A0A6B8VKQ8 · A0A6B8VKQ8_9CORY

  • 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.

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.
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 site38-39D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site39Mg2+ 1 (UniProtKB | ChEBI)
Binding site39Mg2+ 2 (UniProtKB | ChEBI)
Binding site43D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site136Essential for DHBP synthase activity
Binding site150-154D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site153Mg2+ 2 (UniProtKB | ChEBI)
Binding site174D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site174Essential for DHBP synthase activity
Binding site264-268GTP (UniProtKB | ChEBI)
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site280Zn2+ (UniProtKB | ChEBI); catalytic
Binding site282Zn2+ (UniProtKB | ChEBI); catalytic
Binding site285GTP (UniProtKB | ChEBI)
Binding site308-310GTP (UniProtKB | ChEBI)
Binding site330GTP (UniProtKB | ChEBI)
Active site342Proton acceptor; for GTP cyclohydrolase activity
Active site344Nucleophile; for GTP cyclohydrolase activity
Binding site365GTP (UniProtKB | ChEBI)
Binding site370GTP (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
      CETAM_07060

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2019
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium

Accessions

  • Primary accession
    A0A6B8VKQ8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-213DHBP synthase
Region214-425GTP cyclohydrolase II
Domain220-385GTP 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
    425
  • Mass (Da)
    46,286
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    CBC50F273BE5483051733AC216917980
MSDESVDLNGRLRLDTVERAIADIAAGKAVVVVDDEDRENEGDLIFAAELATPELVAFMVRYSSGYICAALTNEDCDRLGLPPMVARNEDARHTAYTVTVDAATGSTGISAASRAETIQRLASPTTNRRDLTRPGHVVPLRAVAGGVLARDGHTEASIDLAVLAGLRPAGVLCEIVSEEDPTDMARGPELRRFADEHDLALISIEQLIEHRRRTETQVERLVETNLPTEFGEFRVVGYRHQIDGTEFVALVAGDVTGEEAVLVRVHSECLTGDVFASRRCDCGPQLHESMRMVQEAGRGVIIYLRGHEGRGIGLMSKLEAYRLQDLGLDTVDANLEQGLPADAREYSAAGQILRELGVPSASLMTNNPTKCAALEGYGVEIVGRTSVPVEPNEDNIRYLRTKRDRMGHDLPAVARWEAEHEGTVK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP046453
EMBL· GenBank· DDBJ
QGU04673.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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