Q64YT3 · RIBBA_BACFR

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.
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 site30-31D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site31Mg2+ 1 (UniProtKB | ChEBI)
Binding site31Mg2+ 2 (UniProtKB | ChEBI)
Binding site35D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site129Essential for DHBP synthase activity
Binding site143-147D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site146Mg2+ 2 (UniProtKB | ChEBI)
Binding site167D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site167Essential for DHBP synthase activity
Binding site255-259GTP (UniProtKB | ChEBI)
Binding site260Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273Zn2+ (UniProtKB | ChEBI); catalytic
Binding site276GTP (UniProtKB | ChEBI)
Binding site298-300GTP (UniProtKB | ChEBI)
Binding site320GTP (UniProtKB | ChEBI)
Active site332Proton acceptor; for GTP cyclohydrolase activity
Active site334Nucleophile; for GTP cyclohydrolase activity
Binding site355GTP (UniProtKB | ChEBI)
Binding site360GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
      BF0594

Organism names

Accessions

  • Primary accession
    Q64YT3

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001652471-404Riboflavin biosynthesis protein RibBA

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-204DHBP synthase
Region205-404GTP cyclohydrolase II

Sequence similarities

In the N-terminal section; belongs to the DHBP synthase family.
In the C-terminal section; belongs to the GTP cyclohydrolase II family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    404
  • Mass (Da)
    45,101
  • Last updated
    2004-10-25 v1
  • Checksum
    F456056CAA89C843
MEPIRLNTIEEAIADFKEGNFVIVVDDEDRENEGDFIIAAEKITPEKVNFMLTHGRGVLCAPITEERCAELELDMQVSSNTSIYETPFTVTVDLLEGCTTGVSMHDRAMTIRALADPKTKPADLGRPGHINPLRARSRGVLRRAGHTEASVDLAKLAGLYPAAALIEIINEDGTMARLPQLVEVARRFGLKIISIKDLIAYRLQMESIVDRGVEVDMPTQFGHFRLIPFRQKSNGMEHIALIKGTWDTDEPILVRVHSSCMTGDIFGSCRCECGEQLHKAMEMIEAAGKGVIVYMNQEGRGIGLMNKIAAYKLQEEGYDTVDANLHLGFDADERDYGVGAQILREIGVKKMKLMTNNPVKRIGLEAYGLEITENVGIEIKPNPYNERYLKTKKDRMGHTLHFNK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP006841
EMBL· GenBank· DDBJ
BAD47343.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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