TKT1_KLULA
ID TKT1_KLULA Reviewed; 679 AA.
AC Q12630;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKL1; OrderedLocusNames=KLLA0B09152g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=9000376; DOI=10.1007/s002940050171;
RA Jacoby J.J., Heinisch J.J.;
RT "Analysis of a transketolase gene from Kluyveromyces lactis reveals that
RT the yeast enzymes are more related to transketolases of prokaryotic origins
RT than to those of higher eukaryotes.";
RL Curr. Genet. 31:15-21(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; U65983; AAB05935.1; -; Genomic_DNA.
DR EMBL; CR382122; CAH02329.1; -; Genomic_DNA.
DR RefSeq; XP_451936.1; XM_451936.1.
DR AlphaFoldDB; Q12630; -.
DR SMR; Q12630; -.
DR STRING; 28985.XP_451936.1; -.
DR PRIDE; Q12630; -.
DR EnsemblFungi; CAH02329; CAH02329; KLLA0_B09152g.
DR GeneID; 2896867; -.
DR KEGG; kla:KLLA0_B09152g; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; Q12630; -.
DR OMA; HHTEGIE; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..679
FT /note="Transketolase"
FT /id="PRO_0000191901"
FT ACT_SITE 417
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 116..118
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 30
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 262
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 679 AA; 73703 MW; BC5F3CF61A78CD4A CRC64;
MSQYTDIDRL AVSTIRLLAV DQVSAANSGH PGAPLGLAPA AHVIWKQMRL NPKNPEWINR
DRFVLSNGHA CALLYSLLHL FGYDMSIEDL KHFRHLGSKT PGHPEFELPG VEVTTGPLGQ
GISNAVGMAI AQANFAATYN KPDYELSDSY TYVFLGDGCL QEGVSSEASS LAGHLRLKNL
IAFYDDNQIT IDGNINVSFD EDVSKRYEAY GWEVLHVENG NDDLDAISKA LEQAKLSDRP
TLIKLTTTIG FGSLNAGSHS VHGAPLKADD VKQLKVKFGF NPEESFVVPQ EVYDLYNKST
IEPGIEANKQ WDALLDAYVG QFPELGAEVK RRLAGEFPEG WESKLPTYTP EDSAVASRKL
SEIVLDNVFD TLPELLGGSA DLTPSNLTRS KGAVDFQPPI TGLGDYSGRY IRYGVREHGM
GAIMNGISAF GANYRPYGGT FLNFVSYASG AVRLSALSGH PVIWVATHDS IGLGEDGPTH
QPIETLAHFR AIPNLQVWRP ADGNEVTAAY KVALTNKHTP AIIALSRQNL PQLQGSSVEK
AVKGGYILQD VDQPDLAIVS TGSEVGIAVE AAKVLAEKNI KARIVSLPDF HSFGQQSKEY
QLSVFPDGVP ILSVEVLATS GWSKYAHQSF GLDRFGASGK GPAVYEKFEF TPQGIATRAE
KTVEFYKGKQ VISPLNTAF
