E3HBH8 · E3HBH8_ILYPC

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 site26-27D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site27Mg2+ 1 (UniProtKB | ChEBI)
Binding site27Mg2+ 2 (UniProtKB | ChEBI)
Binding site31D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site125Essential for DHBP synthase activity
Binding site139-143D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site142Mg2+ 2 (UniProtKB | ChEBI)
Binding site163D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site163Essential for DHBP synthase activity
Binding site251-255GTP (UniProtKB | ChEBI)
Binding site256Zn2+ (UniProtKB | ChEBI); catalytic
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site272GTP (UniProtKB | ChEBI)
Binding site294-296GTP (UniProtKB | ChEBI)
Binding site316GTP (UniProtKB | ChEBI)
Active site328Proton acceptor; for GTP cyclohydrolase activity
Active site330Nucleophile; for GTP cyclohydrolase activity
Binding site351GTP (UniProtKB | ChEBI)
Binding site356GTP (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
    • Ordered locus names
      Ilyop_2022

Encoded on

  • Plasmid pILYOP01

Organism names

Accessions

  • Primary accession
    E3HBH8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-200DHBP synthase
Region201-402GTP cyclohydrolase II
Domain209-370GTP 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
    402
  • Mass (Da)
    44,638
  • Last updated
    2011-01-11 v1
  • Checksum
    1EE24DB4BC90B8DA
MLDRIDEAIEDIKAGKMVIVVDDENRENEGDIIIAGEKVSYESINFMAKYARGLTCVPMTRERADQLHLPQMVNRNTDSHGTAFTVSVDAAEGTTTGISVADRVKTITDLVDESKGPWDFKRPGHLFPLVAKDGGVLARPGHTEAAVDLARLAGLKPVGVICEILKDDGTMARLMDLKEFAKEHDLKIVSIEDLIKYRKEHDVLMEVYATATMPTIAGNFEIVAFDNKLDGKEHIALIKGDIKGKEDVLIRIHSECFTGDILGSMRCDCGLQLKEAMKKIDEEGAGIILYLRQEGRGIGLINKIKAYALQDKGLDTVEANEQLGFEADLRDYAVASQMLKALEVKSVRVMTNNLRKVNGLEKYGVKVNKRKGIEVDSNENNLRYLKTKKTKLGHILKLDENK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002282
EMBL· GenBank· DDBJ
ADO83793.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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