A0A0E2H7T7 · A0A0E2H7T7_9FIRM

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.

TypeIDPosition(s)Description
Binding site28-29D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site29Mg2+ 1 (UniProtKB | ChEBI)
Binding site29Mg2+ 2 (UniProtKB | ChEBI)
Binding site33D-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

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
      HMPREF1090_03450

Organism names

Accessions

  • Primary accession
    A0A0E2H7T7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-201DHBP synthase
Region202-399GTP cyclohydrolase II
Domain210-373GTP 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
    399
  • Mass (Da)
    44,756
  • Last updated
    2015-05-27 v1
  • Checksum
    B38C385EBDADA30F
MEGFNTIEEVLDDLRQGKIVLVTDDESRENEGDFICAAQYATTENVNFMAVHGRGLICMPMSTQLCTRLKLPQMVSDNSDNHETAFTVSIDHISTSTGISAAERGVTARQCVNALSRPEDFRRPGHMFPLAARKNGVLERNGHTEATVDLMRLAGLSECGLCCEIMREDGTMMRMPQLLQYAGQWNMKITTIKALQDYRKQHDTLVECAAVTHMPTRYGTFKAYGYRNLLNGEHHVALVKGEIGDGRDLLCRVHSECLTGDAFGSLRCDCGQQLAAAMARIEQEGRGVLLYMRQEGRGIGLLNKLRAYELQDQGMDTLEANLALGFPGDLREYFIGAQILRDLGARTLRLLTNNPDKVYQLSGFGLDIKERVPIQMTPTDHNLFYLRTKEQRMGHLTHY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGYR01000039
EMBL· GenBank· DDBJ
ENZ12327.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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