A0A7C1KKB7 · A0A7C1KKB7_9BACT

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 )

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 site26-27D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site27Mg2+ 1 (UniProtKB | ChEBI)
Binding site27Mg2+ 2 (UniProtKB | ChEBI)
Binding site31D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site125Essential for DHBP synthase activity
Binding site139-143D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site142Mg2+ 2 (UniProtKB | ChEBI)
Binding site163D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site163Essential for DHBP synthase activity
Binding site260-264GTP (UniProtKB | ChEBI)
Binding site265Zn2+ (UniProtKB | ChEBI); catalytic
Binding site276Zn2+ (UniProtKB | ChEBI); catalytic
Binding site278Zn2+ (UniProtKB | ChEBI); catalytic
Binding site281GTP (UniProtKB | ChEBI)
Binding site303-305GTP (UniProtKB | ChEBI)
Binding site325GTP (UniProtKB | ChEBI)
Active site337Proton acceptor; for GTP cyclohydrolase activity
Active site339Nucleophile; for GTP cyclohydrolase activity
Binding site360GTP (UniProtKB | ChEBI)
Binding site365GTP (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
    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
      ENH85_02715

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HyVt-343
  • Taxonomic lineage
    Bacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Scalinduaceae > Candidatus Scalindua

Accessions

  • Primary accession
    A0A7C1KKB7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-200DHBP synthase
Region201-408GTP cyclohydrolase II
Domain208-381GTP 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    408
  • Mass (Da)
    45,278
  • Last updated
    2020-12-02 v1
  • Checksum
    6503F368BB6DC74C
MLNTISEVVEDLKQGKMIIVIDDASRENEGDITIAAEKITPEAINFMLLHARGIICLTITEERAQELGLTPMVTNNTSNYQTPFTVTIDAKKGITTGVSAKDRTKTILTAISEDCTPHDLDRPGHVFPLTSQKGGVLVRAGHTEGAVDLARLAGLKPAAVICEVMNEDGSMSKLPDLRKLAEKHNIKICTIADIIKYRREKERLIEKRVSVNLPTIYGKFVLHLYRSFIDEYLHLALCLGNIGSLDKSPAPIQKEPILVRVHDECLTGDIFGSLRCDCGGQLHNALKMIQREDKGVLLYMRQEGRGIGLENKLHAYALQENGLDTVEANKKLGLVVDTREYGIGAQILKDLGISKMRLLSNNPKKFTALAGYGLEIVERVPIVITPKEENRRYLRTKREKLGHILEGV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DRGJ01000059
EMBL· GenBank· DDBJ
HDY66685.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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