Full text data of TKT
TKT
[Confidence: high (present in two of the MS resources)]
Transketolase; TK; 2.2.1.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transketolase; TK; 2.2.1.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00021716
IPI00021716 Transketolase Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00021716 Transketolase Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P29401
ID TKT_HUMAN Reviewed; 623 AA.
AC P29401; A8K089; B4DE31; E7EPA7; Q8TBA3; Q96HH3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 3.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8419340;
RA McCool B.A., Plonk S.G., Martin P.R., Singleton C.K.;
RT "Cloning of human transketolase cDNAs and comparison of the nucleotide
RT sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-
RT Korsakoff individuals.";
RL J. Biol. Chem. 268:1397-1404(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Jung E.-H., Sheu K.-F.R.E., Szabo P., Blass J.P.;
RT "Molecular cloning, sequence and chromosome localization of human
RT transketolase.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9115179; DOI=10.1007/PL00006179;
RA Schenk G., Layfield R., Candy J.M., Duggleby R.G., Nixon P.F.;
RT "Molecular evolutionary analysis of the thiamine-diphosphate-dependent
RT enzyme, transketolase.";
RL J. Mol. Evol. 44:552-572(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 1-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-623 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1567394; DOI=10.1016/S0006-291X(05)80312-2;
RA Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S.;
RT "Nucleotide and predicted amino acid sequence of a cDNA clone encoding
RT part of human transketolase.";
RL Biochem. Biophys. Res. Commun. 183:1159-1166(1992).
RN [10]
RP COFACTOR.
RX PubMed=3248678; DOI=10.1016/0020-711X(88)90228-5;
RA Jung E.H., Takeuchi T., Nishino K., Itokawa Y.;
RT "Studies on the nature of thiamine pyrophosphate binding and
RT dependency on divalent cations of transketolase from human
RT erythrocytes.";
RL Int. J. Biochem. 20:1255-1259(1988).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275 AND THR-287, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-11; LYS-144;
RP LYS-204; LYS-241; LYS-260 AND LYS-603, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275; THR-287 AND
RP SER-295, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-620 IN COMPLEXES WITH
RP CALCIUM AND THIAMINE PYROPHOSPHATE.
RX PubMed=20667822; DOI=10.1074/jbc.M110.149955;
RA Mitschke L., Parthier C., Schroder-Tittmann K., Coy J., Ludtke S.,
RA Tittmann K.;
RT "The crystal structure of human transketolase and new insights into
RT its mode of action.";
RL J. Biol. Chem. 285:31559-31570(2010).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC a ketose donor to an aldose acceptor, via a covalent intermediate
CC with the cofactor thiamine pyrophosphate.
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29401-2; Sequence=VSP_045566;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the transketolase family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transketolase entry;
CC URL="http://en.wikipedia.org/wiki/Transketolase";
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DR EMBL; X67688; CAA47919.1; -; mRNA.
DR EMBL; L12711; AAA61222.1; -; mRNA.
DR EMBL; U55017; AAA98961.1; -; mRNA.
DR EMBL; AK289454; BAF82143.1; -; mRNA.
DR EMBL; AK293438; BAG56942.1; -; mRNA.
DR EMBL; AC097015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65281.1; -; Genomic_DNA.
DR EMBL; BC008615; AAH08615.1; -; mRNA.
DR EMBL; BC009970; AAH09970.1; -; mRNA.
DR EMBL; BC024026; AAH24026.2; -; mRNA.
DR PIR; A45050; A45050.
DR RefSeq; NP_001055.1; NM_001064.3.
DR RefSeq; NP_001128527.1; NM_001135055.2.
DR RefSeq; NP_001244957.1; NM_001258028.1.
DR UniGene; Hs.89643; -.
DR PDB; 3MOS; X-ray; 1.75 A; A=3-618.
DR PDB; 3OOY; X-ray; 2.05 A; A/B=10-620.
DR PDB; 4KXU; X-ray; 0.98 A; A=1-623.
DR PDB; 4KXV; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXW; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXX; X-ray; 1.03 A; A=1-623.
DR PDB; 4KXY; X-ray; 1.26 A; A/B=1-623.
DR PDBsum; 3MOS; -.
DR PDBsum; 3OOY; -.
DR PDBsum; 4KXU; -.
DR PDBsum; 4KXV; -.
