A0A0J1G8J6 · A0A0J1G8J6_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 site29-30D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site30Mg2+ 2 (UniProtKB | ChEBI)
Binding site30Mg2+ 1 (UniProtKB | ChEBI)
Binding site34D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site127Essential for DHBP synthase activity
Binding site141-145D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site144Mg2+ 2 (UniProtKB | ChEBI)
Binding site165D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site165Essential 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
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
      RHS_2419

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RHS
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Lachnospirales > Lachnospiraceae > Robinsoniella

Accessions

  • Primary accession
    A0A0J1G8J6

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-202DHBP synthase
Region203-404GTP cyclohydrolase II
Domain212-374GTP 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
    404
  • Mass (Da)
    45,517
  • Last updated
    2015-10-14 v1
  • Checksum
    63DB2FB73FA01D3A
MEMKFDSVKEAVSTLQAGKMILVLDDWDRENEGDLICAAEYATTENVNFMASCAKGLICMPMSRKLAEKLCLPPMTETNNDNHGTAFTVSIDYKETTTGISAVERGMTARMCVSDGVLAEDFRRPGHMFPLIAKDNGVLERNGHTEATVDLMRLAELKECGLCCEIMNDDGSMMRSHDLLKFAEQYQIPCITIKDLQEYRKITEKLAECVSITKMPTRYGDFMAHCYVNKLNQEHHIALVMGNIADEKEVLCRVHSECLTGDVFGSLRCDCGQQLDAAMKMIADHGKGVLLYMRQEGRGIGLVNKLKAYHLQDGGMDTLDANLALGFQGDLREYYIGAQILRDLGIQSLRLLTNNPDKVYQLEDYGIEITKRMPIQIKATPYDKFYLKTKQTRMGHLLNLEEEK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JNGB01000020
EMBL· GenBank· DDBJ
KLU71705.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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