A0A517TRC8 · A0A517TRC8_9BACT

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site29-30D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site30Mg2+ 2 (UniProtKB | ChEBI)
Binding site30Mg2+ 1 (UniProtKB | ChEBI)
Binding site34D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site127Essential for DHBP synthase activity
Binding site141-145D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site144Mg2+ 2 (UniProtKB | ChEBI)
Binding site165D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site165Essential for DHBP synthase activity
Binding site253-257GTP (UniProtKB | ChEBI)
Binding site258Zn2+ (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site274GTP (UniProtKB | ChEBI)
Binding site296-298GTP (UniProtKB | ChEBI)
Binding site318GTP (UniProtKB | ChEBI)
Active site330Proton acceptor; for GTP cyclohydrolase activity
Active site332Nucleophile; for GTP cyclohydrolase activity
Binding site353GTP (UniProtKB | ChEBI)
Binding site358GTP (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
      I41_00720

Organism names

  • Taxonomic identifier
  • Strain
    • I41
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Pirellulales > Lacipirellulaceae > Lacipirellula

Accessions

  • Primary accession
    A0A517TRC8

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-202DHBP synthase
Region203-401GTP cyclohydrolase II
Domain209-376GTP 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
    401
  • Mass (Da)
    43,860
  • Last updated
    2019-10-16 v1
  • Checksum
    2270AD789B8C3E99
MSHQFSTIEQAVEAIRQGRVIIVADDEDRENEGDFVCAAEKVTPEIVNFMITYGRGQLCMPILPDVSQRLELGAMVEANNSPLGTNYTVPVDHRTSRTGITAGERSTTIRALCDPTSVPADFIRPGHLFPLVAKEGGVLRRAGHTEAAVDLTRMAGLTPAGVLCEILDDDGDRATRPKLQELAKKFDLPVISIEQLIAHRRLSEKLVYRTAEAKLPTKYGNGKIISYGVKYESQEPVVYVIGDPASVAAPLVRLHSSCFTGDLLESLRCDCGDQLHMALDMIGREGAGVLVYLPQEGRGIGLVEKIKAYALQDQGMDTVEANIALGYMADPRDYGVGIQLLKDLGLRKVRLLTNNPKKTDAFIYGGFDLEVVDQVPIVGPIHEHNAAYMATKREKMGHKLP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036339
EMBL· GenBank· DDBJ
QDT70919.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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