TKTL1_HUMAN
ID TKTL1_HUMAN Reviewed; 596 AA.
AC P51854; A8K896; Q5TYJ8; Q5TYJ9; Q8TC75;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Transketolase-like protein 1;
DE EC=2.2.1.1;
DE AltName: Full=Transketolase 2;
DE Short=TK 2;
DE AltName: Full=Transketolase-related protein;
GN Name=TKTL1; Synonyms=TKR, TKT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=8838793; DOI=10.1006/geno.1996.0124;
RA Coy J.F., Duebel S., Kioschis P., Thomas K., Micklem G., Delius H.,
RA Poustka A.;
RT "Molecular cloning of tissue-specific transcripts of a transketolase-
RT related gene: implications for the evolution of new vertebrate genes.";
RL Genomics 32:309-316(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-24.
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS PHE-24 AND
RP THR-152.
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-537 (ISOFORMS 1/2).
RA Hochgeschwender U.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15991799;
RA Coy J.F., Dressler D., Wilde J., Schubert P.;
RT "Mutations in the transketolase-like gene TKTL1: clinical implications for
RT neurodegenerative diseases, diabetes and cancer.";
RL Clin. Lab. 51:257-273(2005).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16465194; DOI=10.1038/sj.bjc.6602962;
RA Langbein S., Zerilli M., Zur Hausen A., Staiger W., Rensch-Boschert K.,
RA Lukan N., Popa J., Ternullo M.P., Steidler A., Weiss C., Grobholz R.,
RA Willeke F., Alken P., Stassi G., Schubert P., Coy J.F.;
RT "Expression of transketolase TKTL1 predicts colon and urothelial cancer
RT patient survival: Warburg effect reinterpreted.";
RL Br. J. Cancer 94:578-585(2006).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16969476;
RA Staiger W.I., Coy J.F., Grobholz R., Hofheinz R.-D., Lukan N., Post S.,
RA Schwarzbach M.H., Willeke F.;
RT "Expression of the mutated transketolase TKTL1, a molecular marker in
RT gastric cancer.";
RL Oncol. Rep. 16:657-661(2006).
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 Evidence={ECO:0000269|PubMed:15991799};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16465194,
CC ECO:0000269|PubMed:16969476}. Nucleus {ECO:0000269|PubMed:16465194,
CC ECO:0000269|PubMed:16969476}. Note=Predominantly cytoplasmic and to a
CC lesser extent also nuclear (PubMed:16969476).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=3;
CC IsoId=P51854-3; Sequence=Displayed;
CC Name=2; Synonyms=Brain specific;
CC IsoId=P51854-1; Sequence=VSP_022290, VSP_022291;
CC Name=1; Synonyms=Heart specific;
CC IsoId=P51854-2; Sequence=Not described;
CC Name=4;
CC IsoId=P51854-4; Sequence=VSP_022290;
CC -!- TISSUE SPECIFICITY: Expressed in fetal and adult heart, brain, lung,
CC liver, and kidney, and in adult placenta, skeletal muscle and pancreas.
CC Up-regulated in various epithelial tumors.
CC {ECO:0000269|PubMed:15991799, ECO:0000269|PubMed:16465194,
CC ECO:0000269|PubMed:16969476, ECO:0000269|PubMed:8838793}.
CC -!- MISCELLANEOUS: Strong TKTL1 protein expression has been correlated with
CC a certain type of glucose metabolism (aerobic glycolysis; Warburg
CC effect) and to cells which are affected by chronic complications of
CC diabetic patients.
CC -!- MISCELLANEOUS: [Isoform 1]: Lacks the N-terminal. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; X91817; CAA62925.1; -; mRNA.
DR EMBL; X91818; CAA62925.1; JOINED; mRNA.
DR EMBL; AK292261; BAF84950.1; -; mRNA.
DR EMBL; BX664723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z49258; CAH69899.1; -; Genomic_DNA.
DR EMBL; Z49258; CAH69900.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72752.1; -; Genomic_DNA.
DR EMBL; BC025382; AAH25382.2; -; mRNA.
DR EMBL; U14622; AAA21557.1; -; Genomic_DNA.
DR CCDS; CCDS35448.1; -. [P51854-3]
DR CCDS; CCDS55541.1; -. [P51854-4]
DR RefSeq; NP_001139406.1; NM_001145934.1. [P51854-4]
DR RefSeq; NP_036385.3; NM_012253.3. [P51854-3]
DR AlphaFoldDB; P51854; -.
DR SMR; P51854; -.
DR BioGRID; 113890; 14.
DR IntAct; P51854; 6.
DR STRING; 9606.ENSP00000358931; -.
DR DrugCentral; P51854; -.
DR iPTMnet; P51854; -.
