A0A6J4K4W3 · A0A6J4K4W3_9BACT

Function

function

Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 2 [4Fe-4S] clusters per monomer.
cob(II)alamin (UniProtKB | Rhea| CHEBI:16304 )

Pathway

tRNA modification; tRNA-queuosine biosynthesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site64cob(II)alamin (UniProtKB | ChEBI)
Active site137Proton donor
Binding site137cob(II)alamin (UniProtKB | ChEBI)
Binding site158cob(II)alamin (UniProtKB | ChEBI)
Binding site161cob(II)alamin (UniProtKB | ChEBI)
Binding site172cob(II)alamin (UniProtKB | ChEBI)
Binding site192[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site195[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site198[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site202[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site223[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site225cob(II)alamin (UniProtKB | ChEBI)
Binding site250[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site250-251cob(II)alamin (UniProtKB | ChEBI)
Binding site253[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site257[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioncobalamin binding
Molecular Functionepoxyqueuosine reductase activity
Molecular Functionmetal ion binding
Biological Processqueuosine biosynthetic process
Biological ProcesstRNA modification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Epoxyqueuosine reductase
  • EC number
  • Alternative names
    • Queuosine biosynthesis protein QueG

Gene names

    • Name
      queG
    • ORF names
      AVDCRST_MAG68-265

Organism names

Accessions

  • Primary accession
    A0A6J4K4W3

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain183-2124Fe-4S ferredoxin-type

Sequence similarities

Belongs to the QueG family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    392
  • Mass (Da)
    43,012
  • Last updated
    2020-10-07 v1
  • Checksum
    5FBD121E3D33E4ED
MHPNLTRAELTDRIRARALELGFEAVGIAPVRPSEHAERYGAWIGEGMHGEMAYLAREDAVAKRADPGVLVPDARSAVVVAIGYYSGDAEEADPSRGVVARYARNDDYHDLLKDRLIALQEWANAELTPLGGRAYVDAGPVLERELASRAGLGWFGRNTMLIQPRRGSYYFLGVLLLDVELEYDAPFTRDHCGSCSRCLSACPTGALLGRDEAGAPRMDARRCISYLTIELRGPIPRELRPLIGNRVYGCDICQEVCPWNSFAEPASDPAFIPRDGMEGPELIEWMGMTQEEFSRRFKGSAVKRTKRRGLLRNVAVALGNWGAPEAVPALAAALNDEEALVRGHAAWALGRIGTEAARQALSGRAEVEADAWVREEIALALGTDDRRQSDNQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADCTW010000002
EMBL· GenBank· DDBJ
CAA9295747.1
EMBL· GenBank· DDBJ
Genomic DNA

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