P43525 · RIBA_AZOBR

Function

function

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

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 site240-244GTP (UniProtKB | ChEBI)
Binding site245Zn2+ (UniProtKB | ChEBI); catalytic
Binding site256Zn2+ (UniProtKB | ChEBI); catalytic
Binding site258Zn2+ (UniProtKB | ChEBI); catalytic
Binding site261GTP (UniProtKB | ChEBI)
Binding site283-285GTP (UniProtKB | ChEBI)
Binding site305GTP (UniProtKB | ChEBI)
Active site317Proton acceptor
Active site319Nucleophile
Binding site340GTP (UniProtKB | ChEBI)
Binding site345GTP (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
      ribA

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 29145 / DSM 1690 / IMET 11303 / Sp7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Azospirillaceae > Azospirillum

Accessions

  • Primary accession
    P43525

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001517841-385GTP cyclohydrolase-2

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-189DHBP synthase-like
Region190-385GTP cyclohydrolase II

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    385
  • Mass (Da)
    40,972
  • Last updated
    1995-11-01 v1
  • MD5 Checksum
    A09CE1A4E2909F3BB90D982AFC36A144
MYADAPSDSAPPEAVLPMDEAAMRAVDRATAALRRGEAVAIETADGSVGAAVSVESVAIDAVQRLVQLTGAAPVLAVTRRRATVLKLMGEGTGVVALSLPRCLTADEAHALADPEHRPDGDMPDGLTATAMDPGSRETAAVDLARLARLLPAAIVAPATDHTGSAAEWAAEHDLLLVRARDIADYRVHVVRTLRRVAEARVPLSGAENTSIAAFRPIDGGPEHLAIIVGNPVAGEPVLARLHSECFTGDLLAGLRCDCGQQLRGAIAEIARHGSGVLLYLAQEGRGIGLVNKLRAYRIQDRGFDTVDANEILGFEADERVYLPAAEMLRQLGFTAVRLMTNNPEKLRQLARCGIEVVERVPHIFPANGHNEGYLRTKAERSGHMF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U09869
EMBL· GenBank· DDBJ
AAA82170.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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