ID SCOT1_HUMAN Reviewed; 520 AA. AC P55809; B2R5V2; B7Z528; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 205. DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial {ECO:0000303|PubMed:10964512}; DE Short=SCOT {ECO:0000303|PubMed:10964512}; DE EC=2.8.3.5 {ECO:0000269|PubMed:10964512}; DE AltName: Full=3-oxoacid CoA-transferase 1; DE AltName: Full=Somatic-type succinyl-CoA:3-oxoacid CoA-transferase; DE Short=SCOT-s; DE AltName: Full=Succinyl-CoA:3-oxoacid CoA transferase; DE Flags: Precursor; GN Name=OXCT1; Synonyms=OXCT, SCOT; 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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Heart; RX PubMed=8751852; RA Kassovska-Bratinova S., Fukao T., Song X.-Q., Duncan A.M.V., Chen H.S., RA Robert M.-F., Perez-Cerda C., Ugarte M., Chartrand C., Vobecky S., RA Kondo N., Mitchell G.A.; RT "Succinyl CoA:3-oxoacid CoA transferase (SCOT): human cDNA cloning, human RT chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient RT patient."; RL Am. J. Hum. Genet. 59:519-528(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCOTD GLU-219; MET-221 AND RP GLU-324, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=10964512; DOI=10.1006/geno.2000.6282; RA Fukao T., Mitchell G.A., Song X.-Q., Nakamura H., Kassovska-Bratinova S., RA Orii K.E., Wraith J.E., Besley G., Wanders R.J.A., Niezen-Koning K.E., RA Berry G.T., Palmieri M., Kondo N.; RT "Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT RT gene, tertiary structural modeling of the human SCOT monomer, and RT characterization of three pathogenic mutations."; RL Genomics 68:144-151(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cerebellum, and Kidney; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 40-50. RC TISSUE=Colon; RA Reymond M.A., Sanchez J.-C., Hughes G.J., Riese J., Tortola S., RA Peinado M.A., Kirchner T., Hohenberger W., Hochstrasser D.F., RA Kockerling F.; RL Submitted (FEB-1997) to UniProtKB. RN [7] RP TISSUE SPECIFICITY. RX PubMed=9380443; DOI=10.1203/00006450-199710000-00013; RA Fukao T., Song X.Q., Mitchell G.A., Yamaguchi S., Sukegawa K., Orii T., RA Kondo N.; RT "Enzymes of ketone body utilization in human tissues: protein and messenger RT RNA levels of succinyl-coenzyme A (CoA):3-ketoacid CoA transferase and RT mitochondrial and cytosolic acetoacetyl-CoA thiolases."; RL Pediatr. Res. 42:498-502(1997). RN [8] RP PROTEIN SEQUENCE OF 84-104; 111-124; 147-173; 191-211; 391-418; 422-434 AND RP 501-511, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). 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., Buerckstuemmer T., RA 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]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA 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 [13] RP SUBUNIT. RX PubMed=23420214; DOI=10.1007/s10545-013-9589-z; RA Shafqat N., Kavanagh K.L., Sass J.O., Christensen E., Fukao T., Lee W.H., RA Oppermann U., Yue W.W.; RT "A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA RT transferase (SCOT) deficiency."; RL J. Inherit. Metab. Dis. 36:983-987(2013). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 40-520. RG Structural genomics consortium (SGC); RT "Crystal structure of human 3-oxoacid CoA transferase 1."; RL Submitted (AUG-2008) to the PDB data bank. RN [15] RP VARIANTS SCOTD GLU-133 AND PHE-456, AND VARIANT MET-58. RX PubMed=9671268; RX DOI=10.1002/(sici)1098-1004(1998)12:2<83::aid-humu2>3.0.co;2-p; RA Song X.