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A0A7Y4QVV4 · A0A7Y4QVV4_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.
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 site71-72D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site72Mg2+ 2 (UniProtKB | ChEBI)
Binding site72Mg2+ 1 (UniProtKB | ChEBI)
Binding site76D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site170Essential for DHBP synthase activity
Binding site184-188D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site187Mg2+ 2 (UniProtKB | ChEBI)
Binding site208D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site208Essential for DHBP synthase activity
Binding site296-300GTP (UniProtKB | ChEBI)
Binding site301Zn2+ (UniProtKB | ChEBI); catalytic
Binding site312Zn2+ (UniProtKB | ChEBI); catalytic
Binding site314Zn2+ (UniProtKB | ChEBI); catalytic
Binding site317GTP (UniProtKB | ChEBI)
Binding site339-341GTP (UniProtKB | ChEBI)
Binding site361GTP (UniProtKB | ChEBI)
Active site373Proton acceptor; for GTP cyclohydrolase activity
Active site375Nucleophile; for GTP cyclohydrolase activity
Binding site396GTP (UniProtKB | ChEBI)
Binding site401GTP (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
      HOP31_16825

Organism names

Accessions

  • Primary accession
    A0A7Y4QVV4

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-18Basic and acidic residues
Region1-44Disordered
Region1-245DHBP synthase
Compositional bias19-44Polar residues
Region246-449GTP cyclohydrolase II
Domain252-417GTP 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
    449
  • Mass (Da)
    50,000
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    A948E39121116DA59D40183F672D34C5
MKTHNTKTNSDRSHSNKTQGKKSLPVKQKNTAPSSNGSDRNNGKFKFSSIESAIADFKKGKCVIVIDDEDRENEGDLIYSAEKSTPGLVNFLIKYTSGVICVPMEDDRLKALKLDMMTNHNTALHETAFTISVDYVHGTSTGISASDRNKTILSLVNKKTKPEDLGRPGHVFPLKAFPGGVLRRAGHTEAAVDLAKLAGHYPAGVLCEIIKKDGEMARVPQLFELAKKHKLKIITIKDLINYRLEREVLIEKIVDVNLPTRHGAFRLHMFKNLIDNKEHLALVKGEIDPNKPILVRVHSECLTGDLLGSLRCDCQDQLIKSLKIIEHEKNGILLYMRQEGRGIGLANKLKAYKLQDEGADTVEANEALGFKADLRDYGIGAQILRNLGVKKMVLLTNNPKKVVGLKGYGLEIVKRIPIEIPANSVNERYLKTKRDKLGHLLLINKNQEN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Basic and acidic residues
Compositional bias19-44Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFSP010000414
EMBL· GenBank· DDBJ
NOS86798.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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