A0AAJ1DZ51 · A0AAJ1DZ51_9ENTR

Function

function

Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine 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:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Note: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site25substrate
Site25Important for catalytic activity
Binding site260substrate
Site260Important for catalytic activity
Binding site357substrate
Binding site384substrate
Binding site460substrate
Binding site468substrate
Binding site472substrate
Binding site519substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionmetal ion binding
Molecular Functiontransketolase activity
Biological Processpentose-phosphate shunt

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transketolase
  • EC number

Gene names

    • Name
      tkt
    • ORF names
      J0A64_21130

Organism names

  • Taxonomic identifier
  • Strain
    • BK34275
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Enterobacter > Enterobacter cloacae complex

Accessions

  • Primary accession
    A0AAJ1DZ51

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain354-525Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the transketolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    662
  • Mass (Da)
    72,445
  • Last updated
    2024-07-24 v1
  • Checksum
    976701894FE469C6
MSRKELANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWNDFLKHNPNDPTWYDRDRFILSNGHASMLLYSLLHLSGYDLPLEELKNFRQLHSKTPGHPEIGYTPGVETTTGPLGQGLANAVGLAIAERTLAAQFNQPDHEIVDHYTYVFMGDGCLMEGISHEVCSLAGTLGLGKLIGFYDHNGISIDGETEGWFTDDTAKRFEAYHWHVVHEIDGHDPEAVKKAIQEAQSVKDKPSLIICRTVIGFGSPNKAGKEEAHGAALGDEEVALTRQKLGWKYPPFEIPKEIYRAWDAREDGEKAQQAWNEKFAAYKKAYPELAAEFSRRMSGGLPEDWDDKTQALIENLQSNPAKIATRKASQNTLNAIGPLLPELLGGSADLAPSNLTIWSGSKSLKEDIAGNYIHYGVREFGMTAIANGIAHHGGFVPYTATFLMFVEYARNAARMAALMKARQIMVYTHDSIGLGEDGPTHQAVEQLASLRLTPNFSTWRPCDQVEAAVGWKLAVERHNGPTALILSRQNLTQIERTPEQVKNIARGGYILKDSGGKPDVILIATGSEVEITVKAAEKLTAEGHAVRVVSLPSTDTFDAQDEAYRESVLPSNVAARVAVEAGIADYWYKYVGLKGAIVGMRGYGESAPADKLFPYFGFTVENVVEKALSVI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAFKCP010000019
EMBL· GenBank· DDBJ
MBU3769100.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help