P00363 · FRDA_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

FAD (UniProtKB | Rhea| CHEBI:57692 )
Note: Binds 1 FAD covalently per subunit (PubMed:10373108, PubMed:24374335, PubMed:26644464).
Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE (PubMed:24374335, PubMed:26644464).

Activity regulation

Inhibited by oxaloacetate, a substrate analog.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site12-16FAD (UniProtKB | ChEBI)
Binding site36-38FAD (UniProtKB | ChEBI)
Binding site44-52FAD (UniProtKB | ChEBI)
Binding site156-158FAD (UniProtKB | ChEBI)
Binding site192-193FAD (UniProtKB | ChEBI)
Binding site212FAD (UniProtKB | ChEBI)
Active site233
Active site249
Binding site356-357FAD (UniProtKB | ChEBI)
Binding site380FAD (UniProtKB | ChEBI)
Binding site391-397FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmembrane
Cellular Componentplasma membrane
Cellular Componentplasma membrane fumarate reductase complex
Molecular Functionelectron transfer activity
Molecular FunctionFAD binding
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionsuccinate dehydrogenase (quinone) activity
Molecular Functionsuccinate dehydrogenase activity
Biological Processanaerobic electron transport chain
Biological Processanaerobic respiration
Biological Processbacterial-type flagellum assembly
Biological ProcessDNA damage response
Biological Processfermentation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      frdA
    • Ordered locus names
      b4154, JW4115

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / MG1655 / ATCC 47076
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / RP437
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P00363
  • Secondary accessions
    • Q2M6E8

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

No anaerobic growth on glycerol fumarate medium.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis45Inactivates enzyme.
Mutagenesis45Decreased ability (greater than 70%) to reduce fumarate.
Mutagenesis131Increased cross-linking to SdhE, FrdA is slightly less flavinylated.
Mutagenesis177No longer forms cross-link to SdhE, FrdA is still flavinylated.
Mutagenesis178Decreased cross-linking to SdhE, FrdA is still flavinylated.
Mutagenesis207Increased cross-linking to SdhE, FrdA is flavinylated.
Mutagenesis233Severely affects succinate oxidation, decreases fumarate oxidation by 75%.
Mutagenesis240Increased cross-linking to SdhE, FrdA is flavinylated.
Mutagenesis248Does not inactivate enzyme.
Mutagenesis249Inactivates enzyme.

Chemistry

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001586602-602Fumarate reductase flavoprotein subunit
Modified residue45Tele-8alpha-FAD histidine

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) (PubMed:10373108, PubMed:11850430).
Can be cross-linked to SdhE (PubMed:26644464).
Purified from membrane fractions associated with protoporphyrinogen IX dehydrogenase (hemG) (PubMed:20484676).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P00363frdB P0AC474EBI-550480, EBI-906724
BINARY P00363hemG P0ACB42EBI-550480, EBI-1115706
BINARY P00363ydcZ P761112EBI-550480, EBI-550492
View interactors in UniProtKB
View CPX-1967 in Complex Portal

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region581-602Disordered
Compositional bias583-602Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    602
  • Mass (Da)
    65,972
  • Last updated
    2007-01-23 v3
  • Checksum
    3306D7FF6E198AE9
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKANG

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict386in Ref. 1; AAA23437
Compositional bias583-602Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J01611
EMBL· GenBank· DDBJ
AAA23437.1
EMBL· GenBank· DDBJ
Genomic DNA
U14003
EMBL· GenBank· DDBJ
AAA97053.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC77114.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAE78158.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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