A0A6N4UNB1 · A0A6N4UNB1_9MYCO

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribAB
  • 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 site44-45D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site45Mg2+ 1 (UniProtKB | ChEBI)
Binding site45Mg2+ 2 (UniProtKB | ChEBI)
Binding site49D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site143Essential for DHBP synthase activity
Binding site157-161D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site160Mg2+ 2 (UniProtKB | ChEBI)
Binding site181D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site181Essential for DHBP synthase activity
Binding site275-279GTP (UniProtKB | ChEBI)
Binding site280Zn2+ (UniProtKB | ChEBI); catalytic
Binding site291Zn2+ (UniProtKB | ChEBI); catalytic
Binding site293Zn2+ (UniProtKB | ChEBI); catalytic
Binding site296GTP (UniProtKB | ChEBI)
Binding site319-321GTP (UniProtKB | ChEBI)
Binding site341GTP (UniProtKB | ChEBI)
Active site353Proton acceptor; for GTP cyclohydrolase activity
Active site355Nucleophile; for GTP cyclohydrolase activity
Binding site376GTP (UniProtKB | ChEBI)
Binding site381GTP (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
      ribAB
    • Synonyms
      ribBA
    • ORF names
      MALV_10540

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JCM 12272
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium

Accessions

  • Primary accession
    A0A6N4UNB1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-220DHBP synthase
Region221-458GTP cyclohydrolase II
Domain226-397GTP 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
    458
  • Mass (Da)
    49,832
  • Last updated
    2020-10-07 v1
  • Checksum
    F318E0DF26E99DF4
MVPPWGPGMRTGKVAQMTRLDSVERAIADIAAGKAVVVIDDEDRENEGDLIFAAEKATPELVAFMVRYTSGYLCVPLDGEVCDRLGLLPMYAVNQDKHGTAYTVTVDAKKNVGTGISASDRATTMRALADPGSAIDDFTKPGHVVPLRAKDGGVLRRPGHTEAAVDLARLAGLQPAGAICEIVSQKDEGDMARTDELRVFADDHDLALISIADLIEWRRKHEKHIERIAEARIPTRHGEFVAVGYKSIYEDVEHVALVRGDICGPTSDGHDVLVRVHSECLTGDVFGSRRCDCGPQLDAAMAMVAREGRGVVLYMRGHEGRGIGLMHKLQAYQLQDAGEDTVDANLKLGLPADARDYGIGAQILVDLGIRSMRLLTNNPAKRVGLDGYGLHIIERVPLPVRANSENIRYLMTKRDRMGHDLVGLEDYDEAVSMDDYDEAVYLLGDRRPPSATDSGSSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP022565
EMBL· GenBank· DDBJ
BBX25929.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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