SCOT1_RAT
ID SCOT1_RAT Reviewed; 520 AA.
AC B2GV06;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial;
DE Short=SCOT;
DE EC=2.8.3.5 {ECO:0000250|UniProtKB:Q29551};
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 {ECO:0000312|EMBL:AAI66478.1};
GN Synonyms=Oxct {ECO:0000250|UniProtKB:Q29551},
GN Scot {ECO:0000250|UniProtKB:Q29551};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:EDL75738.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI66478.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Spleen {ECO:0000312|EMBL:AAI66478.1};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
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 (By similarity). 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:P55809,
CC ECO:0000250|UniProtKB:Q29551}.
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:0000250|UniProtKB:P55809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565;
CC Evidence={ECO:0000250|UniProtKB:P55809};
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:0000250|UniProtKB:P55809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481;
CC Evidence={ECO:0000250|UniProtKB:P55809};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P55809}.
CC -!- SUBUNIT: Homodimer. Only one subunit is competent to transfer the CoA
CC moiety to the acceptor carboxylate (3-oxo acid).
CC {ECO:0000250|UniProtKB:Q29551}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19343716}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000255}.
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DR EMBL; CH474048; EDL75738.1; -; Genomic_DNA.
DR EMBL; BC166478; AAI66478.1; -; mRNA.
DR RefSeq; NP_001121052.1; NM_001127580.1.
DR AlphaFoldDB; B2GV06; -.
DR SMR; B2GV06; -.
DR BioGRID; 604980; 2.
DR STRING; 10116.ENSRNOP00000063646; -.
DR iPTMnet; B2GV06; -.
DR PhosphoSitePlus; B2GV06; -.
DR jPOST; B2GV06; -.
DR PaxDb; B2GV06; -.
DR PeptideAtlas; B2GV06; -.
DR PRIDE; B2GV06; -.
DR GeneID; 690163; -.
DR KEGG; rno:690163; -.
DR CTD; 5019; -.
DR RGD; 1584008; Oxct1.
DR VEuPathDB; HostDB:ENSRNOG00000043094; -.
DR eggNOG; KOG3822; Eukaryota.
DR HOGENOM; CLU_019942_1_3_1; -.
DR InParanoid; B2GV06; -.
DR OMA; GTDYNKR; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; B2GV06; -.
DR BRENDA; 2.8.3.5; 5301.
DR Reactome; R-RNO-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR PRO; PR:B2GV06; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000043094; Expressed in heart and 19 other tissues.
DR Genevisible; B2GV06; RN.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IDA:RGD.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0060612; P:adipose tissue development; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0046952; P:ketone body catabolic process; ISO:RGD.
DR GO; GO:0042182; P:ketone catabolic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 2.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 2.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01273; COA_TRANSF_1; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 1: Evidence at protein level;
KW Lipid metabolism; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P55809"
FT CHAIN 40..520
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 1,
FT mitochondrial"
FT /id="PRO_0000349127"
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:0000250|UniProtKB:P55809"
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"
SQ SEQUENCE 520 AA; 56204 MW; D34D4F805665BC63 CRC64;
MAALKLLSSG LRLCASARNS RGALHKGCAC YFSVSTRHHT KFYTDPVEAV KDIPNGATLL
VGGFGLCGIP ENLIGALLKT GVKDLTAVSN NAGVDNFGLG LLLRSKQIKR MISSYVGENA
EFERQFLSGE LEVELTPQGT LAERIRAGGA GVPAFYTSTG YGTLVQEGGS PIKYNKDGSV
AIASKPREVR EFRGQHFILE EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAGT
TVVEVEEIVD IGSFAPEDIH IPKIYVHRLI KGEKYEKRIE RLSLRKEGEG KAKSGKPGED
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNMTVH LQSENGVLGL GPYPLKDEAD
ADLINAGKET VTVLPGASFF SSDESFAMIR GGHVNLTMLG AMQVSKYGDL ANWMIPGKMV
KGMGGAMDLV SSSKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKGVFDVDK
KNGLTLIELW EGLTVDDIRK STGCDFAVSP NLMPMQQIST
