ID THIL_HUMAN Reviewed; 427 AA. AC P24752; B2R6H1; G3XAB4; Q96FG8; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 11-NOV-2015, entry version 171. DE RecName: Full=Acetyl-CoA acetyltransferase, mitochondrial; DE EC=2.3.1.9; DE AltName: Full=Acetoacetyl-CoA thiolase; DE AltName: Full=T2; DE Flags: Precursor; GN Name=ACAT1; Synonyms=ACAT, MAT; 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). RX PubMed=1979337; DOI=10.1172/JCI114946; RA Fukao T., Yamaguchi S., Kano M., Orii T., Fujiki Y., Osumi T., RA Hashimoto T.; RT "Molecular cloning and sequence of the complementary DNA encoding RT human mitochondrial acetoacetyl-coenzyme A thiolase and study of the RT variant enzymes in cultured fibroblasts from patients with 3- RT ketothiolase deficiency."; RL J. Clin. Invest. 86:2086-2092(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1684944; DOI=10.1016/0378-1119(91)90623-J; RA Kano M., Fukao T., Yamaguchi S., Orii T., Osumi T., Hashimoto T.; RT "Structure and expression of the human mitochondrial acetoacetyl-CoA RT thiolase-encoding gene."; RL Gene 109:285-290(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-5. RC TISSUE=Brain; 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 [7] RP PROTEIN SEQUENCE OF 50-78 AND 312-338. RC TISSUE=Adipocyte; RX PubMed=15242332; DOI=10.1042/BJ20040647; RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.; RT "Vectorial proteomics reveal targeting, phosphorylation and specific RT fragmentation of polymerase I and transcript release factor (PTRF) at RT the surface of caveolae in human adipocytes."; RL Biochem. J. 383:237-248(2004). RN [8] RP PROTEIN SEQUENCE OF 50-78 AND 231-243, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174; LYS-181; LYS-251 AND RP LYS-263, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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 [11] 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 35-427 IN COMPLEX WITH RP COENZYME A AND POTASSIUM, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, RP CATALYTIC ACTIVITY, AND ENZYME REGULATION. RX PubMed=17371050; DOI=10.1021/bi6026192; RA Haapalainen A.M., Merilaeinen G., Pirilae P.L., Kondo N., Fukao T., RA Wierenga R.K.; RT "Crystallographic and kinetic studies of human mitochondrial RT acetoacetyl-CoA thiolase: the importance of potassium and chloride RT ions for its structure and function."; RL Biochemistry 46:4305-4321(2007). RN [15] RP REVIEW ON 3KTD VARIANTS. RX PubMed=7749408; DOI=10.1002/humu.1380050203; RA Fukao T., Yamaguchi S., Orii T., Hashimoto T.; RT "Molecular basis of beta-ketothiolase deficiency: mutations and RT polymorphisms in the human mitochondrial acetoacetyl-coenzyme A RT thiolase gene."; RL Hum. Mutat. 5:113-120(1995). RN [16] RP VARIANT 3KTD ARG-183. RX PubMed=1346617; DOI=10.1172/JCI115608; RA Fukao T., Yamaguchi S., Orii T., Schutgens R.B.H., Osumi T., RA Hashimoto T.; RT "Identification of three mutant alleles of the gene for mitochondrial RT acetoacetyl-coenzyme A thiolase. A complete analysis of two RT generations of a family with 3-ketothiolase deficiency."; RL J. Clin. Invest. 