P0AC47 · FRDB_ECOLI

Function

function

Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol-binding sites are functionally relevant (PubMed:10373108, PubMed:11850430).

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 Componentcytosol
Cellular Componentmembrane
Cellular Componentplasma membrane fumarate reductase complex
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 Functioniron-sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionsuccinate dehydrogenase (quinone) activity
Biological Processanaerobic electron transport chain
Biological Processanaerobic respiration
Biological Processbacterial-type flagellum assembly
Biological Processfermentation
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
      b4153, JW4114

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P0AC47
  • Secondary accessions
    • P00364
    • Q2M6E9

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis58Affects center 1 (2Fe-2S).
Mutagenesis63Affects center 1 (2Fe-2S).
Mutagenesis66Affects center 1 (2Fe-2S).
Mutagenesis78Affects center 1 (2Fe-2S).

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001586982-244Fumarate reductase iron-sulfur subunit

Proteomic databases

Interaction

Subunit

Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P0AC47frdA P003634EBI-906724, EBI-550480
BINARY P0AC47mutT P083374EBI-906724, EBI-1121389
BINARY P0AC47ompW P0A9152EBI-906724, EBI-1132929
View interactors in UniProtKB
View CPX-1967 in Complex Portal

Protein-protein interaction databases

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
J01611
EMBL· GenBank· DDBJ
AAA23438.1
EMBL· GenBank· DDBJ
Genomic DNA
U14003
EMBL· GenBank· DDBJ
AAA97052.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC77113.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE78157.1
EMBL· GenBank· DDBJ
Genomic DNA
V00277
EMBL· GenBank· DDBJ
CAA23534.1
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.
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