DR PDBsum; 4KXW; -.
DR PDBsum; 4KXX; -.
DR PDBsum; 4KXY; -.
DR ProteinModelPortal; P29401; -.
DR SMR; P29401; 3-618.
DR IntAct; P29401; 11.
DR MINT; MINT-3011391; -.
DR STRING; 9606.ENSP00000405455; -.
DR BindingDB; P29401; -.
DR ChEMBL; CHEMBL4983; -.
DR DrugBank; DB00152; Thiamine.
DR PhosphoSite; P29401; -.
DR DMDM; 1729976; -.
DR REPRODUCTION-2DPAGE; IPI00643920; -.
DR PaxDb; P29401; -.
DR PRIDE; P29401; -.
DR DNASU; 7086; -.
DR Ensembl; ENST00000423516; ENSP00000391481; ENSG00000163931.
DR Ensembl; ENST00000423525; ENSP00000405455; ENSG00000163931.
DR Ensembl; ENST00000462138; ENSP00000417773; ENSG00000163931.
DR GeneID; 7086; -.
DR KEGG; hsa:7086; -.
DR UCSC; uc011beq.2; human.
DR CTD; 7086; -.
DR GeneCards; GC03M053258; -.
DR HGNC; HGNC:11834; TKT.
DR HPA; HPA029480; -.
DR HPA; HPA029481; -.
DR MIM; 606781; gene.
DR neXtProt; NX_P29401; -.
DR PharmGKB; PA36537; -.
DR eggNOG; COG0021; -.
DR HOGENOM; HOG000243868; -.
DR HOVERGEN; HBG004036; -.
DR InParanoid; P29401; -.
DR KO; K00615; -.
DR OMA; AFENKAC; -.
DR OrthoDB; EOG72RMXF; -.
DR PhylomeDB; P29401; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P29401; -.
DR ChiTaRS; TKT; human.
DR EvolutionaryTrace; P29401; -.
DR GenomeRNAi; 7086; -.
DR NextBio; 27715; -.
DR PRO; PR:P29401; -.
DR ArrayExpress; P29401; -.
DR Bgee; P29401; -.
DR CleanEx; HS_TKT; -.
DR Genevestigator; P29401; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0048037; F:cofactor binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004802; F:transketolase activity; IDA:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; NAS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0005999; P:xylulose biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
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; SSF52922; SSF52922; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Complete proteome; Direct protein sequencing; Magnesium;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1 623 Transketolase.
FT /FTId=PRO_0000191894.
FT NP_BIND 123 125 Thiamine pyrophosphate.
FT ACT_SITE 366 366 Proton donor (By similarity).
FT METAL 155 155 Magnesium.
FT METAL 185 185 Magnesium.
FT METAL 187 187 Magnesium; via carbonyl oxygen.
FT BINDING 37 37 Substrate (By similarity).
FT BINDING 40 40 Thiamine pyrophosphate.
FT BINDING 77 77 Thiamine pyrophosphate.
FT BINDING 156 156 Thiamine pyrophosphate; via amide
FT nitrogen.
FT BINDING 185 185 Thiamine pyrophosphate.
FT BINDING 244 244 Thiamine pyrophosphate.
FT BINDING 258 258 Substrate (By similarity).
FT BINDING 258 258 Thiamine pyrophosphate.
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 345 345 Substrate (By similarity).
FT BINDING 392 392 Thiamine pyrophosphate.
FT BINDING 416 416 Substrate (By similarity).
FT BINDING 424 424 Substrate (By similarity).
FT BINDING 428 428 Thiamine pyrophosphate.
FT BINDING 474 474 Substrate (By similarity).
FT SITE 37 37 Important for catalytic activity (By
FT similarity).
FT SITE 258 258 Important for catalytic activity (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 N6-acetyllysine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 144 144 N6-acetyllysine.
FT MOD_RES 204 204 N6-acetyllysine.
FT MOD_RES 241 241 N6-acetyllysine.
FT MOD_RES 260 260 N6-acetyllysine.
FT MOD_RES 275 275 Phosphotyrosine.
FT MOD_RES 287 287 Phosphothreonine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 603 603 N6-acetyllysine.
FT VAR_SEQ 146 146 S -> SLPSSWDYS (in isoform 2).
FT /FTId=VSP_045566.
