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A0A142XAW2 · A0A142XAW2_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.
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 site32-33D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site33Mg2+ 1 (UniProtKB | ChEBI)
Binding site33Mg2+ 2 (UniProtKB | ChEBI)
Binding site37D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site132Essential for DHBP synthase activity
Binding site146-150D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site149Mg2+ 2 (UniProtKB | ChEBI)
Binding site170D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site170Essential for DHBP synthase activity
Binding site272-276GTP (UniProtKB | ChEBI)
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Binding site290Zn2+ (UniProtKB | ChEBI); catalytic
Binding site293GTP (UniProtKB | ChEBI)
Binding site315-317GTP (UniProtKB | ChEBI)
Binding site338GTP (UniProtKB | ChEBI)
Active site350Proton acceptor; for GTP cyclohydrolase activity
Active site352Nucleophile; for GTP cyclohydrolase activity
Binding site373GTP (UniProtKB | ChEBI)
Binding site378GTP (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
      VT84_06890

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SH-PL17
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Gemmatales > Gemmataceae > Gemmata

Accessions

  • Primary accession
    A0A142XAW2

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-207DHBP synthase
Region208-427GTP cyclohydrolase II
Domain216-394GTP 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
    427
  • Mass (Da)
    46,916
  • Last updated
    2016-06-08 v1
  • MD5 Checksum
    7789FD0EC1A51BE52D08EBBD01583970
MPRTAEGFCSIDAALDDLRAGRMIVLVDDEHRENEGDLVMAAEAVTPAAINFMIRYACGRLCVSFSRPHAERLGLELLPGVNLDPTATPFTHNFDARFGVSTGISAFDRARTVQVCADPASGPQDLVRDKGHLDGLIARPGGVLVRAGHTEGSVDLCRLAGLREIAVICEVLNDDGSMARLPDLREFCKKHELKMCTIADLIEHRRRREKLIKREIALKLPTEFGTFDLFAYTSMVDQEPHLALALGGIGLPTADAAGASNIPVQEESVLVRMHSECLTGDVLHSTKCDCGPQLKYAMQQVAEAGRGVIVYMRQEGRGIGLLNKLKAYKLQQEEGLDTVEANKRLGFAPDLRHFGIGAQILHDLGVRDIKLLTNNPRKVIGLEGYGLRIVERVPIQMQPGDHNRDYLQTKKDKLGHLLDEFETGGED

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011271
EMBL· GenBank· DDBJ
AMV24105.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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