A0A1F1QNT1 · A0A1F1QNT1_9LACO

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.

Type
IDPosition(s)Description
Binding site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site125Essential for catalytic activity
Binding site139-143D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site142Mg2+ 2 (UniProtKB | ChEBI)
Site163Essential for catalytic activity
Binding site244-248GTP (UniProtKB | ChEBI)
Binding site249Zn2+ (UniProtKB | ChEBI); catalytic
Binding site260Zn2+ (UniProtKB | ChEBI); catalytic
Binding site262Zn2+ (UniProtKB | ChEBI); catalytic
Binding site265GTP (UniProtKB | ChEBI)
Binding site287-289GTP (UniProtKB | ChEBI)
Binding site309GTP (UniProtKB | ChEBI)
Active site321Proton acceptor
Active site323Nucleophile
Binding site344GTP (UniProtKB | ChEBI)
Binding site349GTP (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 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
    Multifunctional fusion protein

Including 2 domains:

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

Gene names

    • Name
      ribB
    • Synonyms
      ribA
    • ORF names
      HMPREF3168_04605

Organism names

  • Taxonomic identifier
  • Strain
    • HMSC08B12
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus

Accessions

  • Primary accession
    A0A1F1QNT1

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain209-365GTP cyclohydrolase II

Sequence similarities

Belongs to the DHBP synthase family.
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
    392
  • Mass (Da)
    43,957
  • Last updated
    2017-02-15 v1
  • Checksum
    CCACFD4A971FFE0B
MDVKKIQDAIAWMKQGGLVIVADDEDREAEGDMIGLGSKVTPEKINFMTKHARGLLCTSIGREIAERLELPQMWQDNTDPFGTAFTVSVDYKTTTTGISAYDRATTIKALADPEAKPEDFFKPGHCFPLVAKDGGVLERNGHTEASVTLARLAGEAEVAYICEILKEDGHMARRPELEEIAKEYDLPYFTIAELQEYCRSFASSRSEFVKLPTDYGDFEIKDYGNGNLVIKKGEIAKNEPVMLRIHSKCLTGDVFGSKRCDCGHQLHQAMRRIEEKGSGLILYLNQEGRGIGLTNKLRAYALQDQGHDTYDANLLLGFAPDERKYDVAAKMIKDLGIKQVQLLTNNPDKIKQLEEAGVEITDRLPLEMAATAEDRRYLETKRDRFKHMLVSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LWNA01000082
EMBL· GenBank· DDBJ
OFS78269.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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