D1PSV0 · D1PSV0_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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site59cob(II)alamin (UniProtKB | ChEBI)
Active site132Proton donor
Binding site132cob(II)alamin (UniProtKB | ChEBI)
Binding site153cob(II)alamin (UniProtKB | ChEBI)
Binding site156cob(II)alamin (UniProtKB | ChEBI)
Binding site167cob(II)alamin (UniProtKB | ChEBI)
Binding site186[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site189[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site192[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site196[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site212[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site214cob(II)alamin (UniProtKB | ChEBI)
Binding site239[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site239-240cob(II)alamin (UniProtKB | ChEBI)
Binding site242[4Fe-4S] cluster 2 (UniProtKB | ChEBI)
Binding site246[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site297tRNA (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
      HMPREF0645_0059

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 17361
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Hallella

Accessions

  • Primary accession
    D1PSV0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain174-2064Fe-4S ferredoxin-type

Sequence similarities

Belongs to the QueG family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    311
  • Mass (Da)
    35,777
  • Last updated
    2010-02-09 v1
  • Checksum
    B4EFBC94BD790879
MSSRFSNEIKAEAKRLGFFSCGIAKAERVSQEVENHLRQWLADGMNADMEWMGNYLDKRMDPRLLMDGLKSIVSVAMNYAPTQRLPQDQPQIAAYALGQDYHEVMKQRLHRLAAFIYGEDRLKDANYRVFVDSGPVLERYWAVRAGLGWVGKNRQLIIPHAGSMFFLGELFLDFETDYDRPIADRCGACTKCIDHCPTRALSPNHDFNSTLCLSYQTIENRKELSEEAKKAMGNVIYGCDRCQAACPWNRFATPSDIPEFQPKPELLRMTRDNWKNLSVEDYRRLFKGSAVKRVKYKGLMRNISTLFSEGE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACKS01000009
EMBL· GenBank· DDBJ
EFA45468.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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