A0AA96UKF1 · A0AA96UKF1_9BACI

  • 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.

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 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 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
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

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
      RUI02_11575

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • TSA-4
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    A0AA96UKF1

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-199DHBP synthase
Region200-398GTP cyclohydrolase II
Domain206-372GTP 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    44,135
  • Last updated
    2024-03-27 v1
  • Checksum
    D7183417DB4D0BA1
MFHPIEEALDALKKGEVIIVVDDEDRENEGDFVALAEHATPEVINFMATHGRGLICTPLSEEIADRLDLHPMVEHNTDSHHTAFTVSIDHRETKTGISAQERSFTVQALLDSKSVPSDFQRPGHIFPLIAKKGGVLKRAGHTEAAVDLAEACGSPGAGVICEIMNEDGTMARVPELIEIAKKHQLKMITIKDLIQYRYNLTTLVEREVDITLPTDFGTFKVYGYTNEVDGKEHVAFVMGEVPFGEEPVLVRVHSECLTGDVFGSHRCDCGPQLHAALNQIAAEGRGVLLYLRQEGRGIGLINKLKAYKLQEQGYDTVEANEALGFLPDLRNYGIGAQILRDLGVRNMKLLTNNPRKIAGLEGYGLSISERVPLQMEAKEHNKKYLQTKMNKLGHLLHF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP136099
EMBL· GenBank· DDBJ
WNW98425.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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