A0A2W1BB03 · A0A2W1BB03_UNCCH

  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site27-28D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site28Mg2+ 1 (UniProtKB | ChEBI)
Binding site28Mg2+ 2 (UniProtKB | ChEBI)
Binding site32D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site126Essential for DHBP synthase activity
Binding site164D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site164Essential for DHBP synthase activity
Binding site252-256GTP (UniProtKB | ChEBI)
Binding site257Zn2+ (UniProtKB | ChEBI); catalytic
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273GTP (UniProtKB | ChEBI)
Binding site295-297GTP (UniProtKB | ChEBI)
Binding site317GTP (UniProtKB | ChEBI)
Active site329Proton acceptor; for GTP cyclohydrolase activity
Active site331Nucleophile; for GTP cyclohydrolase activity
Binding site352GTP (UniProtKB | ChEBI)
Binding site357GTP (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
      DK304_001149

Organism names

Accessions

  • Primary accession
    A0A2W1BB03

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-201DHBP synthase
Region202-414GTP cyclohydrolase II
Domain208-373GTP 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
    414
  • Mass (Da)
    45,216
  • Last updated
    2018-09-12 v1
  • Checksum
    B0665245E88B0FCA
MPFCTVEEAVEDIRAGKFVIIVDDEDRENEGDLSIAAEFADAESISFMANHGRGLICMPMTGKRLDQLEIGLMVGDNTARLSTAFTVSIDAINGTTTGISATDRAETIRALIDPETKPADLARPGHLFPLRYAEGGVLVRAGQTEGIVDLVKIAGLYPSGVICEVMNEDGTMARLNDLEKLTAAHGIRIISIAQIVAYRKANETLVKRVAETKLPTQYGEFKAVAYASIIDSDEHVVLVKGDISTNDPVLVRVHSQCLTGDTFGSQRCDCGEQIHRSLEAIQAEGRGVFLYMRQEGRGIGLHNKLRAYQLQDAGLDTVEANEKLGFPADLRWYGIGAQILVDLGIKRIRLLTNNPKKVVGLDGYGLEIMERVPIQIPANKTNRAYLNTKLTKLGHLLDSDLLEIDSQETVSPEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QGNO01000015
EMBL· GenBank· DDBJ
PZC49831.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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