A0A133SK80 · A0A133SK80_9FIRM

  • 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.

TypeIDPosition(s)Description
Binding site44-45D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site45Mg2+ 1 (UniProtKB | ChEBI)
Binding site45Mg2+ 2 (UniProtKB | ChEBI)
Binding site49D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site142Essential for DHBP synthase activity
Binding site156-160D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site159Mg2+ 2 (UniProtKB | ChEBI)
Binding site180D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site180Essential for DHBP synthase activity
Binding site268-272GTP (UniProtKB | ChEBI)
Binding site273Zn2+ (UniProtKB | ChEBI); catalytic
Binding site284Zn2+ (UniProtKB | ChEBI); catalytic
Binding site286Zn2+ (UniProtKB | ChEBI); catalytic
Binding site289GTP (UniProtKB | ChEBI)
Binding site311-313GTP (UniProtKB | ChEBI)
Binding site333GTP (UniProtKB | ChEBI)
Active site345Proton acceptor; for GTP cyclohydrolase activity
Active site347Nucleophile; for GTP cyclohydrolase activity
Binding site368GTP (UniProtKB | ChEBI)
Binding site373GTP (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

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
      HMPREF3201_00369

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MJR9396C
  • Taxonomic lineage
    Bacteria > Bacillota > Negativicutes > Veillonellales > Veillonellaceae > Megasphaera

Accessions

  • Primary accession
    A0A133SK80

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-217DHBP synthase
Region218-417GTP cyclohydrolase II
Domain226-389GTP 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
    417
  • Mass (Da)
    46,939
  • Last updated
    2016-06-08 v1
  • Checksum
    31A4D33C4E23B634
MAQGFSYKEVFILTTEKRKFNTIEEAIEELQAGHIVIVTDDPDRENEGDFICAAQYCTTENMNFMASHGKGLICMPMSIEYAHKLGLPPMVSENTDNHETAFTVSIDHVDTTTGISAVERALTARKCAEESARPEDFRRPGHNFPLIAKRGGVLTRNGHTEATVDLMRLAGLKQVGLCCEIMADDGTMMRTPSLWEIADKYNLKFITIHDLQNYCRRHDKHVIREAVAKMPTKYGEFKIYGYINDLTGEHHVALIKGDIGDGKNLLCRVHSECLTGDVFGSCRCDCGEQLAAALSQINAEGRGILLYMRQEGRGIGLINKLKAYVLQEQGYDTVEANEKLGFAPDLREYWIGAQMLQDMGAKEIRLLTNNPEKIYGLEGFGVEIVERVPIEMEPQKFDEFYLETKKNKMGHILPHLH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LRVC01000011
EMBL· GenBank· DDBJ
KXA70097.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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