A0A2N5JAG3 · A0A2N5JAG3_9BIFI

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 site51-52D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site52Mg2+ 1 (UniProtKB | ChEBI)
Binding site52Mg2+ 2 (UniProtKB | ChEBI)
Binding site56D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site149Essential for catalytic activity
Binding site163-167D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site166Mg2+ 2 (UniProtKB | ChEBI)
Site187Essential for catalytic activity
Binding site287-291GTP (UniProtKB | ChEBI)
Binding site292Zn2+ (UniProtKB | ChEBI); catalytic
Binding site303Zn2+ (UniProtKB | ChEBI); catalytic
Binding site305Zn2+ (UniProtKB | ChEBI); catalytic
Binding site308GTP (UniProtKB | ChEBI)
Binding site330-332GTP (UniProtKB | ChEBI)
Binding site352GTP (UniProtKB | ChEBI)
Active site364Proton acceptor
Active site366Nucleophile
Binding site387GTP (UniProtKB | ChEBI)
Binding site392GTP (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
      ribA
    • Synonyms
      ribB
    • ORF names
      Uis1B_0933

Organism names

  • Taxonomic identifier
  • Strain
    • 61
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A2N5JAG3

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-29Disordered
Compositional bias15-29Basic and acidic residues
Domain233-408GTP 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
    441
  • Mass (Da)
    48,662
  • Last updated
    2018-04-25 v1
  • Checksum
    235CEE4EC8765522
MNMSMNIMSGGPEDGAPAERREERHAGDPVERAIRDIAAGRIVVVADDESRENEGDLICAARFATPRNIAFMASEGRGLICTPMSAKLAERLELPAMCATNTDNHHTAFTVSIDHIATSTGISARDRSVTAMACVDPQTKPEDFRRPGHMFPLVARPGGVLERNGHTEATVDLARLAGLEPCGLCCEMMKRDGTMMRRDDLKAFAEEHELAYITIAQLQEYRRTHEFPRTVRRVARVSLPSEYGMFTMVGYESENGGEHVALVMGDDLLAAMDDEAPLPDSEPVLCRVHSQCLTGDVFGSRRCDCGPQLHEAMRRIAERGRGVLLYLSQEGRGIGLLNKLRTYELQEQGFDTLDANLRLGFPADLREYHTAAAILRDLGVHAIDLMTNNPDKIDQLRHAGITVASRVPIIIAANEFDANYLSTKQQRMGHLLGVPAKEERS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias15-29Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NMWU01000015
EMBL· GenBank· DDBJ
PLS31189.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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