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   07-APR-2021, entry version 180.
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   SMR; P51854; -.
DR   BioGRID; 113890; 7.
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; 67 antibodies.
DR   DNASU; 8277; -.
DR   Ensembl; ENST00000369912; ENSP00000358928; ENSG00000007350. [P51854-4]
DR   Ensembl; ENST00000369915; ENSP00000358931; ENSG00000007350. [P51854-3]
DR   GeneID; 8277; -.
DR   KEGG; hsa:8277; -.
DR   UCSC; uc004fkg.4; human. [P51854-3]
DR   CTD; 8277; -.
DR   DisGeNET; 8277; -.
DR   GeneCards; TKTL1; -.
DR   HGNC; HGNC:11835; TKTL1.
DR   HPA; ENSG00000007350; Group enriched (blood, testis).
DR   MIM; 300044; gene.
DR   neXtProt; NX_P51854; -.
DR   OpenTargets; ENSG00000007350; -.
DR   PharmGKB; PA36538; -.
DR   VEuPathDB; HostDB:ENSG00000007350.16; -.
DR   eggNOG; KOG0523; Eukaryota.
DR   GeneTree; ENSGT00940000162426; -.
DR   HOGENOM; CLU_009227_3_0_1; -.
DR   InParanoid; P51854; -.
DR   OMA; YALQQTD; -.
DR   OrthoDB; 354970at2759; -.
DR   PhylomeDB; P51854; -.
DR   TreeFam; TF313097; -.
DR   BRENDA; 2.2.1.1; 2681.
DR   PathwayCommons; P51854; -.
DR   SABIO-RK; P51854; -.
DR   BioGRID-ORCS; 8277; 3 hits in 612 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 testis and 118 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   NP_BIND         94..96
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        340
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   METAL           126
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           156
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           158
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /note="Thiamine pyrophosphate; via amide nitrogen"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         402
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         448
FT                   /note="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
//