FT VARIANT 181 181 I -> V (in dbSNP:rs17052920).
FT /FTId=VAR_052634.
FT CONFLICT 30 31 TT -> SS (in Ref. 1; CAA47919).
FT CONFLICT 46 46 E -> V (in Ref. 1; CAA47919).
FT CONFLICT 224 230 LCKAFGQ -> AVQGLCE (in Ref. 9; AA
FT sequence).
FT CONFLICT 366 366 E -> G (in Ref. 4; BAG56942).
FT CONFLICT 426 426 P -> A (in Ref. 1; CAA47919).
FT CONFLICT 585 587 THL -> KTM (in Ref. 2; AAA61222).
FT CONFLICT 608 623 DRDAIAQAVRGLITKA -> TGMPLHKL (in Ref. 9;
FT AA sequence).
FT HELIX 9 33
FT HELIX 38 42
FT HELIX 45 53
FT STRAND 70 75
FT HELIX 76 78
FT HELIX 79 88
FT HELIX 94 99
FT HELIX 128 141
FT STRAND 149 155
FT HELIX 156 159
FT HELIX 161 172
FT STRAND 178 184
FT STRAND 189 192
FT TURN 194 197
FT HELIX 199 208
FT STRAND 212 217
FT HELIX 221 229
FT STRAND 236 241
FT TURN 244 247
FT TURN 249 253
FT HELIX 264 275
FT STRAND 314 316
FT HELIX 317 331
FT STRAND 335 341
FT HELIX 343 346
FT HELIX 349 354
FT HELIX 356 358
FT STRAND 359 361
FT HELIX 366 377
FT HELIX 378 380
FT STRAND 383 389
FT HELIX 390 396
FT HELIX 397 405
FT STRAND 410 418
FT HELIX 419 421
FT HELIX 426 428
FT STRAND 430 432
FT HELIX 433 438
FT STRAND 443 446
FT HELIX 451 462
FT STRAND 466 471
FT STRAND 474 478
FT STRAND 493 496
FT STRAND 501 506
FT HELIX 510 523
FT TURN 524 526
FT STRAND 528 533
FT STRAND 535 539
FT HELIX 542 551
FT TURN 552 554
FT STRAND 555 564
FT HELIX 568 576
FT STRAND 583 589
FT HELIX 598 604
FT HELIX 609 620
SQ SEQUENCE 623 AA; 67878 MW; 176C89C02FD2712B CRC64;
MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS
QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA
ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI
ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE
LLKMFGIDRD AIAQAVRGLI TKA
//
ID TKT_HUMAN Reviewed; 623 AA.
AC P29401; A8K089; B4DE31; E7EPA7; Q8TBA3; Q96HH3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 3.
DT 22-JAN-2014, entry version 149.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8419340;
RA McCool B.A., Plonk S.G., Martin P.R., Singleton C.K.;
RT "Cloning of human transketolase cDNAs and comparison of the nucleotide
RT sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-
RT Korsakoff individuals.";
RL J. Biol. Chem. 268:1397-1404(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Jung E.-H., Sheu K.-F.R.E., Szabo P., Blass J.P.;
RT "Molecular cloning, sequence and chromosome localization of human
RT transketolase.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9115179; DOI=10.1007/PL00006179;
RA Schenk G., Layfield R., Candy J.M., Duggleby R.G., Nixon P.F.;
RT "Molecular evolutionary analysis of the thiamine-diphosphate-dependent
RT enzyme, transketolase.";
RL J. Mol. Evol. 44:552-572(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 1-21.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-623 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1567394; DOI=10.1016/S0006-291X(05)80312-2;
RA Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S.;
RT "Nucleotide and predicted amino acid sequence of a cDNA clone encoding
RT part of human transketolase.";
RL Biochem. Biophys. Res. Commun. 183:1159-1166(1992).
RN [10]
RP COFACTOR.
RX PubMed=3248678; DOI=10.1016/0020-711X(88)90228-5;
RA Jung E.H., Takeuchi T., Nishino K., Itokawa Y.;
RT "Studies on the nature of thiamine pyrophosphate binding and
RT dependency on divalent cations of transketolase from human
RT erythrocytes.";
RL Int. J. Biochem. 20:1255-1259(1988).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275 AND THR-287, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-11; LYS-144;
RP LYS-204; LYS-241; LYS-260 AND LYS-603, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275; THR-287 AND
RP SER-295, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-620 IN COMPLEXES WITH
RP CALCIUM AND THIAMINE PYROPHOSPHATE.
