A0A0Z4H2C8 · A0A0Z4H2C8_STAAU

  • 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 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 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 site249-253GTP (UniProtKB | ChEBI)
Binding site254Zn2+ (UniProtKB | ChEBI); catalytic
Binding site265Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270GTP (UniProtKB | ChEBI)
Binding site291-293GTP (UniProtKB | ChEBI)
Binding site313GTP (UniProtKB | ChEBI)
Active site325Proton acceptor; for GTP cyclohydrolase activity
Active site327Nucleophile; for GTP cyclohydrolase activity
Binding site348GTP (UniProtKB | ChEBI)
Binding site353GTP (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
    • Synonyms
      ribA
    • ORF names
      C0102_13685
      , GQX37_04670
      , NCTC13131_06069
      , SAMEA1029536_02857
      , SAMEA2078260_02811
      , SAMEA2078588_02831
      , SAMEA2080344_02807
      , SAMEA2081063_02334
      , SAMEA4008575_02837
      , SAMEA70146418_02294

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • SAUR390
    • UE1097
    • MOS105
    • NCTC13131
    • S021_N01_C01
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A0Z4H2C8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-200DHBP synthase
Region201-393GTP cyclohydrolase II
Domain209-368GTP 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
    393
  • Mass (Da)
    44,159
  • Last updated
    2016-04-13 v1
  • Checksum
    BBEE8FCCC3D1FAD8
MQFDNIDSALMALKNGEPIIVVDDENRENEGDLVAVTEWMNDNTINFMAKEARGLICAPVSKDIAQRLDLVQMVDDNSDIFGTQFTVSIDHVDTTTGISAYERTLTAKNLIDPSSEAKDFNRPGHLFPLVAQDKGVLARNGHTEAAVDLAKLTGAKPAGVICEIMNDDGTMAKGQDLQKFKEKHQLKMITIDDLIEYRKKLEPEIEFKAKVKMPTDFGTFDMYGFKATYTDEEIVVLTKGAIRQHENVRLHSACLTGDIFHSQRCDCGAQLESSMKYINEHGGMIIYLPQEGRGIGLLNKLRAYELIEQGYDTVTANLALGFDEDLRDYHIAAQILKYFNIEHINLLSNNPSKFEGLKLYGIDIAERIEVIVPETVHNHDYMETKKIKMGHLI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CACTPG010000034
EMBL· GenBank· DDBJ
CAA4185478.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTQT010000028
EMBL· GenBank· DDBJ
CAA4402179.1
EMBL· GenBank· DDBJ
Genomic DNA
CACTWD010000016
EMBL· GenBank· DDBJ
CAA4700252.1
EMBL· GenBank· DDBJ
Genomic DNA
CACUNS010000029
EMBL· GenBank· DDBJ
CAA6134882.1
EMBL· GenBank· DDBJ
Genomic DNA
CACURZ010000028
EMBL· GenBank· DDBJ
CAA6396718.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIGXB010000018
EMBL· GenBank· DDBJ
CAC5811922.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIIGD010000009
EMBL· GenBank· DDBJ
CAC8228977.1
EMBL· GenBank· DDBJ
Genomic DNA
UAUZ02000004
EMBL· GenBank· DDBJ
CAD7355051.1
EMBL· GenBank· DDBJ
Genomic DNA
JAANEC010000046
EMBL· GenBank· DDBJ
NUY11845.1
EMBL· GenBank· DDBJ
Genomic DNA
PKSU01000014
EMBL· GenBank· DDBJ
PZL78673.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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