-Q., Fukao T., Watanabe H., Shintaku H., Hirayama K., RA Kassovska-Bratinova S., Kondo N., Mitchell G.A.; RT "Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic RT mutations, V133E and C456F, in Japanese siblings."; RL Hum. Mutat. 12:83-88(1998). RN [16] RP VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468, RP VARIANT MET-58, AND CHARACTERIZATION OF VARIANTS SCOTD VAL-215; ASN-226; RP PRO-327; PHE-404; PRO-405 AND CYS-468. RX PubMed=21296660; DOI=10.1016/j.bbadis.2011.01.015; RA Fukao T., Sass J.O., Kursula P., Thimm E., Wendel U., Ficicioglu C., RA Monastiri K., Guffon N., Baric I., Zabot M.T., Kondo N.; RT "Clinical and molecular characterization of five patients with succinyl- RT CoA:3-ketoacid CoA transferase (SCOT) deficiency."; RL Biochim. Biophys. Acta 1812:619-624(2011). RN [17] RP VARIANT SCOTD PHE-245. RX PubMed=31073471; DOI=10.1055/s-0037-1604270; RA Zheng D.J., Hooper M., Spencer-Manzon M., Pierce R.W.; RT "A Case of Succinyl-CoA:3-Oxoacid CoA Transferase Deficiency Presenting RT with Severe Acidosis in a 14-Month-Old Female: Evidence for Pathogenicity RT of a Point Mutation in the OXCT1 Gene."; RL J. Pediatr. Intensive Care 7:62-66(2018). RN [18] RP VARIANTS SCOTD 124-ARG--ASN-520 DEL; LYS-270; ALA-280 AND MET-437. RX PubMed=33596448; DOI=10.1016/j.biochi.2021.02.003; RA Gruenert S.C., Foster W., Schumann A., Lund A., Pontes C., Roloff S., RA Weinhold N., Yue W.W., AlAsmari A., Obaid O.A., Faqeih E.A., Stuebbe L., RA Yamamoto R., Gemperle-Britschgi C., Walter M., Spiekerkoetter U., RA Mackinnon S., Sass J.O.; RT "Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare RT and potentially fatal metabolic disease."; RL Biochimie 183:55-62(2021). CC -!- FUNCTION: Key enzyme for ketone body catabolism. Catalyzes the first, CC rate-limiting step of ketone body utilization in extrahepatic tissues, CC by transferring coenzyme A (CoA) from a donor thiolester species CC (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces CC acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl- CC CoA thiolase into two acetyl-CoA molecules which enter the citric acid CC cycle for energy production (PubMed:10964512). Forms a dimeric enzyme CC where both of the subunits are able to form enzyme-CoA thiolester CC intermediates, but only one subunit is competent to transfer the CoA CC moiety to the acceptor carboxylate (3-oxo acid) and produce a new acyl- CC CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable CC anhydride species formed between the carboxylate groups of the enzyme CC and substrate (By similarity). {ECO:0000250|UniProtKB:Q29551, CC ECO:0000269|PubMed:10964512}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate; CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973, CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5; CC Evidence={ECO:0000269|PubMed:10964512}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565; CC Evidence={ECO:0000305|PubMed:10964512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetoacetate + succinyl-CoA = acetoacetyl-CoA + succinate; CC Xref=Rhea:RHEA:25480, ChEBI:CHEBI:13705, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57292; EC=2.8.3.5; CC Evidence={ECO:0000269|PubMed:10964512}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481; CC Evidence={ECO:0000269|PubMed:10964512}; CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA CC from succinyl-CoA: step 1/1. {ECO:0000305|PubMed:10964512}. CC -!- SUBUNIT: Homodimer (PubMed:10964512, PubMed:23420214). Only one subunit CC is competent to transfer the CoA moiety to the acceptor carboxylate (3- CC oxo acid) (By similarity). {ECO:0000250|UniProtKB:Q29551, CC ECO:0000269|PubMed:10964512, ECO:0000269|PubMed:23420214}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:B2GV06}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P55809-1; Sequence=Displayed; CC Name=2; CC IsoId=P55809-2; Sequence=VSP_056310; CC -!- TISSUE SPECIFICITY: Abundant in heart, followed in order by brain, CC kidney, skeletal muscle, and lung, whereas in liver it is undetectable. CC Expressed (at protein level) in all tissues (except in liver), most CC abundant in myocardium, then brain, kidney, adrenal glands, skeletal CC muscle and lung; also detectable in leukocytes and fibroblasts. CC {ECO:0000269|PubMed:9380443}. CC -!- DISEASE: Succinyl-CoA:3-oxoacid CoA transferase deficiency (SCOTD) CC [MIM:245050]: A disorder of ketone body metabolism, characterized by CC episodic ketoacidosis. Patients are usually asymptomatic between CC episodes. {ECO:0000269|PubMed:10964512, ECO:0000269|PubMed:21296660, CC ECO:0000269|PubMed:31073471, ECO:0000269|PubMed:33596448, CC ECO:0000269|PubMed:9671268}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family. CC {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; U62961; AAB07366.1; -; mRNA. DR EMBL; AB029576; BAB13733.1; -; Genomic_DNA. DR EMBL; AK298352; BAH12764.1; -; mRNA. DR EMBL; AK312327; BAG35249.1; -; mRNA. DR EMBL; AK315902; BAH14273.1; -; mRNA. DR EMBL; AC008817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC034222; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009001; AAH09001.1; -; mRNA. DR CCDS; CCDS3937.1; -. [P55809-1] DR RefSeq; NP_000427.1; NM_000436.3. [P55809-1] DR PDB; 3DLX; X-ray; 2.20 A; A/B/C/D=40-520. DR PDBsum; 3DLX; -. DR AlphaFoldDB; P55809; -. DR SMR; P55809; -. DR BioGRID; 111059; 120. DR IntAct; P55809; 30. DR MINT; P55809; -. DR STRING; 9606.ENSP00000196371; -. DR DrugBank; DB02731; Ethylmercurithiosalicylic acid. DR DrugBank; DB00139; Succinic acid. DR GlyGen; P55809; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55809; -. DR PhosphoSitePlus; P55809; -. DR SwissPalm; P55809; -. DR BioMuta; OXCT1; -. DR DMDM; 2492998; -. DR EPD; P55809; -. DR jPOST; P55809; -. DR MassIVE; P55809; -. DR MaxQB; P55809; -. DR PaxDb; 9606-ENSP00000196371; -. DR PeptideAtlas; P55809; -. DR ProteomicsDB; 56871; -. [P55809-1] DR ProteomicsDB; 6656; -. DR Pumba; P55809; -. DR Antibodypedia; 1558; 223 antibodies from 27 providers. DR DNASU; 5019; -. DR Ensembl; ENST00000196371.10; ENSP00000196371.5; ENSG00000083720.13. [P55809-1] DR Ensembl; ENST00000510634.5; ENSP00000423144.1; ENSG00000083720.13. [P55809-2] DR Ensembl; ENST00000512084.5; ENSP00000421143.1; ENSG00000083720.13. [P55809-2] DR GeneID; 5019; -. DR KEGG; hsa:5019; -. DR MANE-Select; ENST00000196371.10; ENSP00000196371.5; NM_000436.4; NP_000427.1. DR UCSC; uc003jmn.4; human. [P55809-1] DR AGR; HGNC:8527; -. DR CTD; 5019; -. DR DisGeNET; 5019; -. DR GeneCards; OXCT1; -. DR HGNC; HGNC:8527; OXCT1. DR HPA; ENSG00000083720; Tissue enhanced (heart). DR MalaCards; OXCT1; -. DR MIM; 245050; phenotype. DR MIM; 601424; gene. DR neXtProt; NX_P55809; -. DR OpenTargets; ENSG00000083720; -. DR Orphanet; 832; Succinyl-CoA:3-oxoacid CoA transferase deficiency. DR PharmGKB; PA32855; -. DR VEuPathDB; HostDB:ENSG00000083720; -. DR eggNOG; KOG3822; Eukaryota. DR GeneTree; ENSGT00390000009130; -. DR HOGENOM; CLU_019942_1_3_1; -. DR InParanoid; P55809; -. DR OMA; VKTMGQI; -. DR OrthoDB; 177109at2759; -. DR PhylomeDB; P55809; -. DR TreeFam; TF313991; -. DR BioCyc; MetaCyc:HS01447-MONOMER; -. DR BRENDA; 2.8.3.5; 2681. DR PathwayCommons; P55809; -. DR Reactome; R-HSA-77108; Utilization of Ketone Bodies. DR SignaLink; P55809; -. DR UniPathway; UPA00929; UER00894. DR BioGRID-ORCS; 5019; 16 hits in 1162 CRISPR screens. DR ChiTaRS; OXCT1; human. DR EvolutionaryTrace; P55809; -. DR GeneWiki; OXCT1; -. DR GenomeRNAi; 5019; -. DR Pharos; P55809; Tbio. DR PRO; PR:P55809; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P55809; Protein. DR Bgee; ENSG00000083720; Expressed in left ventricle myocardium and 205 other cell types or tissues. DR ExpressionAtlas; P55809; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0008260; F:succinyl-CoA:3-oxo-acid CoA-transferase activity; IMP:UniProtKB. DR GO; GO:0046950; P:cellular ketone body metabolic process; IMP:UniProtKB. DR GO; GO:0046952; P:ketone body catabolic process; IEA:Ensembl. DR GO; GO:0042182; P:ketone catabolic process; IEA:Ensembl. DR Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2. DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A. DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B. DR InterPro; IPR014388; 3-oxoacid_CoA-transferase. DR InterPro; IPR004165; CoA_trans_fam_I. DR InterPro; IPR004164; CoA_transf_AS. DR InterPro; IPR004163; CoA_transf_BS. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR NCBIfam; TIGR02429; pcaI_scoA_fam; 1. DR NCBIfam; TIGR02428; pcaJ_scoB_fam; 1. DR PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1. DR PANTHER; PTHR13707:SF30; SUCCINYL-COA:3-KETOACID COENZYME A TRANSFERASE 1, MITOCHONDRIAL; 1. DR Pfam; PF01144; CoA_trans; 2. DR PIRSF; PIRSF000858; SCOT-t; 1. DR SMART; SM00882; CoA_trans; 2. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2. DR PROSITE; PS01273; COA_TRANSF_1; 1. DR PROSITE; PS01274; COA_TRANSF_2; 1. DR UCD-2DPAGE; P55809; -. DR Genevisible; P55809; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease variant; Lipid metabolism; Mitochondrion; Phosphoprotein; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1..39 FT /note="Mitochondrion" FT /evidence="ECO:0000269|Ref.6" FT CHAIN 40..520 FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 1, FT mitochondrial" FT /id="PRO_0000002413" FT ACT_SITE 344 FT /note="5-glutamyl coenzyme A thioester intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 185 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0K2" FT MOD_RES 418 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0K2" FT MOD_RES 421 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0K2" FT MOD_RES 455 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D0K2" FT VAR_SEQ 1..397 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056310" FT VARIANT 58 FT /note="T -> M (in dbSNP:rs75134564)" FT /evidence="ECO:0000269|PubMed:21296660, FT ECO:0000269|PubMed:9671268" FT /id="VAR_000695" FT VARIANT 124..520 FT /note="Missing (in SCOTD)" FT /evidence="ECO:0000269|PubMed:33596448" FT /id="VAR_085802" FT VARIANT 133 FT /note="V -> E (in SCOTD; dbSNP:rs267606930)" FT /evidence="ECO:0000269|PubMed:9671268" FT /id="VAR_000696" FT VARIANT 215 FT /note="A -> V (in SCOTD; partial loss of activity; FT dbSNP:rs201752548)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065564" FT VARIANT 219 FT /note="G -> E (in SCOTD; dbSNP:rs121909302)" FT /evidence="ECO:0000269|PubMed:10964512" FT /id="VAR_010337" FT VARIANT 221 FT /note="V -> M (in SCOTD; dbSNP:rs121909303)" FT /evidence="ECO:0000269|PubMed:10964512" FT /id="VAR_010338" FT VARIANT 226 FT /note="S -> N (in SCOTD; loss of activity; FT dbSNP:rs368841359)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065565" FT VARIANT 245 FT /note="V -> F (in SCOTD; uncertain significance; FT dbSNP:rs727504063)" FT /evidence="ECO:0000269|PubMed:31073471" FT /id="VAR_085803" FT VARIANT 270 FT /note="I -> K (in SCOTD; uncertain significance; FT dbSNP:rs886043862)" FT /evidence="ECO:0000269|PubMed:33596448" FT /id="VAR_085804" FT VARIANT 280 FT /note="E -> A (in SCOTD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33596448" FT /id="VAR_085805" FT VARIANT 324 FT /note="G -> E (in SCOTD; dbSNP:rs121909301)" FT /evidence="ECO:0000269|PubMed:10964512" FT /id="VAR_010339" FT VARIANT 327 FT /note="L -> P (in SCOTD; partial loss of activity)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065566" FT VARIANT 404 FT /note="V -> F (in SCOTD; loss of activity)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065567" FT VARIANT 405 FT /note="S -> P (in SCOTD; loss of activity)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065568" FT VARIANT 437 FT /note="V -> M (in SCOTD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33596448" FT /id="VAR_085806" FT VARIANT 456 FT /note="C -> F (in SCOTD; dbSNP:rs121909300)" FT /evidence="ECO:0000269|PubMed:9671268" FT /id="VAR_000697" FT VARIANT 468 FT /note="R -> C (in SCOTD; partial loss of activity; the FT mutant retains half of the activity of the wild-type at 30 FT degrees; dbSNP:rs1327401976)" FT /evidence="ECO:0000269|PubMed:21296660" FT /id="VAR_065569" FT CONFLICT 95 FT /note="D -> G (in Ref. 4; BAG35249)" FT /evidence="ECO:0000305" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 46..50 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 100..104 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 108..114 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 120..127 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 138..150 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 154..158 FT /evidence="ECO:0007829|PDB:3DLX" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 205..211 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 237..249 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 300..309 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 318..321 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:3DLX" FT TURN 344..346 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 382..390 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 395..399 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 402..405 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:3DLX" FT TURN 416..418 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 435..440 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 450..455 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 461..464 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 472..479 FT /evidence="ECO:0007829|PDB:3DLX" FT TURN 480..482 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 483..489 FT /evidence="ECO:0007829|PDB:3DLX" FT HELIX 495..499 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:3DLX" FT STRAND 507..514 FT /evidence="ECO:0007829|PDB:3DLX" SQ SEQUENCE 520 AA; 56158 MW; 54DA790FB8EDA546 CRC64; MAALKLLSSG LRLCASARGS GATWYKGCVC SFSTSAHRHT KFYTDPVEAV KDIPDGATVL VGGFGLCGIP ENLIDALLKT GVKGLTAVSN NAGVDNFGLG LLLRSKQIKR MVSSYVGENA EFERQYLSGE LEVELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGS PIKYNKDGSV AIASKPREVR EFNGQHFILE EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAET TVVEVEEIVD IGAFAPEDIH IPQIYVHRLI KGEKYEKRIE RLSIRKEGDG EAKSAKPGDD VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNITVH LQSENGVLGL GPYPRQHEAD ADLINAGKET VTILPGASFF SSDESFAMIR GGHVDLTMLG AMQVSKYGDL ANWMIPGKMV KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKAVFDVDK KKGLTLIELW EGLTVDDVQK STGCDFAVSP KLMPMQQIAN //