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A0A6J4JLR9 · A0A6J4JLR9_9ACTN

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.

Type
IDPosition(s)Description
Binding site28-29D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site29Mg2+ 1 (UniProtKB | ChEBI)
Binding site29Mg2+ 2 (UniProtKB | ChEBI)
Binding site33D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site127Essential for DHBP synthase activity
Binding site141-145D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site144Mg2+ 2 (UniProtKB | ChEBI)
Binding site165D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site165Essential for DHBP synthase activity
Binding site253-257GTP (UniProtKB | ChEBI)
Binding site258Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site274GTP (UniProtKB | ChEBI)
Binding site297-299GTP (UniProtKB | ChEBI)
Binding site319GTP (UniProtKB | ChEBI)
Active site331Proton acceptor; for GTP cyclohydrolase activity
Active site333Nucleophile; for GTP cyclohydrolase activity
Binding site354GTP (UniProtKB | ChEBI)
Binding site359GTP (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
      AVDCRST_MAG41-3617

Organism names

Accessions

  • Primary accession
    A0A6J4JLR9

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-202DHBP synthase
Region203-404GTP cyclohydrolase II
Domain209-375GTP 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
    404
  • Mass (Da)
    43,205
  • Last updated
    2020-10-07 v1
  • MD5 Checksum
    D8F5CD3838742DC299B0B97C7E2D2E49
MTAFGTVDRALTDIAAGIPVVVVDDADRENEGDLILAAELATPELMAFFVRWTSGVLCAPLTGEDCDRLALPPMSVTNTDRKQTAYTVSVDARDGTSTGISAADRALTLRLLADPAGKAEHFTRPGHVFPLRAKEGGVLRRPGHTEAGVDLARLAGLHPAAVIGEVVNDDGTMKRLPELTAFAAEHGLTLISIADLVAHRMRTERQVRRVAGARMPTKHGVFSGVGYASDLDDREHVALVAGDIGDGRDILVRVHSECLTGDVFGSQRCDCGPQLDASLAAVAAEGRGVVLYMRGHEGRGIGLLHKLQAYQLQDLGADTVDANLELGLPADARDYGTGAQILVDLGVRTMRLLTNNPDKRAGLEGYGLTILERVPLPVHETRDNLRYLLTKRDRMGHDLPGLSS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADCTP010000331
EMBL· GenBank· DDBJ
CAA9281864.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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