RX PubMed=20667822; DOI=10.1074/jbc.M110.149955;
RA Mitschke L., Parthier C., Schroder-Tittmann K., Coy J., Ludtke S.,
RA Tittmann K.;
RT "The crystal structure of human transketolase and new insights into
RT its mode of action.";
RL J. Biol. Chem. 285:31559-31570(2010).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC a ketose donor to an aldose acceptor, via a covalent intermediate
CC with the cofactor thiamine pyrophosphate.
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29401-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29401-2; Sequence=VSP_045566;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the transketolase family.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Transketolase entry;
CC URL="http://en.wikipedia.org/wiki/Transketolase";
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DR EMBL; X67688; CAA47919.1; -; mRNA.
DR EMBL; L12711; AAA61222.1; -; mRNA.
DR EMBL; U55017; AAA98961.1; -; mRNA.
DR EMBL; AK289454; BAF82143.1; -; mRNA.
DR EMBL; AK293438; BAG56942.1; -; mRNA.
DR EMBL; AC097015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65281.1; -; Genomic_DNA.
DR EMBL; BC008615; AAH08615.1; -; mRNA.
DR EMBL; BC009970; AAH09970.1; -; mRNA.
DR EMBL; BC024026; AAH24026.2; -; mRNA.
DR PIR; A45050; A45050.
DR RefSeq; NP_001055.1; NM_001064.3.
DR RefSeq; NP_001128527.1; NM_001135055.2.
DR RefSeq; NP_001244957.1; NM_001258028.1.
DR UniGene; Hs.89643; -.
DR PDB; 3MOS; X-ray; 1.75 A; A=3-618.
DR PDB; 3OOY; X-ray; 2.05 A; A/B=10-620.
DR PDB; 4KXU; X-ray; 0.98 A; A=1-623.
DR PDB; 4KXV; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXW; X-ray; 0.97 A; A=1-623.
DR PDB; 4KXX; X-ray; 1.03 A; A=1-623.
DR PDB; 4KXY; X-ray; 1.26 A; A/B=1-623.
DR PDBsum; 3MOS; -.
DR PDBsum; 3OOY; -.
DR PDBsum; 4KXU; -.
DR PDBsum; 4KXV; -.
DR PDBsum; 4KXW; -.
DR PDBsum; 4KXX; -.
DR PDBsum; 4KXY; -.
DR ProteinModelPortal; P29401; -.
DR SMR; P29401; 3-618.
DR IntAct; P29401; 11.
DR MINT; MINT-3011391; -.
DR STRING; 9606.ENSP00000405455; -.
DR BindingDB; P29401; -.
DR ChEMBL; CHEMBL4983; -.
DR DrugBank; DB00152; Thiamine.
DR PhosphoSite; P29401; -.
DR DMDM; 1729976; -.
DR REPRODUCTION-2DPAGE; IPI00643920; -.
DR PaxDb; P29401; -.
DR PRIDE; P29401; -.
DR DNASU; 7086; -.
DR Ensembl; ENST00000423516; ENSP00000391481; ENSG00000163931.
DR Ensembl; ENST00000423525; ENSP00000405455; ENSG00000163931.
DR Ensembl; ENST00000462138; ENSP00000417773; ENSG00000163931.
DR GeneID; 7086; -.
DR KEGG; hsa:7086; -.
DR UCSC; uc011beq.2; human.
DR CTD; 7086; -.
DR GeneCards; GC03M053258; -.
DR HGNC; HGNC:11834; TKT.
DR HPA; HPA029480; -.
DR HPA; HPA029481; -.
DR MIM; 606781; gene.
DR neXtProt; NX_P29401; -.
DR PharmGKB; PA36537; -.
DR eggNOG; COG0021; -.
DR HOGENOM; HOG000243868; -.
DR HOVERGEN; HBG004036; -.
DR InParanoid; P29401; -.
DR KO; K00615; -.
DR OMA; AFENKAC; -.
DR OrthoDB; EOG72RMXF; -.
DR PhylomeDB; P29401; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P29401; -.
DR ChiTaRS; TKT; human.
