A0A925ZXP0 · A0A925ZXP0_9BACT

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.

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:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.

Features

Showing features for binding site, site, active site.

Type
IDPosition(s)Description
Binding site26-27D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site27Mg2+ 1 (UniProtKB | ChEBI)
Binding site27Mg2+ 2 (UniProtKB | ChEBI)
Binding site31D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site126Essential for DHBP synthase activity
Binding site140-144D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site143Mg2+ 2 (UniProtKB | ChEBI)
Binding site164D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site164Essential for DHBP synthase activity
Binding site252-256GTP (UniProtKB | ChEBI)
Binding site257Zn2+ (UniProtKB | ChEBI); catalytic
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273GTP (UniProtKB | ChEBI)
Binding site295-297GTP (UniProtKB | ChEBI)
Binding site317GTP (UniProtKB | ChEBI)
Active site329Proton acceptor; for GTP cyclohydrolase activity
Active site331Nucleophile; for GTP cyclohydrolase activity
Binding site352GTP (UniProtKB | ChEBI)
Binding site357GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP binding
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin biosynthesis protein RibBA

Including 2 domains:

  • Recommended name
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • EC number
  • Short names
    DHBP synthase
  • Recommended name
    GTP cyclohydrolase-2
  • EC number
  • Alternative names
    • GTP cyclohydrolase II

Gene names

    • Name
      ribBA
    • ORF names
      H7Z21_05305

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ES-bin-153
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Hymenobacteraceae > Hymenobacter

Accessions

  • Primary accession
    A0A925ZXP0

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-201DHBP synthase
Region202-414GTP cyclohydrolase II
Domain210-372GTP cyclohydrolase II

Sequence similarities

In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    414
  • Mass (Da)
    45,235
  • Last updated
    2023-02-22 v1
  • MD5 Checksum
    6A42BC0D987C0A05265740B5D92B5F5C
MLDSIEDAIADIRAGKVVVVVDDEDRENEGDFICAARCATPDVINFMATHGRGLVCAPLSEELCETLGLELMVGRNTALHATPFTVSIDLLKNGVTTGISTSDRSKTILALIDPATKPEELGKPGHIFPLKARKEGVLRRAGHTEAAVDLARLAGFEPAGVLVEILREDGEMARLPELRAVATRWNLKLISVQDLIKYRLAKESLIARDISVRMPTQWGDFDLYAYTQRSNGAQHLALVKGDISTPEPVLVRVHSSCVTGDIFGSCRCDCGPQLHKAMEQIELEGRGVVVYMNQEGRGIGLLNKLRAYKLQEQGRDTVEANVELGFGVDERDYGVGAQILRDLGISQMRLLSNNPRKRTGLVGYGLEIVESVAIEIEPNEHNQTYLATKRDKLGHTILGHVPVPHLNPDAADVA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACMJH010000270
EMBL· GenBank· DDBJ
MBC8082610.1
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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help