A0A2X4PI40 · A0A2X4PI40_9PORP

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 site33-34D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site34Mg2+ 1 (UniProtKB | ChEBI)
Binding site34Mg2+ 2 (UniProtKB | ChEBI)
Binding site38D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site133Essential for DHBP synthase activity
Binding site147-151D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site150Mg2+ 2 (UniProtKB | ChEBI)
Binding site171D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site171Essential for DHBP synthase activity
Binding site259-263GTP (UniProtKB | ChEBI)
Binding site264Zn2+ (UniProtKB | ChEBI); catalytic
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Binding site280GTP (UniProtKB | ChEBI)
Binding site302-304GTP (UniProtKB | ChEBI)
Binding site324GTP (UniProtKB | ChEBI)
Active site336Proton acceptor; for GTP cyclohydrolase activity
Active site338Nucleophile; for GTP cyclohydrolase activity
Binding site359GTP (UniProtKB | ChEBI)
Binding site364GTP (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
      NCTC12858_01459

Organism names

  • Taxonomic identifier
  • Strain
    • NCTC12858
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Porphyromonadaceae > Porphyromonas

Accessions

  • Primary accession
    A0A2X4PI40

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-208DHBP synthase
Region209-408GTP cyclohydrolase II
Domain215-380GTP 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
    408
  • Mass (Da)
    45,663
  • Last updated
    2018-09-12 v1
  • Checksum
    A406D2DC17B3C16C
MDTVDTFKLNTIEEALEDFKQGKFLIVVDDEDRENEGDFIIAAEKVTPEKINFMMRYGRGVLCAPISEERAAQLELEMQVPNNTSVHETPFTITVDRLGNGCTTGVSMYDRAQTILALADPKTLPTDLGRPGHICPLRARSRGVLRRAGHTEAAVDLTKLCGMQPAAALIEIINEDGTMARMPQLIEASEKWGIKIITIKDLIAYRLKRDCIIERGVEVKMPTQYGDFRLIPYRQKSNGQEHIALFKGDISGSTPLLVRMHSSCSTGDIFASKRCDCGEQLHKAMEIIEAEGRGLIVYLNQEGRGIGLMDKMRAYRLQEEGMDTVEANLHIGHDADERDYGVGAQILRDLGVSKMRLMTNNPVKRVGLEAYGLEISEVVPLEVTPNAYNKKYLETKRDRMGHSLHKLK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LS483447
EMBL· GenBank· DDBJ
SQH73596.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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