A0A410W8P1 · A0A410W8P1_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.
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 site35-36D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site36Mg2+ 1 (UniProtKB | ChEBI)
Binding site36Mg2+ 2 (UniProtKB | ChEBI)
Binding site40D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site133Essential for DHBP synthase activity
Binding site147-151D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site150Mg2+ 2 (UniProtKB | ChEBI)
Binding site171D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site171Essential for DHBP synthase activity
Binding site270-274GTP (UniProtKB | ChEBI)
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Binding site286Zn2+ (UniProtKB | ChEBI); catalytic
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Binding site291GTP (UniProtKB | ChEBI)
Binding site314-316GTP (UniProtKB | ChEBI)
Binding site336GTP (UniProtKB | ChEBI)
Active site348Proton acceptor; for GTP cyclohydrolase activity
Active site350Nucleophile; for GTP cyclohydrolase activity
Binding site371GTP (UniProtKB | ChEBI)
Binding site376GTP (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
      CPELA_05220

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 136/3
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium

Accessions

  • Primary accession
    A0A410W8P1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-210DHBP synthase
Region211-427GTP 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
    427
  • Mass (Da)
    46,568
  • Last updated
    2019-05-08 v1
  • Checksum
    3CCF7F12A363E629
MTQAEHDSIQLDSVDDAIQAIAQGEAVVVVDNVDRENEGDLIFAAECATPELVSFMVRYSSGYICAALEGAHLDRLALPPMVRRNEDQRGTAYAVTVDAANGSTGISATHRAETLRLLADQAAQPEDFTRPGHVVPLRARAGGVLVRDGHTEASVDLARLAGLQPVGVLCELVSEEDPTDMARSPELRAFADRHGLKMISIEQLIAWREEHDPAGEREQEDRTLSKVVSTTLPTDYGTFECIGFRDEREGTEHVALVKGNVTGAEDVLVRVHSECLTGDVFASRRCDCGDQLHAALKAIAEEGTGIVLYLRGHEGRGIGLLEKLRAYKLQDEGADTVDANLALGLPADARDYRAAALMLQDLEVQSIRLLSNNPSKQDSLAAYGVLSNEVLPLKVRVHEDNLHYLETKRDRMGHRLPWLPASDSQDT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP035299
EMBL· GenBank· DDBJ
QAU52316.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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