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A0A0D7LL41 · A0A0D7LL41_CITFR

  • Protein
    Pyruvate dehydrogenase [ubiquinone]
  • Gene
    poxB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO2. It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Activity regulation

The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site50thiamine diphosphate (UniProtKB | ChEBI)
Binding site251-254FAD (UniProtKB | ChEBI)
Binding site274-278FAD (UniProtKB | ChEBI)
Binding site292FAD (UniProtKB | ChEBI)
Binding site406-408thiamine diphosphate (UniProtKB | ChEBI)
Binding site433Mg2+ (UniProtKB | ChEBI)
Binding site433-435thiamine diphosphate (UniProtKB | ChEBI)
Binding site460Mg2+ (UniProtKB | ChEBI)
Binding site460-466thiamine diphosphate (UniProtKB | ChEBI)
Site465Moves into active site upon enzyme activation, plays a role in electron transfer

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionlipid binding
Molecular Functionmagnesium ion binding
Molecular Functionpyruvate dehydrogenase (quinone) activity
Molecular Functionthiamine pyrophosphate binding
Molecular Functionubiquinone binding
Biological Processpyruvate catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate dehydrogenase [ubiquinone]
  • EC number
  • Alternative names
    • Pyruvate oxidase
      (POX
      )
    • Pyruvate:ubiquinone-8 oxidoreductase

Gene names

    • Name
      poxB
    • ORF names
      AI2602V1_1800
      , AI2666V1_1610
      , AI2935V1_1888
      , AN672_10600
      , B9P89_08315
      , HV178_08830
      , HXS83_09440
      , I9Y29_000164
      , IF853_14410
      , KY227_000567
      , P7U51_001650
      , PF691_08200
      , PQQ21_000262
      , RYZ67_14185
      , RZR66_06465
      , SGX49_002978
      , SJ346_06885

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 18
    • 112
    • ISC11
    • ST62:944112508
    • C191
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter > Citrobacter freundii complex

Accessions

  • Primary accession
    A0A0D7LL41

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain4-116Thiamine pyrophosphate enzyme N-terminal TPP-binding
Region183-334FAD-binding domain
Domain192-319Thiamine pyrophosphate enzyme central
Region335-530PP-binding domain
Domain379-525Thiamine pyrophosphate enzyme TPP-binding
Region531-572Membrane-binding domain

Domain

Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.

Sequence similarities

Belongs to the TPP enzyme family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    572
  • Mass (Da)
    62,094
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    4833ADCE8E5E51AC496514F7BE3AC937
MKQTVAAFIAKTLEQAGVKRIWGVTGDSLNGLSDSLNRMGTIDWMPTRHEEVAAFAAGAEAQLTGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPESATTHWYHAPLPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAAKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLILLGTQFPYRPFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALLPLVEEKTERQFLDKALEHYREARKGLDDLAKPSDKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQATEPGRQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIIVFNNSVLGFVAMEMKAGGYLTDGTELHDTNFARIAEACGITGIRVEKSSEVDEALQRAMSIDGPVLVDVVVAKEELAIPPQIKLEQAKGFSLYMLRAIISGRGDEVIELAKTNWLR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
OW848788
EMBL· GenBank· DDBJ
CAH3279356.1
EMBL· GenBank· DDBJ
Genomic DNA
OW849256
EMBL· GenBank· DDBJ
CAH3618696.1
EMBL· GenBank· DDBJ
Genomic DNA
OW995941
EMBL· GenBank· DDBJ
CAH6581838.1
EMBL· GenBank· DDBJ
Genomic DNA
CBWP010000021
EMBL· GenBank· DDBJ
CDL37018.1
EMBL· GenBank· DDBJ
Genomic DNA
ABBJDF010000002
EMBL· GenBank· DDBJ
EHT9937540.1
EMBL· GenBank· DDBJ
Genomic DNA
ABOSXX010000013
EMBL· GenBank· DDBJ
ELV3680539.1
EMBL· GenBank· DDBJ
Genomic DNA
ABLGCN030000003
EMBL· GenBank· DDBJ
EMM7457165.1
EMBL· GenBank· DDBJ
Genomic DNA
ABKLER030000001
EMBL· GenBank· DDBJ
EMN4143072.1
EMBL· GenBank· DDBJ
Genomic DNA
DACSXJ010000001
EMBL· GenBank· DDBJ
HAT3895788.1
EMBL· GenBank· DDBJ
Genomic DNA
LJEB01000042
EMBL· GenBank· DDBJ
KPR55570.1
EMBL· GenBank· DDBJ
Genomic DNA
JACYCN010000027
EMBL· GenBank· DDBJ
MBD5600983.1
EMBL· GenBank· DDBJ
Genomic DNA
JAWIHX010000004
EMBL· GenBank· DDBJ
MDV2042570.1
EMBL· GenBank· DDBJ
Genomic DNA
JAWPBU010000015
EMBL· GenBank· DDBJ
MDW2759624.1
EMBL· GenBank· DDBJ
Genomic DNA
JAXABZ010000002
EMBL· GenBank· DDBJ
MDX7209873.1
EMBL· GenBank· DDBJ
Genomic DNA
NEFA01000007
EMBL· GenBank· DDBJ
OYR05875.1
EMBL· GenBank· DDBJ
Genomic DNA
CP058318
EMBL· GenBank· DDBJ
QLD06680.1
EMBL· GenBank· DDBJ
Genomic DNA
CP056573
EMBL· GenBank· DDBJ
QLV30080.1
EMBL· GenBank· DDBJ
Genomic DNA
CP115614
EMBL· GenBank· DDBJ
WBS48993.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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