A0A414KRN7 · A0A414KRN7_BACSE

  • 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 site30-31D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site31Mg2+ 2 (UniProtKB | ChEBI)
Binding site31Mg2+ 1 (UniProtKB | ChEBI)
Binding site35D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site129Essential for DHBP synthase activity
Binding site143-147D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site146Mg2+ 2 (UniProtKB | ChEBI)
Binding site167D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site167Essential for DHBP synthase activity
Binding site255-259GTP (UniProtKB | ChEBI)
Binding site260Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273Zn2+ (UniProtKB | ChEBI); catalytic
Binding site276GTP (UniProtKB | ChEBI)
Binding site298-300GTP (UniProtKB | ChEBI)
Binding site320GTP (UniProtKB | ChEBI)
Active site332Proton acceptor; for GTP cyclohydrolase activity
Active site334Nucleophile; for GTP cyclohydrolase activity
Binding site355GTP (UniProtKB | ChEBI)
Binding site360GTP (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
      F9962_17425

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BIOML-A17
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A414KRN7

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-204DHBP synthase
Region205-404GTP cyclohydrolase II
Domain212-376GTP 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)
    44,935
  • Last updated
    2019-05-08 v1
  • Checksum
    320458724927CA73
MEKVKLNTIEEAIEDFKAGNFVIVVDDEDRENEGDLIIAAEKITSEKVNFMLKHARGVLCAPITVSRCKELDLPHQVTDNTSVLGTPFTVTVDKLEGCTTGVSAADRAATIQALADPLSTPATFGRPGHINPLYAQEKGVLRRAGHTEATIDMCRLSGFYPAGALMEIMNEDGTMARLPELRKMADEFNLKLISIRDMIAYRLQQESIVEKGVEVDMPTEHGHFRLIPFRQKSNGLEHVALFKGTWAPDEPVLVRVHSSCATGDIFGSMRCDCGEQLHKAMEVIEKAGKGVVVYLNQEGRGIGLMEKMRAYKLQEDGMDTVDANICLGHLADERDYGVGAQILRELGVHKMRLLTNNPVKRVGLEAYGLEIVENVPVETTPNQYNERYLRTKKERMGHTLHFSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WCLP01000072
EMBL· GenBank· DDBJ
KAB5278897.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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