D2QU60 · D2QU60_SPILD

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 site51-52D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site52Mg2+ 1 (UniProtKB | ChEBI)
Binding site52Mg2+ 2 (UniProtKB | ChEBI)
Binding site56D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site151Essential for DHBP synthase activity
Binding site165-169D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site168Mg2+ 2 (UniProtKB | ChEBI)
Binding site189D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site189Essential for DHBP synthase activity
Binding site277-281GTP (UniProtKB | ChEBI)
Binding site282Zn2+ (UniProtKB | ChEBI); catalytic
Binding site293Zn2+ (UniProtKB | ChEBI); catalytic
Binding site295Zn2+ (UniProtKB | ChEBI); catalytic
Binding site298GTP (UniProtKB | ChEBI)
Binding site320-322GTP (UniProtKB | ChEBI)
Binding site342GTP (UniProtKB | ChEBI)
Active site354Proton acceptor; for GTP cyclohydrolase activity
Active site356Nucleophile; for GTP cyclohydrolase activity
Binding site377GTP (UniProtKB | ChEBI)
Binding site382GTP (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
      Slin_6384

Organism names

Accessions

  • Primary accession
    D2QU60

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-20Polar residues
Region1-24Disordered
Region1-226DHBP synthase
Region227-432GTP cyclohydrolase II
Domain236-398GTP 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
    432
  • Mass (Da)
    47,621
  • Last updated
    2010-03-02 v1
  • Checksum
    2103DF9F08ED4892
MMSNNSTNSEINSANEENPAESNPIRLDRIEDAIADIKAGKIVLVVDDEDRENEGDMICAAEMITPEMVNFMVREARGLMCAPLTQERCDELGLDMMVTSNTSVHTTPFTVSVDLLGNGCTTGISASDRSKTIQALVDPNTTPDDLGRPGHIFPLRAVEGGVIRRAGHTEAAVDLAKLAGLSPVGVLIEVLNEDGTMARLPELRVLADRFGMRLVSIQDLIAYRLRTETLIRREIGVDMPTQWGHFDLIAYKQSNTGDTHLALVKGTWEPNEPVMVRVHSSCVTGDIFGSCRCDCGPQLHAAMELVEKEGKGVVVYMFQEGRGIGLINKLKAYKLQEMGRDTVEANLDLGLPMDARDYGVGAQILRDLGIRKLRLISNNPKKRAGLMGYGLEIVDTVPLEIKSNPHNERYLRTKRDKMGHTIMNEPVNEEQE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-20Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001769
EMBL· GenBank· DDBJ
ADB42342.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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