A0A6G6WE23 · A0A6G6WE23_9ACTN

  • 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 site41-42D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site42Mg2+ 1 (UniProtKB | ChEBI)
Binding site42Mg2+ 2 (UniProtKB | ChEBI)
Binding site46D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site140Essential for DHBP synthase activity
Binding site154-158D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site157Mg2+ 2 (UniProtKB | ChEBI)
Binding site178D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site178Essential for DHBP synthase activity
Binding site266-270GTP (UniProtKB | ChEBI)
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site282Zn2+ (UniProtKB | ChEBI); catalytic
Binding site284Zn2+ (UniProtKB | ChEBI); catalytic
Binding site287GTP (UniProtKB | ChEBI)
Binding site310-312GTP (UniProtKB | ChEBI)
Binding site332GTP (UniProtKB | ChEBI)
Active site344Proton acceptor; for GTP cyclohydrolase activity
Active site346Nucleophile; for GTP cyclohydrolase activity
Binding site367GTP (UniProtKB | ChEBI)
Binding site372GTP (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
      G5V58_12390

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • R-3366
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides

Accessions

  • Primary accession
    A0A6G6WE23

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-215DHBP synthase
Region216-423GTP cyclohydrolase II
Domain222-388GTP 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
    423
  • Mass (Da)
    45,952
  • Last updated
    2020-08-12 v1
  • Checksum
    CEB5D7A2475C2250
MTQSPSQPQPQHGGVRLDTVERAIADIAAGKAVVVVDDEGRENEGDLIFAASKATPELMAFTIRHSSGVICCPMPGAMLDRLEIPLMTPHNKDRMRTAYTISVDARDGVTTGISAADRAHTVKVLADSATESWEITRPGHVFPLRYREGGVLARRGHTEAAVDLARLAGLTPAGVLVEVVNDDGTMKRAPELRAFADEHGLAMISIEDLVRWRRRNEVLVKRVAETRLPTRHGDFTAYGYRITVDDSEHVALVYGDVSGPEPVLTRVHSECLTGDVFGSSRCDCGPQLDEAMDRIVAEGRGVVVYLRGHEGRGIGLVAKLQAYQLQDGGRDTVDANLDLGLPADARHYGAATQVLKDLGVTSVRLLTNNPDKVTNLEEYGVTVAERVPLTPHPNDHNLAYLLTKRDRMGHVLPGLEALEGVHQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP049257
EMBL· GenBank· DDBJ
QIG43456.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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