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi 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 (His10 in man and Escherichia coli, His8 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 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
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Danio rerio
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
phosphoglycerate mutase, pgam1, phosphoglycerate mutase 1, sts-1, pgam2, cofactor-dependent phosphoglycerate mutase, dpgm-b, bisphosphoglycerate phosphatase, rv3214, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase, more
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-dependent)
The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi 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 (His10 in man and Escherichia coli, His8 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 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reactions of EC 5.4.2.4 bisphosphoglycerate mutase.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q7SZR4_DANRE
254
0
28912
TrEMBL
other Location (Reliability: 3)
Q7T3G4_DANRE
255
0
28824
TrEMBL
other Location (Reliability: 4)
B8A4H6_DANRE
254
0
28845
TrEMBL
other Location (Reliability: 3)
A8KBY7_DANRE
259
0
29755
TrEMBL
other Location (Reliability: 3)
Q6DHM0_DANRE
259
0
29671
TrEMBL
other Location (Reliability: 2)
Q6TNR9_DANRE
254
0
28838
TrEMBL
other Location (Reliability: 2)
A7MCL3_DANRE
227
0
25791
TrEMBL
other Location (Reliability: 4)
Q7SYB4_DANRE
254
0
28814
TrEMBL
other Location (Reliability: 3)