A0A075R1S5 · A0A075R1S5_BRELA

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.

TypeIDPosition(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 site250-254GTP (UniProtKB | ChEBI)
Binding site255Zn2+ (UniProtKB | ChEBI); catalytic
Binding site266Zn2+ (UniProtKB | ChEBI); catalytic
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271GTP (UniProtKB | ChEBI)
Binding site293-295GTP (UniProtKB | ChEBI)
Binding site315GTP (UniProtKB | ChEBI)
Active site327Proton acceptor; for GTP cyclohydrolase activity
Active site329Nucleophile; for GTP cyclohydrolase activity
Binding site350GTP (UniProtKB | ChEBI)
Binding site355GTP (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
      BRLA_c022210

Organism names

Accessions

  • Primary accession
    A0A075R1S5

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-199DHBP synthase
Region200-398GTP cyclohydrolase II
Domain206-371GTP 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)
    44,619
  • Last updated
    2014-10-29 v1
  • Checksum
    D014125F0EE5E510
MLHTIEEALEELRQGKPIIVVDDENRENEGDFLCMAEKATPEMINFMVTHGRGLVCVSIEDKRARELQLRQMVENNTDHHGTAFTVSIDERDTHTGISAHERSQTIMAMLDPQAEADRFRRPGHIFPLVAKEGGVLKRAGHTEAAVDLARLAGGYPAGVICEIMQEDGSMARLPALLEIAKRLDVKIVSIEQLIHYRMQSESLVKKEAETILPTEYGDFRIFAYSNTLDGKEHVALVKGDIRPYQPVLVRVHSECLTGDIFGSLRCDCGPQLHAALQQIDEVGAGILLYMRQEGRGIGLINKLKAYQLQEEGLDTVEANERLGFPADLREYGIGAQILRDLGAKKLRLLTNNPRKIVALNGYGLKVAERVPLQMKSHQHNYHYLHTKQQKLGHMLTIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007806
EMBL· GenBank· DDBJ
AIG26542.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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