TKT_STAEQ
ID TKT_STAEQ Reviewed; 662 AA.
AC Q5HPJ9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transketolase;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=SERP0912;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; CP000029; AAW54287.1; -; Genomic_DNA.
DR RefSeq; WP_002456536.1; NC_002976.3.
DR AlphaFoldDB; Q5HPJ9; -.
DR SMR; Q5HPJ9; -.
DR STRING; 176279.SERP0912; -.
DR EnsemblBacteria; AAW54287; AAW54287; SERP0912.
DR KEGG; ser:SERP0912; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_9; -.
DR OMA; HHTEGIE; -.
DR OrthoDB; 188169at2; -.
DR UniPathway; UPA00115; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium; DNA recombination; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..662
FT /note="Transketolase"
FT /id="PRO_0000191877"
FT ACT_SITE 410
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 115..117
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 28
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 662 AA; 72939 MW; 6691C2AB3825404F CRC64;
MFNEKDQLAI DTIRALSIDA IEKANSGHPG LPMGAAPMAY TLWTRHLNFN PQSKDFFNRD
RFILSAGHGS ALLYSLLHVS GSLELEELKQ FRQWGSKTPG HPEYRHTDGV EVTTGPLGQG
FAMSVGMALA ESHLAGKFNK DQFDIVNHYT YVLASDGDLM EGISHEAASF AGHNQLDKLI
VLYDSNDISL DGDLDKSFSE DTKQRFEAYG WNYILVENGN DLDEIDNAIT QAKSQQGPTI
IEVKTIIGFG SPNKAGSNGV HGAPLGEEER ALTFKEYGLD PEKRFNVPED VYEIFKSTML
KRANENEEAW NNMLKNYSEA YPELAEEFKL AMSGKLPNNY ADALPEYDLN HSGASRADSG
EIIQKLSEFV PSFFGGSADL AGSNKSNVKE AKDYNKDTPE GKNVWFGVRE FAMGAAINGM
AAHGGLHPYA ATFFVFSDYL KPALRLSSIM GLNSTFIFTH DSIAVGEDGP THEPIEQLAG
LRAIPNMNVI RPADGNETRV AWEVALESEQ TPTSLVLTRQ NLPTLDVDKQ TVENGVRKGA
YIVFETEQQL EYLLLASGSE VNLAVEAAKE LEQQGKGVRV ISMPNWYAFE QQSSEYKESI
LPSDVTKRIA IEMASPLGWH KYVGIEGKVI GINSFGASAP GDLVVEKYGF TKENILKQVR
SL
