Summary: Fumarate reductase flavoprotein C-term
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Fumarate reductase flavoprotein C-term Provide feedback
This family contains fumarate reductases, succinate dehydrogenases and L-aspartate oxidases.
Internal database links
|SCOOP:||Retrotrans_gag Myb_DNA-bind_4 MLANA|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015939
This entry represents a domain with a spectrin-repeat-like fold consisting of three helices in a closed bundle with a left-handed twist. This domain is found in the succinate dehydrogenase/fumarate reductase oxidoreductase family of proteins, such as:
- L-aspartate oxidase (EC), a flavoenzyme component of the bacterial quinolinate synthase system that catalyses the conversion of L-aspartate to oxaloacetate, the first step in the de novo biosynthesis of NAD+ [PUBMED:11863440, PUBMED:10425677].
- Fumarate reductase, which is part of the quinol-fumarate reductase (QFR) respiratory complex that catalyses the terminal step of anaerobic respiration when fumarate acts as the terminal electron acceptor [PUBMED:11850430].
- Succinate dehydrogenase (SQR; EC), an iron-sulphur flavoenzyme from bacteria that is analogous to the mitochondrial respiratory complex II, forming part of the electron transport pathway from the electron acceptor (succinate) to the terminal donor (ubiquinone) [PUBMED:12560550].
- Adenylylsulphate reductase A subunit (EC), an iron-sulphur flavoenzyme that catalyses the reversible reduction of adenosine-5'-phosphate (APS) to sulphite and AMP [PUBMED:11842205].
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Structural domain|
|Number in seed:||765|
|Number in full:||35138|
|Average length of the domain:||118.70 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||20.56 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There are 9 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Succ_DH_flav_C domain has been found. There are 111 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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