89:474-479(1992). RN [17] RP VARIANT 3KTD THR-380. RX PubMed=1715688; DOI=10.1016/0006-291X(91)91343-B; RA Fukao T., Yamaguchi S., Tomatsu S., Orii T., Frauendienst-Egger G., RA Schrod L., Osumi T., Hashimoto T.; RT "Evidence for a structural mutation (347Ala to Thr) in a German family RT with 3-ketothiolase deficiency."; RL Biochem. Biophys. Res. Commun. 179:124-129(1991). RN [18] RP VARIANTS 3KTD ASP-158; MET-297 AND PRO-301. RX PubMed=7728148; DOI=10.1002/humu.1380050105; RA Wakazono A., Fukao T., Yamaguchi S., Hori T., Orii T., Lambert M., RA Mitchell G.A., Lee G.W., Hashimoto T.; RT "Molecular, biochemical, and clinical characterization of RT mitochondrial acetoacetyl-coenzyme A thiolase deficiency in two RT further patients."; RL Hum. Mutat. 5:34-42(1995). RN [19] RP VARIANTS 3KTD SER-93; THR-312 AND PRO-333. RX PubMed=9744475; RX DOI=10.1002/(SICI)1098-1004(1998)12:4<245::AID-HUMU5>3.0.CO;2-E; RA Fukao T., Nakamura H., Song X.-Q., Nakamura K., Orii K.E., Kohno Y., RA Kano M., Yamaguchi S., Hashimoto T., Orii T., Kondo N.; RT "Characterization of N93S, I312T, and A333P missense mutations in two RT Japanese families with mitochondrial acetoacetyl-CoA thiolase RT deficiency."; RL Hum. Mutat. 12:245-254(1998). CC -!- FUNCTION: Plays a major role in ketone body metabolism. CC -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA. CC {ECO:0000255|PROSITE-ProRule:PRU10020, CC ECO:0000269|PubMed:17371050}. CC -!- ENZYME REGULATION: Activated by potassium ions, but not sodium CC ions. {ECO:0000269|PubMed:17371050}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4 uM for acetoacetyl coenzyme A CC {ECO:0000269|PubMed:17371050}; CC KM=20 uM for coenzyme A {ECO:0000269|PubMed:17371050}; CC KM=8 uM for 2-methylacetoacetyl coenzyme A CC {ECO:0000269|PubMed:17371050}; CC KM=508 uM for acetyl coenzyme A {ECO:0000269|PubMed:17371050}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17371050}. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P24752-1; Sequence=Displayed; CC Name=2; CC IsoId=P24752-2; Sequence=VSP_056844, VSP_056845; CC Note=No experimental confirmation available.; CC -!- PTM: Succinylation at Lys-268, adjacent to a coenzyme A binding CC site. Desuccinylated by SIRT5 (By similarity). {ECO:0000250}. CC -!- DISEASE: 3-ketothiolase deficiency (3KTD) [MIM:203750]: An inborn CC error of isoleucine catabolism characterized by intermittent CC ketoacidotic attacks associated with unconsciousness. Some CC patients die during an attack or are mentally retarded. Urinary CC excretion of 2-methyl-3-hydroxybutyric acid, 2-methylacetoacetic CC acid, triglylglycine, butanone is increased. It seems likely that CC the severity of this disease correlates better with the CC environmental or acquired factors than with the ACAT1 genotype. CC {ECO:0000269|PubMed:1346617, ECO:0000269|PubMed:1715688, CC ECO:0000269|PubMed:7728148, ECO:0000269|PubMed:9744475}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D90228; BAA14278.1; -; mRNA. DR EMBL; D10511; BAA01387.1; -; Genomic_DNA. DR EMBL; AK312574; BAG35468.1; -; mRNA. DR EMBL; AP002433; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67104.