DR EvolutionaryTrace; P29401; -.
DR GenomeRNAi; 7086; -.
DR NextBio; 27715; -.
DR PRO; PR:P29401; -.
DR ArrayExpress; P29401; -.
DR Bgee; P29401; -.
DR CleanEx; HS_TKT; -.
DR Genevestigator; P29401; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0048037; F:cofactor binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004802; F:transketolase activity; IDA:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; NAS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0005999; P:xylulose biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR005476; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
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; SSF52922; SSF52922; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calcium;
KW Complete proteome; Direct protein sequencing; Magnesium;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1 623 Transketolase.
FT /FTId=PRO_0000191894.
FT NP_BIND 123 125 Thiamine pyrophosphate.
FT ACT_SITE 366 366 Proton donor (By similarity).
FT METAL 155 155 Magnesium.
FT METAL 185 185 Magnesium.
FT METAL 187 187 Magnesium; via carbonyl oxygen.
FT BINDING 37 37 Substrate (By similarity).
FT BINDING 40 40 Thiamine pyrophosphate.
FT BINDING 77 77 Thiamine pyrophosphate.
FT BINDING 156 156 Thiamine pyrophosphate; via amide
FT nitrogen.
FT BINDING 185 185 Thiamine pyrophosphate.
FT BINDING 244 244 Thiamine pyrophosphate.
FT BINDING 258 258 Substrate (By similarity).
FT BINDING 258 258 Thiamine pyrophosphate.
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 345 345 Substrate (By similarity).
FT BINDING 392 392 Thiamine pyrophosphate.
FT BINDING 416 416 Substrate (By similarity).
FT BINDING 424 424 Substrate (By similarity).
FT BINDING 428 428 Thiamine pyrophosphate.
FT BINDING 474 474 Substrate (By similarity).
FT SITE 37 37 Important for catalytic activity (By
FT similarity).
FT SITE 258 258 Important for catalytic activity (By
FT similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 N6-acetyllysine.
FT MOD_RES 11 11 N6-acetyllysine.
FT MOD_RES 144 144 N6-acetyllysine.
FT MOD_RES 204 204 N6-acetyllysine.
FT MOD_RES 241 241 N6-acetyllysine.
FT MOD_RES 260 260 N6-acetyllysine.
FT MOD_RES 275 275 Phosphotyrosine.
FT MOD_RES 287 287 Phosphothreonine.
FT MOD_RES 295 295 Phosphoserine.
FT MOD_RES 603 603 N6-acetyllysine.
FT VAR_SEQ 146 146 S -> SLPSSWDYS (in isoform 2).
FT /FTId=VSP_045566.
FT VARIANT 181 181 I -> V (in dbSNP:rs17052920).
FT /FTId=VAR_052634.
FT CONFLICT 30 31 TT -> SS (in Ref. 1; CAA47919).
FT CONFLICT 46 46 E -> V (in Ref. 1; CAA47919).
FT CONFLICT 224 230 LCKAFGQ -> AVQGLCE (in Ref. 9; AA
FT sequence).
FT CONFLICT 366 366 E -> G (in Ref. 4; BAG56942).
FT CONFLICT 426 426 P -> A (in Ref. 1; CAA47919).
FT CONFLICT 585 587 THL -> KTM (in Ref. 2; AAA61222).
FT CONFLICT 608 623 DRDAIAQAVRGLITKA -> TGMPLHKL (in Ref. 9;
FT AA sequence).
