R7WKE6 · R7WKE6_9NOCA

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 )

Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
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, site, active site.

TypeIDPosition(s)Description
Binding site48-49D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site49Mg2+ 1 (UniProtKB | ChEBI)
Binding site49Mg2+ 2 (UniProtKB | ChEBI)
Binding site53D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site147Essential for DHBP synthase activity
Binding site161-165D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site164Mg2+ 2 (UniProtKB | ChEBI)
Binding site185D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site185Essential for DHBP synthase activity
Binding site279-283GTP (UniProtKB | ChEBI)
Binding site284Zn2+ (UniProtKB | ChEBI); catalytic
Binding site295Zn2+ (UniProtKB | ChEBI); catalytic
Binding site297Zn2+ (UniProtKB | ChEBI); catalytic
Binding site300GTP (UniProtKB | ChEBI)
Binding site323-325GTP (UniProtKB | ChEBI)
Binding site345GTP (UniProtKB | ChEBI)
Active site357Proton acceptor; for GTP cyclohydrolase activity
Active site359Nucleophile; for GTP cyclohydrolase activity
Binding site380GTP (UniProtKB | ChEBI)
Binding site385GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP binding
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin biosynthesis protein RibBA

Including 2 domains:

  • Recommended name
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • EC number
  • Short names
    DHBP synthase
  • Recommended name
    GTP cyclohydrolase-2
  • EC number
  • Alternative names
    • GTP cyclohydrolase II

Gene names

    • Name
      ribBA
    • ORF names
      Rrhod_2859

Organism names

  • Taxonomic identifier
  • Strain
    • LMG 5362
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus

Accessions

  • Primary accession
    R7WKE6

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-224DHBP synthase
Region225-452GTP cyclohydrolase II
Domain231-400GTP cyclohydrolase II

Sequence similarities

In the C-terminal section; 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
    452
  • Mass (Da)
    48,772
  • Last updated
    2013-07-24 v1
  • Checksum
    EEF0B7B219E20969
MLTRTPGDDSEWRNDPSGVEVTRFDSIERAVADIAAGKAVVVVDDEDRENEGDLIFAAEKATPELVAFMVRYTSGYLCVPMTGADCDRLGLPPMYATNQDKHGTAYTVTVDAKDGIGTGISASDRATTMRKLADETTGAADFTRPGHVVPLRAKEGGVLRRPGHTEAAVDLARMADLRPAGVICEIVSQKDEGEMARTDELRVFADDHDLALISIADLIAWRRKHEKQVVRVASARIPTRHGEFTAVGYKSLYDDVEHVALVRGDVAGPDGDGADVLVRVHSECLTGDVFGSLRCDCGPQLDAALDMVAQEGRGIVLYMRGHEGRGIGLLHKLQAYQLQDAGVDTVDANLQLGLPADARDYGTGAQILVDLGVTSMRLLTNNPAKRVGLDGYGLEIVDRVAMPLRANSENLTYLRTKRDRMGHDLVGLDEFEVDTPAEPGDYFQASGQGDAP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
APMY01000082
EMBL· GenBank· DDBJ
EOM75786.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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