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67105.1; -; Genomic_DNA. DR EMBL; BC010942; AAH10942.1; -; mRNA. DR CCDS; CCDS8339.1; -. [P24752-1] DR PIR; JH0255; JH0255. DR RefSeq; NP_000010.1; NM_000019.3. [P24752-1] DR UniGene; Hs.232375; -. DR PDB; 2F2S; X-ray; 2.00 A; A/B/C/D=41-427. DR PDB; 2IB7; X-ray; 2.05 A; A/B/C/D=34-427. DR PDB; 2IB8; X-ray; 1.85 A; A/B/C/D=34-427. DR PDB; 2IB9; X-ray; 2.05 A; A/B/C/D=34-427. DR PDB; 2IBU; X-ray; 1.90 A; A/B/C/D=34-427. DR PDB; 2IBW; X-ray; 1.90 A; A/B/C/D=34-427. DR PDB; 2IBY; X-ray; 1.85 A; A/B/C/D=34-427. DR PDBsum; 2F2S; -. DR PDBsum; 2IB7; -. DR PDBsum; 2IB8; -. DR PDBsum; 2IB9; -. DR PDBsum; 2IBU; -. DR PDBsum; 2IBW; -. DR PDBsum; 2IBY; -. DR ProteinModelPortal; P24752; -. DR SMR; P24752; 35-427. DR BioGrid; 106556; 38. DR IntAct; P24752; 4. DR MINT; MINT-5000530; -. DR STRING; 9606.ENSP00000265838; -. DR BindingDB; P24752; -. DR ChEMBL; CHEMBL2616; -. DR DrugBank; DB00795; Sulfasalazine. DR PhosphoSite; P24752; -. DR BioMuta; ACAT1; -. DR DMDM; 135755; -. DR REPRODUCTION-2DPAGE; IPI00030363; -. DR UCD-2DPAGE; P24752; -. DR MaxQB; P24752; -. DR PaxDb; P24752; -. DR PeptideAtlas; P24752; -. DR PRIDE; P24752; -. DR DNASU; 38; -. DR Ensembl; ENST00000265838; ENSP00000265838; ENSG00000075239. [P24752-1] DR Ensembl; ENST00000299355; ENSP00000299355; ENSG00000075239. [P24752-2] DR GeneID; 38; -. DR KEGG; hsa:38; -. DR UCSC; uc001pjw.1; human. DR UCSC; uc001pjy.3; human. [P24752-1] DR CTD; 38; -. DR GeneCards; ACAT1; -. DR HGNC; HGNC:93; ACAT1. DR HPA; HPA004428; -. DR HPA; HPA007569; -. DR MIM; 203750; phenotype. DR MIM; 607809; gene. DR neXtProt; NX_P24752; -. DR Orphanet; 134; Ketoacidosis due to beta-ketothiolase deficiency. DR PharmGKB; PA24431; -. DR eggNOG; KOG1390; Eukaryota. DR eggNOG; COG0183; LUCA. DR GeneTree; ENSGT00390000009412; -. DR HOGENOM; HOG000012238; -. DR HOVERGEN; HBG003112; -. DR InParanoid; P24752; -. DR KO; K00626; -. DR OMA; APVGAMN; -. DR OrthoDB; EOG7JQBNG; -. DR PhylomeDB; P24752; -. DR TreeFam; TF300650; -. DR BioCyc; MetaCyc:HS01167-MONOMER; -. DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism. DR Reactome; R-HSA-77108; Utilization of Ketone Bodies. DR Reactome; R-HSA-77111; Synthesis of Ketone Bodies. DR ChiTaRS; ACAT1; human. DR EvolutionaryTrace; P24752; -. DR GeneWiki; ACAT1; -. DR GenomeRNAi; 38; -. DR NextBio; 149; -. DR PRO; PR:P24752; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P24752; -. DR CleanEx; HS_ACAT1; -. DR ExpressionAtlas; P24752; baseline and differential. DR Genevisible; P24752; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; EXP:Reactome. DR GO; GO:0050662; F:coenzyme binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome. DR GO; GO:0046950; P:cellular ketone body metabolic process; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0046951; P:ketone body biosynthetic process; TAS:Reactome. DR GO; GO:0046952; P:ketone body catabolic process; TAS:Reactome. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0072229; P:metanephric proximal convoluted tubule development; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl. DR GO; GO:0009725; P:response to hormone; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.40.47.10; -; 4. