A0A316MMN3 · A0A316MMN3_9BACT

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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site126Essential for DHBP synthase activity
Binding site164D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site164Essential for DHBP synthase activity
Binding site253-257GTP (UniProtKB | ChEBI)
Binding site258Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site274GTP (UniProtKB | ChEBI)
Binding site296-298GTP (UniProtKB | ChEBI)
Binding site318GTP (UniProtKB | ChEBI)
Active site330Proton acceptor; for GTP cyclohydrolase activity
Active site332Nucleophile; for GTP cyclohydrolase activity
Binding site353GTP (UniProtKB | ChEBI)
Binding site358GTP (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
      DBY37_09845

Organism names

  • Taxonomic identifier
  • Strain
    • CIM:MAG 900
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae

Accessions

  • Primary accession
    A0A316MMN3

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-201DHBP synthase
Region202-406GTP cyclohydrolase II
Domain209-374GTP 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
    406
  • Mass (Da)
    44,657
  • Last updated
    2018-10-10 v1
  • Checksum
    F29D9BFEC050F96F
MPICNTETAIEDLRSGKMIILVDDEDRENEGDLTIAAEFVTPEAINFMATYGRGLICLPMSSEMADRLNLPLMTKRNGSRFGTNFTVSIEAREGVTTGISAADRARTIQAAVADDAKAEDLVTPGHIFPLRAHPGGVLMRAGQTEGSVDLARLAGIKHAAVICEIMRDDGEMARMPDLEIFAEKHGLHIATIKDIIKYRMDRGQVAVRRVAEANMPTRYGDFRIYAYENSLDNQTHVALVKGNVADGEPVLTRVHSECLTGDAFGSLRCDCGDQLAAAMRQVEKEGRGLILYMRQEGRGIGLANKIKAYALQDEGLDTVEANIRLGFPPDLRDYGVGAQILVDLGAHRLRLLTNNPKKIIGLEGYGIEIVERVPIELEAGDYNEEYLLTKKEKMGHLLCCMHHHKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QAMY01000070
EMBL· GenBank· DDBJ
PWL59737.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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