A0A0A2ADN1 · A0A0A2ADN1_PROMR

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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)
Site149Essential for DHBP synthase activity
Binding site163-167D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site166Mg2+ 2 (UniProtKB | ChEBI)
Binding site187D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site187Essential for DHBP synthase activity
Binding site276-280GTP (UniProtKB | ChEBI)
Binding site281Zn2+ (UniProtKB | ChEBI); catalytic
Binding site292Zn2+ (UniProtKB | ChEBI); catalytic
Binding site294Zn2+ (UniProtKB | ChEBI); catalytic
Binding site297GTP (UniProtKB | ChEBI)
Binding site319-321GTP (UniProtKB | ChEBI)
Binding site341GTP (UniProtKB | ChEBI)
Active site353Proton acceptor; for GTP cyclohydrolase activity
Active site355Nucleophile; for GTP cyclohydrolase activity
Binding site376GTP (UniProtKB | ChEBI)
Binding site381GTP (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
      EU96_0557

Organism names

Accessions

  • Primary accession
    A0A0A2ADN1

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-224DHBP synthase
Region225-574GTP cyclohydrolase II
Domain234-397GTP 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
    574
  • Mass (Da)
    64,158
  • Last updated
    2015-02-04 v1
  • Checksum
    6AD40E531DF3593B
MKETSPKSNNGTILDINKSFKIEFDPISDALAAIRNGECIIVVDDERRENEGDLICAAQFATPQQINFMATEGRGLICLAMQGEKLDSLDLPLMVDRNTDENQTAFTISIDAGPENNVSTGISAEDRAKTIQVAINPNTKPEELRRPGHIFPLRAKKGGVLKRAGHTEAAVDIAAMSGLYPAGVICEIQNPDGSMSRLPQLKEYAKQWGMKLISIADLISYRFQTERFVFRKSDAVLPSIFGNFKAYGYVNELDGSEHVALVKQKASRLSEPVLVRMHSECLTGDAFGSLRCDCRPQLEAALSRIEKEEEGVVVYLRQEGRGIGLINKLKAYSLQDGGLDTVEANEKLGFPADLRNYGVGAQILTDLGIKKLKLLTNNPRKIAGLGGYGIEVIERVPLVICPNDNNAEYLSVKKTKLGHMFDEDISNPRNIDPFISIFLDGNYKSIDLVSIKNKVIKFCNIQNINIKLESTPRLLAFWNRPKLVWKILHDRNRTNSNITDEEIKNIELFIQFLSKYENSTKVGVIVSRNIEQALHPKSSIKLIKTKFTINNEILYSSTRKFNLDKETFSIVFED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JNAM01000005
EMBL· GenBank· DDBJ
KGF98594.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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