A0A5C6BAP7 · A0A5C6BAP7_9PLAN

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.

Type
IDPosition(s)Description
Binding site257-261GTP (UniProtKB | ChEBI)
Binding site262Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273Zn2+ (UniProtKB | ChEBI); catalytic
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Binding site278GTP (UniProtKB | ChEBI)
Binding site300-302GTP (UniProtKB | ChEBI)
Binding site322GTP (UniProtKB | ChEBI)
Active site334Proton acceptor
Active site336Nucleophile
Binding site357GTP (UniProtKB | ChEBI)
Binding site362GTP (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
      ribBA_1
    • Synonyms
      ribA
    • ORF names
      CA54_43100

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CA54
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Symmachiella

Accessions

  • Primary accession
    A0A5C6BAP7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias77-91Polar residues
Region77-97Disordered
Domain213-379GTP 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
    422
  • Mass (Da)
    46,878
  • Last updated
    2019-11-13 v1
  • Checksum
    F11ED2B5EE8F41CE
MPTTHSKNIDDAITAIQEGRPVIVIDDADRENEGDFICAAESITPETVRLMLRYGMGLLCTPVSAAFAQRLNFSPMVDSRRSSTPMQTPFQIPVDHRSAGTGVSVENRLRTIRAIGDPNSRPDDFFGPGHIHPLVAKEGGVLRRAGHTEAAIDLMHLAGMQPAAALIEICSQETDGMSDHQELKQLAVQFDLPLLTIEELIRYRSEREQLIHREVDAHMPSRYGDLRVIAYRVEHEDQVPIAIVMGDLSSVDAPLVRMHSSCFTGDLLASLRCDCGDQLHMALDMIRREGVGAVVYLPQEGRGIGLIPKLKAYVLQDEGYDTVEANHKLGFKADPRDYGIGLQVLKDLDLRRVRLLTNNPKKTDAFAQRFDLEVVEQIPIVASPEKHRQHYLETKRTKMGHILPAAEIDPVQPASGQELAEN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias77-91Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SJPP01000002
EMBL· GenBank· DDBJ
TWU09070.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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