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InterPro: IPR011167 Iron-dependent fumarate hydratase

Protein matchesHelp
UniProtKB
Matches:
856 proteins
AccessionHelp IPR011167 Fe_dep_fumarate_hydratase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR004646 Fe-S type hydro-lyases tartrate/fumarate alpha region
IPR004647 Fe-S type hydro-lyases tartrate/fumarate beta region
IPR020557 Fumarate lyase, conserved site
GO Term annotationHelp
Process GO:0006091 generation of precursor metabolites and energy
Function GO:0004333 fumarate hydratase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Iron-dependent fumarate hydratase, or fumarase, is a bacterial enzyme that converts malate to fumarate. There are three fumarase proteins in Escherichia coli, FumA, FumB, and FumC, which fall into two biochemically distinct classes: class I (FumA, FumB) are dimeric enzymes and class II (FumC) are tetrameric enzymes, the latter sharing homology with eukaryotic enzymes [1]. This entry represents the class I enzymes. FumA functions in the citric acid cycle, accounting for 80% of the fumarase activity when the bacteria grows aerobically. FumB functions in the generation of fumarate as an anaerobic electron acceptor in the fermentative pathway that leads to the production of succinate.

Database linksHelp
Enzyme: EC:4.2.1.2

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011167 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0AC33 Fumarate hydratase class I, aerobic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004646 Fe-S type hydro-lyases tartrate/fumarate alpha region
IPR020557 Fumarate lyase, conserved site
IPR004647 Fe-S type hydro-lyases tartrate/fumarate beta region
IPR011167 Iron-dependent fumarate hydratase
SWISS-MODEL
ModBase

PublicationsHelp
1. Woods SA, Schwartzbach SD, Guest JR.
Two biochemically distinct classes of fumarase in Escherichia coli.
Biochim. Biophys. Acta 954 14-26 1988 [PubMed: 3282546]

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InterPro 23.1