P0AC48 · FRDB_ECOL6

Function

function

Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster.
[3Fe-4S] cluster (UniProtKB | Rhea| CHEBI:21137 )

Note: Binds 1 [3Fe-4S] cluster.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site14a menaquinone (UniProtKB | ChEBI)
Binding site58[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site63[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site66[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site78[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site149[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site152[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site155[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site159[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site205[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site211[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site215[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site226-229a menaquinone (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function3 iron, 4 sulfur cluster binding
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functionmetal ion binding
Molecular Functionsuccinate dehydrogenase (quinone) activity
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fumarate reductase iron-sulfur subunit
  • EC number
  • Alternative names
    • Quinol-fumarate reductase iron-sulfur subunit (QFR iron-sulfur subunit)

Gene names

    • Name
      frdB
    • Ordered locus names
      c5241

Organism names

Accessions

  • Primary accession
    P0AC48
  • Secondary accessions
    • P00364

Proteomes

Subcellular Location

Cell inner membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001587002-244Fumarate reductase iron-sulfur subunit

Interaction

Subunit

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-972Fe-2S ferredoxin-type
Domain140-1694Fe-4S ferredoxin-type

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    244
  • Mass (Da)
    27,123
  • Last updated
    2007-01-23 v2
  • Checksum
    AC1D7A73244D7AC0
MAEMKNLKIEVVRYNPEVDTAPHSAFYEVPYDATTSLLDALGYIKDNLAPDLSYRWSCRMAICGSCGMMVNNVPKLACKTFLRDYTDGMKVEALANFPIERDLVVDMTHFIESLEAIKPYIIGNSRTADQGTNIQTPAQMAKYHQFSGCINCGLCYAACPQFGLNPEFIGPAAITLAHRYNEDSRDHGKKERMAQLNSQNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKVESSKDFLIATLKPR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014075
EMBL· GenBank· DDBJ
AAN83663.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp