A0A1I6DIY6 · A0A1I6DIY6_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.

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 site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site125Essential for DHBP synthase activity
Binding site139-143D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site142Mg2+ 2 (UniProtKB | ChEBI)
Binding site163D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site163Essential for DHBP synthase activity
Binding site251-255GTP (UniProtKB | ChEBI)
Binding site256Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site272GTP (UniProtKB | ChEBI)
Binding site294-296GTP (UniProtKB | ChEBI)
Binding site316GTP (UniProtKB | ChEBI)
Active site328Proton acceptor; for GTP cyclohydrolase activity
Active site330Nucleophile; for GTP cyclohydrolase activity
Binding site351GTP (UniProtKB | ChEBI)
Binding site356GTP (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
      SAMN05660706_11210

Organism names

Accessions

  • Primary accession
    A0A1I6DIY6

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-200DHBP synthase
Region201-406GTP cyclohydrolase II
Domain207-372GTP 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
    406
  • Mass (Da)
    44,708
  • Last updated
    2017-11-22 v1
  • Checksum
    3880DD8123B95FB9
MPFSTIEEAIEDIRQGKMLVVVDDEDRENEGDLIMAAEKVTPEAIAFMATYGRGLICMPIVGSRLDELDLQAMVTNNTDPHGTAFTVSVDYKETTTGISAHERAATVRAILDPDTKPDDLRRPGHIFPLRAKEGGVLRRAGHTEAAVDLTRLAGLYPAGVICEIMKDDGTMARVPELIEFCKTHGLKLVTIADLIEYRRHHEKLIRRVDSAKLPTSYGHFVAVAYESLLDKKEHIALVKGNLSSVEAPLVRVHSECLTGDVFGSARCDCGDQLARALEMIEKEGVGVLLYMRQEGRGIGLSNKIRAYRLQDQGKDTVEANEALGFPADLRDYGIGAQILADLGLSKIRLMTNNPRKIAGLEGHGLEVVGRVPIEICPKRENKFYLSTKKRKLGHLLSIEDVSKKSS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOYM01000012
EMBL· GenBank· DDBJ
SFR05399.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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