FT HELIX 9 33
FT HELIX 38 42
FT HELIX 45 53
FT STRAND 70 75
FT HELIX 76 78
FT HELIX 79 88
FT HELIX 94 99
FT HELIX 128 141
FT STRAND 149 155
FT HELIX 156 159
FT HELIX 161 172
FT STRAND 178 184
FT STRAND 189 192
FT TURN 194 197
FT HELIX 199 208
FT STRAND 212 217
FT HELIX 221 229
FT STRAND 236 241
FT TURN 244 247
FT TURN 249 253
FT HELIX 264 275
FT STRAND 314 316
FT HELIX 317 331
FT STRAND 335 341
FT HELIX 343 346
FT HELIX 349 354
FT HELIX 356 358
FT STRAND 359 361
FT HELIX 366 377
FT HELIX 378 380
FT STRAND 383 389
FT HELIX 390 396
FT HELIX 397 405
FT STRAND 410 418
FT HELIX 419 421
FT HELIX 426 428
FT STRAND 430 432
FT HELIX 433 438
FT STRAND 443 446
FT HELIX 451 462
FT STRAND 466 471
FT STRAND 474 478
FT STRAND 493 496
FT STRAND 501 506
FT HELIX 510 523
FT TURN 524 526
FT STRAND 528 533
FT STRAND 535 539
FT HELIX 542 551
FT TURN 552 554
FT STRAND 555 564
FT HELIX 568 576
FT STRAND 583 589
FT HELIX 598 604
FT HELIX 609 620
SQ SEQUENCE 623 AA; 67878 MW; 176C89C02FD2712B CRC64;
MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS
QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA
ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI
ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE
LLKMFGIDRD AIAQAVRGLI TKA
//
MIM
606781
*RECORD*
*FIELD* NO
606781
*FIELD* TI
*606781 TRANSKETOLASE; TKT
;;TKT1
*FIELD* TX
BIOCHEMICAL FEATURES
Transketolase (EC 2.2.1.1) is a thiamine-dependent enzyme that links the
read morepentose phosphate pathway with the glycolytic pathway. The pentose
phosphate pathway, which is active in most tissues, provides sugar
phosphates for intermediary biosynthesis, especially nucleotide
metabolism, and generates the biosynthetic reducing power for the cell
in the form of NADPH. Transketolase is directly involved in the branch
of the pathway that channels excess sugar phosphates to glycolysis,
enabling the production of NADPH to be maintained under different
metabolic conditions. NADPH is critical for maintaining cerebral
glutathione, and thus it is likely that transketolase plays an important
role in brain metabolism.
CLONING
Abedinia et al. (1992) cloned a cDNA encoding transketolase from a human
brain cDNA library. The library was screened with oligonucleotide probes
based on the amino acid sequence of proteolytic fragments of the
purified protein. Northern blot analysis showed that the transketolase
mRNA is approximately 2.2 kb.
GENE STRUCTURE
McCool et al. (1993) isolated transketolase cDNA clones and concluded
that the gene is present in single copy in the haploid genome.
MAPPING
Using a 10-kb genomic clone in fluorescence in situ hybridization,
Lapsys et al. (1992) mapped the TKT gene to chromosome 3p14 at a site
distal to the fragile site designated FRA3B (601153). TKT is therefore
located at 3p14.3. Southern blot analysis of a series of rodent/human
hybrid cell lines corroborated the localization.
Coy et al. (1996) identified a transketolase-related gene (TKTL1;
300044) located in Xq28.
ANIMAL MODEL
Xu et al. (2002) found that Tkt-null mouse embryos died at or before the
morula stage. Disruption of 1 Tkt allele caused overall growth
retardation and a specific reduction in adipose tissue. No phenotype was
observed in Tkt +/- cornea, where Tkt expression was especially abundant
in wildtype mice. The small female Tkt +/- mice mated infrequently and
had few progeny when pregnant.
*FIELD* RF
1. Abedinia, M.; Layfield, R.; Jones, S. M.; Nixon, P. F.; Mattick,
J. S.: Nucleotide and predicted amino acid sequence of a cDNA clone
encoding part of human transketolase. Biochem. Biophys. Res. Commun. 183:
1159-1166, 1992.
2. Coy, J. F.; Dubel, S.; Kioschis, P.; Thomas, K.; Micklem, G.; Delius,
H.; Poustka, A.: Molecular cloning of tissue-specific transcripts
of a transketolase-related gene: implications for the evolution of
new vertebrate genes. Genomics 32: 309-316, 1996.
3. Lapsys, N. M.; Layfield, R.; Baker, E.; Callen, D. F.; Sutherland,
G. R.; Abedinia, M.; Nixon, P. F.; Mattick, J. S.: Chromosomal location
of the human transketolase gene. Cytogenet. Cell Genet. 61: 274-275,
1992.
4. McCool, B. A.; Plonk, S. G.; Martin, P. R.; Singleton, C. K.:
Cloning of human transketolase cDNAs and comparison of the nucleotide
sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff
individuals. J. Biol. Chem. 268: 1397-1404, 1993.
