Aldehyde ferredoxin oxidoreductase, N-terminal (IPR013983)

Short name: Ald_Fedxn_OxRdtase_N

Overlapping homologous superfamilies

Domain relationships



Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [PMID: 9242907] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [PMID: 8672295]. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea [PMID: 9242907]; carboxylic acid reductase found in clostridia [PMID: 2550230]; and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum [PMID: 8026480]. GAPOR may be involved in glycolysis [PMID: 7721730], but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases [PMID: 9275170].

This entry represents the N-terminal domain of these enzymes. This domain has been shown to interact with the tungsten cofactor [PMID: 7878465].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0051536 iron-sulfur cluster binding
GO:0016491 oxidoreductase activity
GO:0016625 oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.