DR PhosphoSitePlus; P51854; -.
DR BioMuta; TKTL1; -.
DR DMDM; 122066426; -.
DR jPOST; P51854; -.
DR MassIVE; P51854; -.
DR PaxDb; P51854; -.
DR PeptideAtlas; P51854; -.
DR PRIDE; P51854; -.
DR ProteomicsDB; 56434; -. [P51854-3]
DR ProteomicsDB; 56435; -. [P51854-1]
DR ProteomicsDB; 65205; -.
DR Antibodypedia; 17549; 69 antibodies from 22 providers.
DR DNASU; 8277; -.
DR Ensembl; ENST00000369912.2; ENSP00000358928.2; ENSG00000007350.17. [P51854-4]
DR Ensembl; ENST00000369915.8; ENSP00000358931.3; ENSG00000007350.17. [P51854-3]
DR GeneID; 8277; -.
DR KEGG; hsa:8277; -.
DR MANE-Select; ENST00000369915.8; ENSP00000358931.3; NM_012253.4; NP_036385.3.
DR UCSC; uc004fkg.4; human. [P51854-3]
DR CTD; 8277; -.
DR DisGeNET; 8277; -.
DR GeneCards; TKTL1; -.
DR HGNC; HGNC:11835; TKTL1.
DR HPA; ENSG00000007350; Tissue enriched (testis).
DR MIM; 300044; gene.
DR neXtProt; NX_P51854; -.
DR OpenTargets; ENSG00000007350; -.
DR PharmGKB; PA36538; -.
DR VEuPathDB; HostDB:ENSG00000007350; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000162426; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; P51854; -.
DR OMA; LTRAHDF; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; P51854; -.
DR TreeFam; TF313097; -.
DR BRENDA; 2.2.1.1; 2681.
DR PathwayCommons; P51854; -.
DR SABIO-RK; P51854; -.
DR SignaLink; P51854; -.
DR BioGRID-ORCS; 8277; 7 hits in 695 CRISPR screens.
DR ChiTaRS; TKTL1; human.
DR GeneWiki; TKTL1; -.
DR GenomeRNAi; 8277; -.
DR Pharos; P51854; Tbio.
DR PRO; PR:P51854; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51854; protein.
DR Bgee; ENSG00000007350; Expressed in right testis and 108 other tissues.
DR ExpressionAtlas; P51854; baseline and differential.
DR Genevisible; P51854; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; TAS:ProtInc.
DR GO; GO:0006772; P:thiamine metabolic process; TAS:ProtInc.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 2.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Magnesium; Metal-binding;
KW Nucleus; Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..596
FT /note="Transketolase-like protein 1"
FT /id="PRO_0000191899"
FT REGION 256..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 94..96
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 127
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 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 46
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8838793"
FT /id="VSP_022290"
FT VAR_SEQ 467
FT /note="K -> KGVSMLQDSWSSVISYQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8838793"
FT /id="VSP_022291"
FT VARIANT 24
FT /note="L -> F (in dbSNP:rs17855509)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15772651"
FT /id="VAR_029867"
FT VARIANT 152
FT /note="I -> T (in dbSNP:rs17852259)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029868"
FT CONFLICT 519
FT /note="I -> N (in Ref. 6; AAA21557)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> S (in Ref. 6; AAA21557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 65333 MW; F492A902441E2A14 CRC64;
MADAEARAEF PEEARPDRGT LQVLQDMASR LRIHSIRATC STSSGHPTSC SSSSEIMSVL
FFYIMRYKQS DPENPDNDRF VLAKRLSFVD VATGWLGQGL GVACGMAYTG KYFDRASYRV
FCLMSDGESS EGSVWEAMAF ASYYSLDNLV AIFDVNRLGH SGALPAEHCI NIYQRRCEAF
GWNTYVVDGR DVEALCQVFW QASQVKHKPT AVVAKTFKGR GTPSIEDAES WHAKPMPRER
ADAIIKLIES QIQTSRNLDP QPPIEDSPEV NITDVRMTSP PDYRVGDKIA TRKACGLALA
KLGYANNRVV VLDGDTRYST FSEIFNKEYP ERFIECFMAE QNMVSVALGC ASRGRTIAFA
STFAAFLTRA FDHIRIGGLA ESNINIIGSH CGVSVGDDGA SQMALEDIAM FRTIPKCTIF
YPTDAVSTEH AVALAANAKG MCFIRTTRPE TMVIYTPQER FEIGQAKVLR HCVSDKVTVI
GAGITVYEAL AAADELSKQD IFIRVIDLFT IKPLDVATIV SSAKATEGRI ITVEDHYPQG
GIGEAVCAAV SMDPDIQVHS LAVSGVPQSG KSEELLDMYG ISARHIIVAV KCMLLN
