A0A7G7G0P8 · A0A7G7G0P8_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 site250-254GTP (UniProtKB | ChEBI)
Binding site255Zn2+ (UniProtKB | ChEBI); catalytic
Binding site266Zn2+ (UniProtKB | ChEBI); catalytic
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271GTP (UniProtKB | ChEBI)
Binding site293-295GTP (UniProtKB | ChEBI)
Binding site315GTP (UniProtKB | ChEBI)
Active site327Proton acceptor; for GTP cyclohydrolase activity
Active site329Nucleophile; for GTP cyclohydrolase activity
Binding site350GTP (UniProtKB | ChEBI)
Binding site355GTP (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
      HUW50_26610

Organism names

Accessions

  • Primary accession
    A0A7G7G0P8

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-199DHBP synthase
Region200-397GTP cyclohydrolase II
Domain206-371GTP 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
    397
  • Mass (Da)
    44,277
  • Last updated
    2021-02-10 v1
  • Checksum
    BB832A1B90443304
MFHKIEDAIHDLKEGKVIIVVDDEDRENEGDFVSLADRVTPETINFMIKHGRGLVCVPITEQQAKRLELTPMVNQNTDPHGTAFTVSVDYKSNKTGISAFERADTVKALLADDTNPSDFKRPGHTFPLVAKEGGVLRRAGHTEAAVDLSILCGAKPGGVICEIIKEDGTMARVPDLLIIAEQLDLKIITIKDLIQYRNRSEKLVKREIEIDLPTEYGSFKAIGYSNSLDDKEHVALVKGEIDTTVPTLVRVHSECLTGDVFSSYRCDCGPQLHAALAQIEKEGKGVLLYMRQEGRGIGLLNKMRAYKLQEQGYDTVAANEKLGFAPDLRDYGIGAQILKDLGIEKMNLLTNNPRKIAGLEGYDLTVVDRVPIEMPAREENEQYLRTKYEKLGHYLHF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP055263
EMBL· GenBank· DDBJ
QNF30732.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp