Q827M0 · Q827M0_STRAW

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 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
      ribA1
    • Synonyms
      ribBA
    • ORF names
      SAVERM_6904

Organism names

Accessions

  • Primary accession
    Q827M0

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    429
  • Mass (Da)
    46,389
  • Last updated
    2003-06-01 v1
  • Checksum
    6BD615FFD1F1FC46
MTTAPILYSTDNIEDFALDPVERAIADIAAGRPVVVVDDEDRENEGDLVIAAEKATPEIVAFMMSECRGLICAPMEGGELDRLQLPQMVDHNTESMRTAFTVSVDASGAHGVTTGISAADRATTLRLLAQGEAGAADFVRPGHIFPLRAKPGGVLVRNGHTEAAVDLARLAGLRPAGAIVEIAGEDGHMLRLPELIPFARKHGLTIISIEDLIAYRQSSEPTVRREAEVHLPTAFGEFTAYGYRSTVDGVEHVALVHGEIGDGEGVLVRVHSECLTGDVFHSLRCDCGPQLEASLERIRSEGRGVVVYLRGHEGRGIGLVSKLRAYELQERGRDTLDANLELGLPADARDYAAGAQILEDLGVRSLRLMTNNPDKTDALLRHGLKVTGREPMPVQAGEHNLRYLTTKRDRMGHDLPWLDTVPVSTCGNQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000030
EMBL· GenBank· DDBJ
BAC74615.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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