A0A533QMI7 · A0A533QMI7_9BACT

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Type
IDPosition(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 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 site261-265GTP (UniProtKB | ChEBI)
Binding site266Zn2+ (UniProtKB | ChEBI); catalytic
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Binding site279Zn2+ (UniProtKB | ChEBI); catalytic
Binding site282GTP (UniProtKB | ChEBI)
Binding site304-306GTP (UniProtKB | ChEBI)
Binding site326GTP (UniProtKB | ChEBI)
Active site338Proton acceptor; for GTP cyclohydrolase activity
Active site340Nucleophile; for GTP cyclohydrolase activity
Binding site361GTP (UniProtKB | ChEBI)
Binding site366GTP (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
      JETT_1945

Organism names

  • Taxonomic identifier
  • Strain
    • J2
  • Taxonomic lineage
    Bacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Jettenia

Accessions

  • Primary accession
    A0A533QMI7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-201DHBP synthase
Region202-409GTP cyclohydrolase II
Domain209-381GTP 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
    409
  • Mass (Da)
    45,893
  • Last updated
    2019-10-16 v1
  • Checksum
    3A8F6BA1615AC16A
MRFNTIQEAVEDLKQGKMVILIDDENRENEGDIIIAAEKITPEVVNFMLMHARGIVCIAIDAERAEKLNLYPMVSNNTSNFQTPFTVSVDARENITTGVSSKDRATTVLTILDDKTTPEDLVRPGHMFPLKAQKGGVLVRTGHTEGAVDLTRIAGLKQAAVICEIMTEDGNMAKLPELRKFAEKYHLKICTIADIIKYRHEQERLIEKRVTVKLPTIYGNFTLHLYRSFVDEYLHLALCLGVGKESGTSPSPLHTEPVLVRVHDECLTGDIFGSLRCDCGEQLHNTLRMIQENGKGVLLYMRQEGRGIGLENKLHSYLLQENGLDTVEANEKLGFPADKRDYGIGAQILRDLGITKMKLLTNNPKKFAALAGYGLEIVERISIATEPKEENKHYLRTKKEKLGHMIEIV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SULG01000036
EMBL· GenBank· DDBJ
TLD41790.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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