D9QAL2 · D9QAL2_CORP2

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 site48-49D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site49Mg2+ 1 (UniProtKB | ChEBI)
Binding site49Mg2+ 2 (UniProtKB | ChEBI)
Binding site53D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site146Essential for DHBP synthase activity
Binding site160-164D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site163Mg2+ 2 (UniProtKB | ChEBI)
Binding site184D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site184Essential for DHBP synthase activity
Binding site294-298GTP (UniProtKB | ChEBI)
Binding site299Zn2+ (UniProtKB | ChEBI); catalytic
Binding site310Zn2+ (UniProtKB | ChEBI); catalytic
Binding site312Zn2+ (UniProtKB | ChEBI); catalytic
Binding site315GTP (UniProtKB | ChEBI)
Binding site338-340GTP (UniProtKB | ChEBI)
Binding site360GTP (UniProtKB | ChEBI)
Active site372Proton acceptor; for GTP cyclohydrolase activity
Active site374Nucleophile; for GTP cyclohydrolase activity
Binding site395GTP (UniProtKB | ChEBI)
Binding site400GTP (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
      CPC231_05625

Organism names

Accessions

  • Primary accession
    D9QAL2

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-223DHBP synthase
Region224-451GTP cyclohydrolase II
Domain247-416GTP 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
    451
  • Mass (Da)
    48,734
  • Last updated
    2010-10-05 v1
  • Checksum
    85AAF567E50CF945
MTIHIDTPGQTAHDDTGRTDRVILDSVETAIANIAAGKAVIVVDNEDRENEGDIIFAAEKATPELVAFMVRYSSGYICAPLTGEDCDRLGLSPMVTHNQDIRGTAYTVTVDANTGSTGISATSRAYTIQKLSDIASTPDDFTRPGHVVPLRAVPGGVLERPGHTEAAIDLARLAGLRPAGVLCEVVSEDNPTEMARGPELRRFADKHGLALISIDQMIEWRTKHDPATTSADPLHSRERVASAAIAERVTSTRLPTDFGFFTAVGYRALSDGIEHVALVVGDITDNDGTDVLVRVHSECLTGDVFGSRRCDCGQQLQASMKLVQEKGRGVILYLRGQEGRGIGLAEKLRAYHLQDGGIDTVDANLALGLPADARDYGIAAFILHDLGVRSANLLSNNPSKHEGLTGYGLEVSGRTPVEVAVNEDNLRYLITKRDRMRHDLPWIETYVSSHH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001829
EMBL· GenBank· DDBJ
ADL10588.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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