A0A7C6QNT1 · A0A7C6QNT1_9FIRM

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+ 1 (UniProtKB | ChEBI)
Binding site31Mg2+ 2 (UniProtKB | ChEBI)
Binding site35D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site128Essential for DHBP synthase activity
Binding site142-146D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site145Mg2+ 2 (UniProtKB | ChEBI)
Binding site166D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site166Essential for DHBP synthase activity
Binding site254-258GTP (UniProtKB | ChEBI)
Binding site259Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site272Zn2+ (UniProtKB | ChEBI); catalytic
Binding site275GTP (UniProtKB | ChEBI)
Binding site297-299GTP (UniProtKB | ChEBI)
Binding site319GTP (UniProtKB | ChEBI)
Active site331Proton acceptor; for GTP cyclohydrolase activity
Active site333Nucleophile; for GTP cyclohydrolase activity
Binding site354GTP (UniProtKB | ChEBI)
Binding site359GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
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
      GXX21_05870

Organism names

Accessions

  • Primary accession
    A0A7C6QNT1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-203DHBP synthase
Region204-403GTP cyclohydrolase II
Domain210-375GTP 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
    403
  • Mass (Da)
    44,514
  • Last updated
    2020-12-02 v1
  • Checksum
    3544C3F5AEBCF600
MAKESFDTIEEAIAEIAAGRMVIVVDDEDRENEGDLILAAEKVTPEAINFMAVHARGLICAPMTGERLDELELHQMVANNTDSMETAFTVSVDAVTTTTGISAFERAETIRALVDPKTAPSDLRRPGHVFPLRAVEGGVLRRAGHTEASVDLARLAGLYPAGVCCEIMNEDGTMARVPQLLEFAEKHNLKIITIADLIEYRRHTEKLVRRVSEAHLPTKYGDFTAVAYENLLDHTCNIALVKGDVSNGEPVLTRVHSECLTGDVFGSHRCDCGEQLAQALRMISAEGRGILLYMRQEGRGIGLLNKIRAYKLQDEGKDTVEANELLGFPPDLRDYGIGAQILVDLGVKKLRLMTNNPRKIKGLQGYGLEVVERVPIEMPARAENKRYLQTKKEKMGHFLALNK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DULM01000125
EMBL· GenBank· DDBJ
HHW29059.1
EMBL· GenBank· DDBJ
Genomic DNA

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