K7RV09 · K7RV09_ACIA4

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 )

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.

Type
IDPosition(s)Description
Binding site263-267GTP (UniProtKB | ChEBI)
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site279Zn2+ (UniProtKB | ChEBI); catalytic
Binding site281Zn2+ (UniProtKB | ChEBI); catalytic
Binding site284GTP (UniProtKB | ChEBI)
Binding site306-308GTP (UniProtKB | ChEBI)
Binding site328GTP (UniProtKB | ChEBI)
Active site340Proton acceptor
Active site342Nucleophile
Binding site363GTP (UniProtKB | ChEBI)
Binding site368GTP (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 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
      ribB
    • Synonyms
      ribA
    • Ordered locus names
      PACID_24650

Organism names

Accessions

  • Primary accession
    K7RV09

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain219-380GTP cyclohydrolase II

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    435
  • Mass (Da)
    45,856
  • Last updated
    2013-02-06 v1
  • Checksum
    2F793D4135BEC403
MTGFATIEEALVQVRAGRPVLVLDDQTRENEGDAILAAGAAGTEWVGWMVRHTSGYLCAPMTEERADRLGLPLMWPSSQDPLRTRYTVSVDAAQGTTTGISAAERAITARTLAGPDARPGDLTRPGHILPLRARDGGVLERRGHTEAAVDLARLAGLEPVGLIGEIVDDAGACLRTPEVLALGAEEGLCVITIEQLAAWRRAHDDLRTASGTRVTAGEEAVLPTRHGAFRVTGYHDHLTGAEHVLLVPSAGIAADDGGAPWVRVHSECLTGDALGSLRCDCGEQLSRSMDQVAGHGGAVIMLRGHEGRGVGLINKIDAYHAQDGGLDTVDAQTSLGLPVDAREYGAAVAILTGLGVDSVRLLTNNPAKISALRQGGIEVEPRPLRIPPRPEDIAYLRTKRDRMGHLIDLDETGSLDARDTTAGISTAGDDEEGIA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003493
EMBL· GenBank· DDBJ
AFV90241.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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