A0A6G3D7H4 · A0A6G3D7H4_9ACTN

  • 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.

Type
IDPosition(s)Description
Binding site42-43D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site43Mg2+ 1 (UniProtKB | ChEBI)
Binding site43Mg2+ 2 (UniProtKB | ChEBI)
Binding site47D-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 site269-273GTP (UniProtKB | ChEBI)
Binding site274Zn2+ (UniProtKB | ChEBI); catalytic
Binding site285Zn2+ (UniProtKB | ChEBI); catalytic
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Binding site290GTP (UniProtKB | ChEBI)
Binding site313-315GTP (UniProtKB | ChEBI)
Binding site335GTP (UniProtKB | ChEBI)
Active site347Proton acceptor; for GTP cyclohydrolase activity
Active site349Nucleophile; for GTP cyclohydrolase activity
Binding site370GTP (UniProtKB | ChEBI)
Binding site375GTP (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
      GTY44_14920

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SID5914
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A6G3D7H4

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-218DHBP synthase
Region219-429GTP cyclohydrolase II
Domain225-390GTP 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
    429
  • Mass (Da)
    46,310
  • Last updated
    2020-08-12 v1
  • Checksum
    D1C901ED3B7392A8
MTTAPILYSPDGIDDLSLDPVEQAVADIAAGRPVVVVDDEGRENEGDLVIAAEKATEEIVAFMMTECRGLICAPMEGEELDRLRLPQMVDDNTESMKTAFTVSVDAGAAHGVTTGISAADRAATLQLLASGTAEPTDLVRPGHVFPLRARPGGVLVRNGHTEAAVDLARLAGLRPAGAIVEIAGEDGRMLRLPELIPFARKHGLTIISIEDLIAYRRTEEPTVRREAEVRLPTSHGEFTAYGYRSTVDGVEHVALVHGDIGDGEDVLVRVHSECLTGDVFGSQRCDCGPQLDASLDRIQAEGRGVVVYLRGHEGRGIGLMSKLRAYELQERGRDTLDANLELGLPADARDYGAGAQILKDLGVRAVRLMTNNPDKSDALERHGITVTGREPMPVQAGEHNLRYLRTKRDRMGHDLPWLDTTPVSTCGNQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WWHW01000552
EMBL· GenBank· DDBJ
MZG14767.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp