ID SCOT_HUMAN STANDARD; PRT; 520 AA. AC P55809; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial DE precursor (EC 2.8.3.5) (Succinyl CoA:3-oxoacid CoA-transferase). GN OXCT OR SCOT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Heart; RX MEDLINE=96354545; PubMed=8751852; RA Kassovska-Bratinova S., Fukao T., Song X.-Q., Duncan A.M.V., RA Chen H.S., Robert M.-F., Perez-Cerda C., Ugarte M., Chartrand C., RA Vobecky S., Kondo N., Mitchell G.A.; RT "Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, RT human chromosomal mapping to 5p13, and mutation detection in a SCOT- RT deficient patient."; RL Am. J. Hum. Genet. 59:519-528(1996). RN [2] RP SEQUENCE FROM N.A., AND VARIANTS KETOACIDOSIS GLU-219; MET-221 AND RP GLU-324. RX MEDLINE=20422667; PubMed=10964512; RA Fukao T., Mitchell G.A., Song X.-Q., Nakamura H., RA Kassovska-Bratinova S., Orii K.E., Wraith J.E., Besley G., RA Wanders R.J.A., Niezen-Koning K.E., Berry G.T., Palmieri M., RA Kondo N.; RT "Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human RT SCOT gene, tertiary structural modeling of the human SCOT monomer, RT and characterization of three pathogenic mutations."; RL Genomics 68:144-151(2000). RN [3] RP 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 the SWISS-PROT data bank. RN [4] RP VARIANTS KETOACIDOSIS GLU-133 AND PHE-456, AND VARIANT MET-58. RX MEDLINE=98334343; PubMed=9671268; 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 RT pathogenic mutations, V133E and C456F, in Japanese siblings."; RL Hum. Mutat. 12:83-88(1998). CC -!- FUNCTION: KEY ENZYME FOR KETONE BODY CATABOLISM. TRANSFERS THE COA CC MOIETY FROM SUCCINATE TO ACETOACETATE. FORMATION OF THE ENZYME-COA CC INTERMEDIATE PROCEEDS VIA AN UNSTABLE ANHYDRIDE SPECIES FORMED CC BETWEEN THE CARBOXYLATE GROUPS OF THE ENZYME AND SUBSTRATE. CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + a 3-oxo acid = succinate + a 3- CC oxo-acyl-CoA. CC -!- PATHWAY: FIRST STEP OF KETOLYSIS IN EXTRAHEPATIC TISSUES. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- TISSUE SPECIFICITY: ABUNDANT IN HEART, FOLLOWED IN ORDER BY CC KIDNEY, BRAIN, AND MUSCLE, WHEREAS IN LIVER IT IS UNDETECTABLE; CC ALSO DETECTABLE IN LEUKOCYTES AND FIBROBLASTS. CC -!- DISEASE: Defects in OXCT are a cause of ketoacidosis [MIM:245050]. CC -!- SIMILARITY: BELONGS TO THE 3-OXOACID COA-TRANSFERASE FAMILY. 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; -. DR EMBL; AB029576; BAB13733.1; -. DR EMBL; AB029560; BAB13733.1; JOINED. DR EMBL; AB029561; BAB13733.1; JOINED. DR EMBL; AB029562; BAB13733.1; JOINED. DR EMBL; AB029563; BAB13733.1; JOINED. DR EMBL; AB029564; BAB13733.1; JOINED. DR EMBL; AB029565; BAB13733.1; JOINED. DR EMBL; AB029566; BAB13733.1; JOINED. DR EMBL; AB029567; BAB13733.1; JOINED. DR EMBL; AB029568; BAB13733.1; JOINED. DR EMBL; AB029569; BAB13733.1; JOINED. DR EMBL; AB029570; BAB13733.1; JOINED. DR EMBL; AB029571; BAB13733.1; JOINED. DR EMBL; AB029572; BAB13733.1; JOINED. DR EMBL; AB029573; BAB13733.1; JOINED. DR EMBL; AB029574; BAB13733.1; JOINED. DR EMBL; AB029575; BAB13733.1; JOINED. DR Genew; HGNC:8527; OXCT. DR MIM; 245050; -. DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; TAS. DR InterPro; IPR004165; CoA_trans. DR InterPro; IPR004163; CoA_transf_1. DR InterPro; IPR004164; CoA_transf_2. DR Pfam; PF01144; CoA_trans; 2. DR PROSITE; PS01273; COA_TRANSF_1; 1. DR PROSITE; PS01274; COA_TRANSF_2; 1. KW Mitochondrion; Transferase; Transit peptide; Disease mutation; KW Polymorphism. FT TRANSIT 1 39 MITOCHONDRION. FT CHAIN 40 520 SUCCINYL-COA:3-KETOACID-COENZYME A FT TRANSFERASE. FT DOMAIN 62 68 COA-BINDING (POTENTIAL). FT ACT_SITE 344 344 BY SIMILARITY. FT VARIANT 58 58 T -> M. FT /FTId=VAR_000695. FT VARIANT 133 133 V -> E (in ketoacidosis). FT /FTId=VAR_000696. FT VARIANT 219 219 G -> E (in ketoacidosis). FT /FTId=VAR_010337. FT VARIANT 221 221 V -> M (in ketoacidosis). FT /FTId=VAR_010338. FT VARIANT 324 324 G -> E (in ketoacidosis). FT /FTId=VAR_010339. FT VARIANT 456 456 C -> F (in ketoacidosis). FT /FTId=VAR_000697. SQ SEQUENCE 520 AA; 56157 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 //