TKT2_YEAST
ID TKT2_YEAST Reviewed; 681 AA.
AC P33315; D6VQB5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Transketolase 2;
DE Short=TK 2;
DE EC=2.2.1.1;
GN Name=TKL2; OrderedLocusNames=YBR117C; ORFNames=YBR0912;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7916691; DOI=10.1111/j.1432-1033.1993.tb18268.x;
RA Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K.,
RA Feldmann H.;
RT "TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning,
RT sequence and deletion analysis of the gene.";
RL Eur. J. Biochem. 217:487-492(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- INTERACTION:
CC P33315; P23254: TKL1; NbExp=3; IntAct=EBI-19297, EBI-19291;
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; X73532; CAA51937.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55619.1; -; Genomic_DNA.
DR EMBL; Z35985; CAA85074.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07235.1; -; Genomic_DNA.
DR PIR; S37809; S37809.
DR RefSeq; NP_009675.3; NM_001178465.3.
DR AlphaFoldDB; P33315; -.
DR SMR; P33315; -.
DR BioGRID; 32819; 83.
DR DIP; DIP-757N; -.
DR IntAct; P33315; 2.
DR MINT; P33315; -.
DR STRING; 4932.YBR117C; -.
DR MaxQB; P33315; -.
DR PaxDb; P33315; -.
DR PRIDE; P33315; -.
DR TopDownProteomics; P33315; -.
DR EnsemblFungi; YBR117C_mRNA; YBR117C; YBR117C.
DR GeneID; 852414; -.
DR KEGG; sce:YBR117C; -.
DR SGD; S000000321; TKL2.
DR VEuPathDB; FungiDB:YBR117C; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000176704; -.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; P33315; -.
DR OMA; YALQQTD; -.
DR BioCyc; YEAST:YBR117C-MON; -.
DR BRENDA; 2.2.1.1; 984.
DR SABIO-RK; P33315; -.
DR PRO; PR:P33315; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33315; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; ISS:SGD.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:SGD.
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 1: Evidence at protein level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..681
FT /note="Transketolase 2"
FT /id="PRO_0000191905"
FT ACT_SITE 418
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 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 30
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 681 AA; 75029 MW; 84D7477916D136D5 CRC64;
MAQFSDIDKL AVSTLRLLSV DQVESAQSGH PGAPLGLAPV AHVIFKQLRC NPNNEHWINR
DRFVLSNGHS CALLYSMLHL LGYDYSIEDL RQFRQVNSRT PGHPEFHSAG VEITSGPLGQ
GISNAVGMAI AQANFAATYN EDGFPISDSY TFAIVGDGCL QEGVSSETSS LAGHLQLGNL
ITFYDSNSIS IDGKTSYSFD EDVLKRYEAY GWEVMEVDKG DDDMESISSA LEKAKLSKDK
PTIIKVTTTI GFGSLQQGTA GVHGSALKAD DVKQLKKRWG FDPNKSFVVP QEVYDYYKKT
VVEPGQKLNE EWDRMFEEYK TKFPEKGKEL QRRLNGELPE GWEKHLPKFT PDDDALATRK
TSQQVLTNMV QVLPELIGGS ADLTPSNLTR WEGAVDFQPP ITQLGNYAGR YIRYGVREHG
MGAIMNGISA FGANYKPYGG TFLNFVSYAA GAVRLAALSG NPVIWVATHD SIGLGEDGPT
HQPIETLAHL RAIPNMHVWR PADGNETSAA YYSAIKSGRT PSVVALSRQN LPQLEHSSFE
KALKGGYVIH DVENPDIILV STGSEVSISI DAAKKLYDTK KIKARVVSLP DFYTFDRQSE
EYRFSVLPDG VPIMSFEVLA TSSWGKYAHQ SFGLDEFGRS GKGPEIYKLF DFTADGVASR
AEKTINYYKG KQLLSPMGRA F
