A0A1F2Y6U6 · A0A1F2Y6U6_9BACL

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.
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 site249-253GTP (UniProtKB | ChEBI)
Binding site254Zn2+ (UniProtKB | ChEBI); catalytic
Binding site265Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270GTP (UniProtKB | ChEBI)
Binding site292-294GTP (UniProtKB | ChEBI)
Binding site314GTP (UniProtKB | ChEBI)
Active site326Proton acceptor; for GTP cyclohydrolase activity
Active site328Nucleophile; for GTP cyclohydrolase activity
Binding site349GTP (UniProtKB | ChEBI)
Binding site354GTP (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
      A2201_13315

Organism names

Accessions

  • Primary accession
    A0A1F2Y6U6

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-199DHBP synthase
Region200-396GTP cyclohydrolase II
Domain206-370GTP 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
    396
  • Mass (Da)
    43,288
  • Last updated
    2017-02-15 v1
  • Checksum
    07785B49BF41999F
MFDKIEAALADLRDGKAVIVVDDEDRENEGDFVALGSKTDAAMINFMITHGRGLLCVPIEEERAGRLGFRAMVERNTDSFGTAFTISVDAEPTHTGISAFERAQTVAAIVSESTGPDDFRKPGHIFPLIAKSGGVLRRAGHTEAAVDLARLSGEPGVGVICEILNEDGTMARLPQLEVIAQQHGLKLITIADLIAYRKEQEILVQRQASATLPTAYGDFTAVMYTNKLDDKEHLALVKGDLNDEPTLVRVHSECLTGDAFGSLRCDCGPQLHAALAQIEREGKGVLLYLRQEGRGIGLINKIKAYALQDEGADTVEANHKLGFAADLRDYGIGAQILYDLGVREMRLLTNNPRKVKGIEGHGLEVVERVPLEVDRNPHNEQYLQTKKEKLGHLLHL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MELW01000238
EMBL· GenBank· DDBJ
OFW77191.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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