5. Xu, Z.-P.; Wawrousek, E. F.; Piatigorsky, J.: Transketolase haploinsufficiency
reduces adipose tissue and female fertility in mice. Molec. Cell.
Biol. 22: 6142-6147, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 9/1/2006
*FIELD* CD
Cassandra L. Kniffin: 3/22/2002
*FIELD* ED
mgross: 09/07/2006
terry: 9/1/2006
carol: 3/25/2002
ckniffin: 3/22/2002
*RECORD*
*FIELD* NO
606781
*FIELD* TI
*606781 TRANSKETOLASE; TKT
;;TKT1
*FIELD* TX
BIOCHEMICAL FEATURES
Transketolase (EC 2.2.1.1) is a thiamine-dependent enzyme that links the
read morepentose phosphate pathway with the glycolytic pathway. The pentose
phosphate pathway, which is active in most tissues, provides sugar
phosphates for intermediary biosynthesis, especially nucleotide
metabolism, and generates the biosynthetic reducing power for the cell
in the form of NADPH. Transketolase is directly involved in the branch
of the pathway that channels excess sugar phosphates to glycolysis,
enabling the production of NADPH to be maintained under different
metabolic conditions. NADPH is critical for maintaining cerebral
glutathione, and thus it is likely that transketolase plays an important
role in brain metabolism.
CLONING
Abedinia et al. (1992) cloned a cDNA encoding transketolase from a human
brain cDNA library. The library was screened with oligonucleotide probes
based on the amino acid sequence of proteolytic fragments of the
purified protein. Northern blot analysis showed that the transketolase
mRNA is approximately 2.2 kb.
GENE STRUCTURE
McCool et al. (1993) isolated transketolase cDNA clones and concluded
that the gene is present in single copy in the haploid genome.
MAPPING
Using a 10-kb genomic clone in fluorescence in situ hybridization,
Lapsys et al. (1992) mapped the TKT gene to chromosome 3p14 at a site
distal to the fragile site designated FRA3B (601153). TKT is therefore
located at 3p14.3. Southern blot analysis of a series of rodent/human
hybrid cell lines corroborated the localization.
Coy et al. (1996) identified a transketolase-related gene (TKTL1;
300044) located in Xq28.
ANIMAL MODEL
Xu et al. (2002) found that Tkt-null mouse embryos died at or before the
morula stage. Disruption of 1 Tkt allele caused overall growth
retardation and a specific reduction in adipose tissue. No phenotype was
observed in Tkt +/- cornea, where Tkt expression was especially abundant
in wildtype mice. The small female Tkt +/- mice mated infrequently and
had few progeny when pregnant.
*FIELD* RF
1. Abedinia, M.; Layfield, R.; Jones, S. M.; Nixon, P. F.; Mattick,
J. S.: Nucleotide and predicted amino acid sequence of a cDNA clone
encoding part of human transketolase. Biochem. Biophys. Res. Commun. 183:
1159-1166, 1992.
2. Coy, J. F.; Dubel, S.; Kioschis, P.; Thomas, K.; Micklem, G.; Delius,
H.; Poustka, A.: Molecular cloning of tissue-specific transcripts
of a transketolase-related gene: implications for the evolution of
new vertebrate genes. Genomics 32: 309-316, 1996.
3. Lapsys, N. M.; Layfield, R.; Baker, E.; Callen, D. F.; Sutherland,
G. R.; Abedinia, M.; Nixon, P. F.; Mattick, J. S.: Chromosomal location
of the human transketolase gene. Cytogenet. Cell Genet. 61: 274-275,
1992.
4. McCool, B. A.; Plonk, S. G.; Martin, P. R.; Singleton, C. K.:
Cloning of human transketolase cDNAs and comparison of the nucleotide
sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff
individuals. J. Biol. Chem. 268: 1397-1404, 1993.
5. Xu, Z.-P.; Wawrousek, E. F.; Piatigorsky, J.: Transketolase haploinsufficiency
reduces adipose tissue and female fertility in mice. Molec. Cell.
Biol. 22: 6142-6147, 2002.
*FIELD* CN
Patricia A. Hartz - updated: 9/1/2006
*FIELD* CD
Cassandra L. Kniffin: 3/22/2002
*FIELD* ED
mgross: 09/07/2006
terry: 9/1/2006
carol: 3/25/2002
ckniffin: 3/22/2002