T0VHR7 · T0VHR7_LACLC

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.

Type
IDPosition(s)Description
Binding site28-29D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site29Mg2+ 1 (UniProtKB | ChEBI)
Binding site29Mg2+ 2 (UniProtKB | ChEBI)
Binding site33D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site126Essential for DHBP synthase activity
Binding site140-144D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site143Mg2+ 2 (UniProtKB | ChEBI)
Binding site164D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site164Essential for DHBP synthase activity
Binding site252-256GTP (UniProtKB | ChEBI)
Binding site257Zn2+ (UniProtKB | ChEBI); catalytic
Binding site268Zn2+ (UniProtKB | ChEBI); catalytic
Binding site270Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273GTP (UniProtKB | ChEBI)
Binding site295-297GTP (UniProtKB | ChEBI)
Binding site317GTP (UniProtKB | ChEBI)
Active site329Proton acceptor; for GTP cyclohydrolase activity
Active site331Nucleophile; for GTP cyclohydrolase activity
Binding site352GTP (UniProtKB | ChEBI)
Binding site357GTP (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
      LLT3_01360

Organism names

Accessions

  • Primary accession
    T0VHR7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-201DHBP synthase
Region202-398GTP cyclohydrolase II
Domain208-373GTP 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    398
  • Mass (Da)
    44,552
  • Last updated
    2013-10-16 v1
  • Checksum
    1A796E4074068ED6
MFQYNTVEEALTALKAGEMIIVTDDENRENEGDLICAAEMISPEKINFMASQAKGLICSPMSEKYAKSLHLSAMTERNTDNHGTAFTVSVDHVETSTGVSAFDRSLTIRKLADEESSVEDFRRPGHVFPLIAKKNGVLERNGHTEATVDLLRLAGLKEVGVCVEIMAEDGSMMRTEELQEKAKEWDLNFITIKAIQEYRKQNEQLVEQVTRAKLPTKYGYFEIFGFVNKINGEHHVALVKGDIGEGEAVLCRVHSECLTGDAFGSMKCDCGEQLEQALTQINAEGRGVLLYLRQEGRGIGLINKLRAYSLQDEGLDTIEANLALGFEEDAREYSIGAQILKTLGVKSLRLMTNNPQKINDFSKYGLPVKERVPIQIKENEFDQDYLKVKQNKMGHLFD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ATBE01000178
EMBL· GenBank· DDBJ
EQC95357.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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