Enzyme

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     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.7 With an iron-sulfur protein as acceptor
ID:1.2.7.6
Description:Glyceraldehyde-3-phosphate dehydrogenase (ferredoxin).
Alternative Name: Glyceraldehyde-3-phosphate ferredoxin reductase.
Glyceraldehyde-3-phosphate Fd oxidoreductase.
GAPOR.
Cath: 1.10.569.10; 1.10.599.10; 3.60.9.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.7.6
BRENDA Enzyme Link: BRENDA 1.2.7.6
KEGG Enzyme Link: KEGG1.2.7.6
BioCyc Enzyme Link: BioCyc 1.2.7.6
ExPASy Enzyme Link: ExPASy1.2.7.6
EC2PDB Enzyme Link: EC2PDB 1.2.7.6
ExplorEnz Enzyme Link: ExplorEnz 1.2.7.6
PRIAM enzyme-specific profiles Link: PRIAM 1.2.7.6
IntEnz Enzyme Link: IntEnz 1.2.7.6
MEDLINE Enzyme Link: MEDLINE 1.2.7.6
MSA:

1.2.7.6;

Phylogenetic Tree:

1.2.7.6;

Uniprot:
M-CSA:
RHEA:24148 D-glyceraldehyde 3-phosphate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = 3-phospho-D-glycerate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:7]=[CH;+0:8]-[*:9].[OH2;+0:10]>>[*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]=[C;H0;+0:8](-[*:9])-[OH;+0:10]
Reaction
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References

TitleAuthorsDatePubMed ID
The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation.van der Oost J, Schut G, Kengen SW, Hagen WR, Thomm M, de Vos WM1998 Oct 239774434
Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus.Mukund S, Adams MW1995 Apr 147721730
Aldehyde oxidoreductases from Pyrococcus furiosus.Roy R, Menon AL, Adams MW200111265456
Pyrococcus furiosus glyceraldehyde 3-phosphate oxidoreductase has comparable W(6+/5+) and W(5+/4+) reduction potentials and unusual [4Fe-4S] EPR properties.Hagedoorn PL, Freije JR, Hagen WR1999 Nov 2610580093