A0A7W7GN15 · A0A7W7GN15_9MICC

  • Protein
    GTP cyclohydrolase-2
  • Gene
    ribA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 )

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 site468-472GTP (UniProtKB | ChEBI)
Binding site473Zn2+ (UniProtKB | ChEBI); catalytic
Binding site484Zn2+ (UniProtKB | ChEBI); catalytic
Binding site486Zn2+ (UniProtKB | ChEBI); catalytic
Binding site489GTP (UniProtKB | ChEBI)
Binding site511-513GTP (UniProtKB | ChEBI)
Binding site533GTP (UniProtKB | ChEBI)
Active site545Proton acceptor
Active site547Nucleophile
Binding site568GTP (UniProtKB | ChEBI)
Binding site573GTP (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
    • ORF names
      HDA30_000666

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 23974
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Micrococcus

Accessions

  • Primary accession
    A0A7W7GN15

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain1-109Lumazine-binding
Repeat1-109Lumazine-binding
Domain110-211Lumazine-binding
Repeat110-211Lumazine-binding

Sequence similarities

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    617
  • Mass (Da)
    64,562
  • Last updated
    2021-06-02 v1
  • Checksum
    B364191667E1A242
MFTGIITHIGTVVALQQDEQSDTAVLVLDTAGAAAGLPEGGSLAVNGVCLTSVPQDADPSAPDSAPDDGLFRADLMGQTLRMTALGELSPGDRVNLERCLRPTDHIDGHIVQGHVDGVGTVAQVADEGAWRRVRVAVPDELARVIPAQGAITVQGVSLTVTAVSAPSQRRHWFEVGLIPATLEATVLGALAPGDRVNLETDVMARYAERMTQIPSSEPVRLDGVDRAVEQLAAGRPVIVVDDEDRENEGDIVFAAALATDEVTAFTIRHTSGVLCAPMPGAVADRLELPPMTATNQDPKGTAYTVSVDAAAGVTTGISAADRARTLRVLAGAQSAPADLTRPGHVFPLRAVDGGVAQRSGHTEAGVELCRLAGLPPVAAIAELTHDDGTMMRLPALRRFADDHALALISIEDLQAHLSGVDSTEDALLPTKHGQLRVSAHRDAATGVEHVLLRPVEPVGDSGAPDVVRVHSECLTGDAFGSLRCDCGPQLQHALEQTARTGGAVLYVRGHEGRGIGLAAKLRAYALQDAGRDTVDANLDLGLPADARDWAGAAAVLRAAGLERIRLVTNNPAKADGLREHGIDIVELLPAPAPVTEHNLAYLRTKRDRMGHTVPGLD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHNA010000001
EMBL· GenBank· DDBJ
MBB4735158.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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