A0A6I4P1B3 · A0A6I4P1B3_9MICO

  • Protein
    GTP cyclohydrolase-2
  • Gene
    ribA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Type
IDPosition(s)Description
Binding site270-274GTP (UniProtKB | ChEBI)
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Binding site286Zn2+ (UniProtKB | ChEBI); catalytic
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Binding site291GTP (UniProtKB | ChEBI)
Binding site313-315GTP (UniProtKB | ChEBI)
Binding site335GTP (UniProtKB | ChEBI)
Active site347Proton acceptor
Active site349Nucleophile
Binding site370GTP (UniProtKB | ChEBI)
Binding site375GTP (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
      GB864_17485

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MMS17-SY077
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Agromyces

Accessions

  • Primary accession
    A0A6I4P1B3

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain230-391GTP cyclohydrolase II

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    45,733
  • Last updated
    2020-08-12 v1
  • MD5 Checksum
    D41823D46E4135926E0E26132EEF2010
MSLSSIPEALAALRAGKPIIVADDEGRENEGDAIMAAEFATRETIAWMVRHTSGYLCAPMPPELADRLDLPIMVERSQDARGTAYTVSVDAAQGVTTGISAADRAHTLRVLANPESVPADLIRPGHILPLRAVPGGVRERAGHTEAAVEFMRAAGLAPVGVIGELIDDDGEMMRLPRLIAFGEEENLPVTTIAALIDWLEQGGAEAAEASDAGLAAVGPRAETPRIGFEVETHLPTVHGTFRVRAYRDHVSGADHLAIIAGEPADGALVRLHSECLTGEAFGSLKCECGPQLQAALDTIANEGGVVVYLRGHEGRGIGLINKLRAYRLQEDGLDTLDANLALGLPADARDYTAAAEILADLGIGSVRLLTNNPEKLRQLERQGIRVDERVPLVVGVGSLNAGYLAAKRDRMGHQIDSLEDASPESILEGHAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WSTA01000126
EMBL· GenBank· DDBJ
MWC00337.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help