A0A2T0YHQ4 · A0A2T0YHQ4_9MICC

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

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

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, active site.

TypeIDPosition(s)Description
Binding site512-516GTP (UniProtKB | ChEBI)
Binding site517Zn2+ (UniProtKB | ChEBI); catalytic
Binding site528Zn2+ (UniProtKB | ChEBI); catalytic
Binding site530Zn2+ (UniProtKB | ChEBI); catalytic
Binding site533GTP (UniProtKB | ChEBI)
Binding site555-557GTP (UniProtKB | ChEBI)
Binding site577GTP (UniProtKB | ChEBI)
Active site591Nucleophile
Binding site612GTP (UniProtKB | ChEBI)
Binding site617GTP (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 Functionriboflavin synthase activity
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    GTP cyclohydrolase-2
  • EC number
  • Alternative names
    • GTP cyclohydrolase II

Gene names

    • Name
      ribA
    • ORF names
      BCL67_111101

Organism names

  • Taxonomic identifier
  • Strain
    • CG 35
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Nesterenkonia

Accessions

  • Primary accession
    A0A2T0YHQ4

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain1-98Lumazine-binding
Repeat1-98Lumazine-binding
Repeat99-198Lumazine-binding
Domain99-198Lumazine-binding

Sequence similarities

Belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    664
  • Mass (Da)
    70,407
  • Last updated
    2018-07-18 v1
  • Checksum
    153CD73E74B81ABE
MFTGIVTGLGEVLARRFDPAKGVERLSFSAPGHTAGLGLGGSIAVNGVCVSAVAIEDDQISVELIQETLSRTTLGQLQVGDPLNLERCLPSGARLDGHVVQGHVDGLAQLILADPQDGRHRFLISQDLAPYIAEKGSIAINGVSLTVSAVSAPGSSDPFFEVGLIPTTLADTTLGSTGIGAQVNVEVDVLAKYARRMLQFDQHLADADASVPDTAAERQPEAVPAIPQPETPAPVLDRIDVALNELAAGRPVIVVDDADRENEGDIIFPAAMATPELMALTIRYTSGVLCVPMTPERAEHLGLPPMVTENEDPKGTAYTISCDATSGVSTGISAADRAKTANVLADPASTAADLSRPGHLFPLIADPSGVLGRDGHTEAAVDLCRLAGLPEVGVIAELTHDDGRMMRLPALREFADEHQYALISIADLIVYRGGTPRPGTAMDAVAASWEAPHDEISKLVTPGPVVTLPTDHGVFAAQVWTEHATGHEHMLISALSQAPGEGRESADRPLIRMHSECVTGDVLGSRRCDCGTQLASALESIQRDGGHLLYLRGHEGRGIGLANKMRAYKLQEQGADTVEANEMLGLAAELRDFSGAAAILYASGIRKLMLMTNNPLKVQTLRDAGLDVELVPSTGVVHETNRRYLETKRDRMNHTLDHLQLHEQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PVTY01000011
EMBL· GenBank· DDBJ
PRZ14614.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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