Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A6I7FCM5 · A0A6I7FCM5_9BACI

  • 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.

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.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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)
Site124Essential for DHBP synthase activity
Binding site138-142D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site141Mg2+ 2 (UniProtKB | ChEBI)
Binding site162D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site162Essential for DHBP synthase activity
Binding site251-255GTP (UniProtKB | ChEBI)
Binding site256Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site272GTP (UniProtKB | ChEBI)
Binding site294-296GTP (UniProtKB | ChEBI)
Binding site316GTP (UniProtKB | ChEBI)
Active site328Proton acceptor; for GTP cyclohydrolase activity
Active site330Nucleophile; for GTP cyclohydrolase activity
Binding site351GTP (UniProtKB | ChEBI)
Binding site356GTP (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

Enzyme and pathway databases

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
      M654_014875

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NSP9.1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0A6I7FCM5

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-199DHBP synthase
Region200-398GTP cyclohydrolase II
Domain208-372GTP 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    43,773
  • Last updated
    2020-08-12 v1
  • MD5 Checksum
    C7A5F1A81BA707037C37FFE1CCA0FCB5
MFHTIDEAIHDLKQGKVIIVVDDEDRENEGDFVALAEHATPEVINFMASHGRGLICAPLTEEIASRLDLHPMVDENTDAHHTAFTVSVDHRETKTGISAQERSLTVMSLIDENAGPLDFKRPGHIFPLIAKKGGVLKRAGHTEAAVDLAAACGSKPAGVICEIMNEDGTMARVPELKKIADQHGLKMITIKDLIEYRYSKGTLINREVGITLPSDFGTFKVFGYTNEIDNKEHIALVKGDVPFGDEPVLVRVHSECLTGDVFGSHRCDCGPQLAAALSQIENAGRGVLVYLRQEGRGIGLINKLKAYKLQEEGYDTVQANEQLGFRPDLRNYGIGAQILRDLGVKNMKLLTNNPRKIAGLEGYGLTIAGRIPLQMEANKDNEHYLKTKKAKLGHMLHF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP048273
EMBL· GenBank· DDBJ
QHZ47485.1
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.
Help