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020610; Thiolase_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative splicing; KW Complete proteome; Direct protein sequencing; Disease mutation; KW Metal-binding; Mitochondrion; Polymorphism; Potassium; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1 33 Mitochondrion. {ECO:0000250}. FT CHAIN 34 427 Acetyl-CoA acetyltransferase, FT mitochondrial. FT /FTId=PRO_0000034085. FT REGION 258 260 Coenzyme A binding. FT ACT_SITE 126 126 Acyl-thioester intermediate. FT {ECO:0000305}. FT ACT_SITE 385 385 Proton acceptor. {ECO:0000305}. FT ACT_SITE 413 413 Proton acceptor. {ECO:0000305}. FT METAL 219 219 Potassium. {ECO:0000269|PubMed:17371050}. FT METAL 280 280 Potassium; via carbonyl oxygen. FT {ECO:0000269|PubMed:17371050}. FT METAL 281 281 Potassium; via carbonyl oxygen. FT {ECO:0000269|PubMed:17371050}. FT METAL 283 283 Potassium; via carbonyl oxygen. FT {ECO:0000269|PubMed:17371050}. FT METAL 381 381 Potassium; via carbonyl oxygen. FT {ECO:0000269|PubMed:17371050}. FT BINDING 219 219 Coenzyme A. FT {ECO:0000269|PubMed:17371050}. FT BINDING 263 263 Coenzyme A. FT {ECO:0000269|PubMed:17371050}. FT BINDING 284 284 Coenzyme A. FT {ECO:0000269|PubMed:17371050}. FT MOD_RES 66 66 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 66 66 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 78 78 N6-succinyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 174 174 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 174 174 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 181 181 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 181 181 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 190 190 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 190 190 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 202 202 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 202 202 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 223 223 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 223 223 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 230 230 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 230 230 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 243 243 N6-succinyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 251 251 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 257 257 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 263 263 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 263 263 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 266 266 N6-succinyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 268 268 N6-succinyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 273 273 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT MOD_RES 338 338 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q8QZT1}. FT VAR_SEQ 146 162 DVMVAGGMESMSNVPYV -> IKQETGSLAKICCHVRR FT (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056844. FT VAR_SEQ 163 427 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056845. FT VARIANT 5 5 A -> P (in dbSNP:rs3741056). