F1VYJ2 · F1VYJ2_9BURK

Function

function

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.

Caution

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:
Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Note: Binds 1 divalent metal cation per subunit.

Pathway

Carbohydrate degradation.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site11substrate
Binding site36a divalent metal cation (UniProtKB | ChEBI)
Active site38Proton acceptor
Binding site38a divalent metal cation (UniProtKB | ChEBI)
Binding site69a divalent metal cation (UniProtKB | ChEBI)
Binding site69substrate
Binding site145-148substrate
Active site178Proton donor
Binding site178a divalent metal cation (UniProtKB | ChEBI)
Binding site178-180substrate
Binding site180substrate
Binding site200-201substrate

GO annotations

AspectTerm
Molecular FunctionD-ribulose-phosphate 3-epimerase activity
Molecular Functionmetal ion binding
Biological Processpentose catabolic process
Biological Processpentose-phosphate shunt

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribulose-phosphate 3-epimerase
  • EC number

Gene names

    • Name
      rpe
    • ORF names
      IMCC9480_2601

Organism names

Accessions

  • Primary accession
    F1VYJ2

Proteomes

Family & Domains

Sequence similarities

Belongs to the ribulose-phosphate 3-epimerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    223
  • Mass (Da)
    23,865
  • Last updated
    2011-05-31 v1
  • Checksum
    18B84BDC88554BFD
MTMPTYHIAPSILSADFARLGEEVRNVVSAGADIIHFDVMDNHYVPNLTIGPLVCAAIRPHVQVPIDVHLMVKPVDRLIPDFAKAGANIISFHPEASEHIDRTLQLIRDNGCKAGLVFNPGTPLHFLDHVMDKIDLILIMSVNPGFGGQSFIPEALKKIAAVRKLIDESGRTILLEVDGGIKIENIAAAAKAGADTFVAGSAIFGAADYKTVIDAMRAELAGA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEPR01000248
EMBL· GenBank· DDBJ
EGF32338.1
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