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_007496. FT VARIANT 85 85 Missing (in 3KTD). FT /FTId=VAR_007497. FT VARIANT 93 93 N -> S (in 3KTD; 10% activity). FT {ECO:0000269|PubMed:9744475}. FT /FTId=VAR_007498. FT VARIANT 152 152 G -> A (in 3KTD). FT /FTId=VAR_007499. FT VARIANT 158 158 N -> D (in 3KTD; no activity). FT {ECO:0000269|PubMed:7728148}. FT /FTId=VAR_007500. FT VARIANT 183 183 G -> R (in 3KTD; no activity). FT {ECO:0000269|PubMed:1346617}. FT /FTId=VAR_007501. FT VARIANT 297 297 T -> M (in 3KTD; 10% normal activity). FT {ECO:0000269|PubMed:7728148}. FT /FTId=VAR_007502. FT VARIANT 301 301 A -> P (in 3KTD; 5% normal activity). FT {ECO:0000269|PubMed:7728148}. FT /FTId=VAR_007503. FT VARIANT 312 312 I -> T (in 3KTD; 10% activity). FT {ECO:0000269|PubMed:9744475}. FT /FTId=VAR_007504. FT VARIANT 333 333 A -> P (in 3KTD; no activity). FT {ECO:0000269|PubMed:9744475}. FT /FTId=VAR_007505. FT VARIANT 379 379 G -> V (in 3KTD). FT /FTId=VAR_007506. FT VARIANT 380 380 A -> T (in 3KTD; 7% normal activity). FT {ECO:0000269|PubMed:1715688}. FT /FTId=VAR_007507. FT CONFLICT 340 340 V -> M (in Ref. 2; BAA01387). FT {ECO:0000305}. FT CONFLICT 346 346 D -> N (in Ref. 2; BAA01387). FT {ECO:0000305}. FT CONFLICT 380 380 A -> S (in Ref. 2; BAA01387). FT {ECO:0000305}. FT CONFLICT 412 412 I -> F (in Ref. 2; BAA01387). FT {ECO:0000305}. FT STRAND 42 49 {ECO:0000244|PDB:2IB8}. FT TURN 58 61 {ECO:0000244|PDB:2IB8}. FT HELIX 64 79 {ECO:0000244|PDB:2IB8}. FT HELIX 83 85 {ECO:0000244|PDB:2IB8}. FT STRAND 88 92 {ECO:0000244|PDB:2IB8}. FT HELIX 103 110 {ECO:0000244|PDB:2IB8}. FT STRAND 119 123 {ECO:0000244|PDB:2IB8}. FT HELIX 125 127 {ECO:0000244|PDB:2IB8}. FT HELIX 128 141 {ECO:0000244|PDB:2IB8}. FT STRAND 146 155 {ECO:0000244|PDB:2IB8}. FT HELIX 156 158 {ECO:0000244|PDB:2IB8}. FT STRAND 161 163 {ECO:0000244|PDB:2IB8}. FT STRAND 165 167 {ECO:0000244|PDB:2IB8}. FT STRAND 173 177 {ECO:0000244|PDB:2IB8}. FT HELIX 178 182 {ECO:0000244|PDB:2IB8}. FT TURN 187 190 {ECO:0000244|PDB:2IB8}. FT HELIX 193 204 {ECO:0000244|PDB:2IB8}. FT HELIX 208 227 {ECO:0000244|PDB:2IB8}. FT TURN 228 234 {ECO:0000244|PDB:2IB8}. FT STRAND 238 240 {ECO:0000244|PDB:2IB8}. FT STRAND 248 250 {ECO:0000244|PDB:2IB8}. FT HELIX 255 257 {ECO:0000244|PDB:2IB8}. FT TURN 261 263 {ECO:0000244|PDB:2IB8}. FT HELIX 264 266 {ECO:0000244|PDB:2IB8}. FT STRAND 273 275 {ECO:0000244|PDB:2IB8}. FT TURN 280 282 {ECO:0000244|PDB:2IB8}. FT STRAND 287 297 {ECO:0000244|PDB:2IB8}. FT HELIX 298 303 {ECO:0000244|PDB:2IB8}. FT STRAND 310 319 {ECO:0000244|PDB:2IB8}. FT HELIX 322 327 {ECO:0000244|PDB:2IB8}. FT HELIX 328 340 {ECO:0000244|PDB:2IB8}. FT HELIX 344 346 {ECO:0000244|PDB:2IB8}. FT STRAND 347 352 {ECO:0000244|PDB:2IB8}. FT HELIX 357 367 {ECO:0000244|PDB:2IB8}. FT HELIX 371 373 {ECO:0000244|PDB:2IB8}. FT HELIX 380 383 {ECO:0000244|PDB:2IB8}. FT TURN 387 389 {ECO:0000244|PDB:2IB8}. FT HELIX 390 401 {ECO:0000244|PDB:2IB8}. FT STRAND 407 414 {ECO:0000244|PDB:2IB8}. FT TURN 415 417 {ECO:0000244|PDB:2IB8}. FT STRAND 418 426 {ECO:0000244|PDB:2IB8}. SQ SEQUENCE 427 AA; 45200 MW; 2E81168EB39D0142 CRC64; MAVLAALLRS GARSRSPLLR RLVQEIRYVE RSYVSKPTLK EVVIVSATRT PIGSFLGSLS LLPATKLGSI AIQGAIEKAG IPKEEVKEAY MGNVLQGGEG QAPTRQAVLG AGLPISTPCT TINKVCASGM KAIMMASQSL MCGHQDVMVA GGMESMSNVP YVMNRGSTPY GGVKLEDLIV KDGLTDVYNK IHMGSCAENT AKKLNIARNE QDAYAINSYT RSKAAWEAGK FGNEVIPVTV TVKGQPDVVV KEDEEYKRVD FSKVPKLKTV FQKENGTVTA ANASTLNDGA AALVLMTADA AKRLNVTPLA RIVAFADAAV EPIDFPIAPV YAASMVLKDV GLKKEDIAMW EVNEAFSLVV LANIKMLEID PQKVNINGGA VSLGHPIGMS GARIVGHLTH ALKQGEYGLA SICNGGGGAS AMLIQKL //