SCOT_CAEEL
ID SCOT_CAEEL Reviewed; 521 AA.
AC Q09450;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable succinyl-CoA:3-ketoacid coenzyme A transferase, mitochondrial;
DE EC=2.8.3.5;
DE AltName: Full=3-oxoacid CoA-transferase;
DE Flags: Precursor;
GN ORFNames=C05C10.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(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 between
CC the carboxylate groups of the enzyme and substrate.
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:0000255|PROSITE-ProRule:PRU10034};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; Z48178; CAA88202.1; -; Genomic_DNA.
DR PIR; T18942; T18942.
DR RefSeq; NP_496144.1; NM_063743.5.
DR AlphaFoldDB; Q09450; -.
DR SMR; Q09450; -.
DR BioGRID; 39870; 29.
DR DIP; DIP-26691N; -.
DR STRING; 6239.C05C10.3; -.
DR EPD; Q09450; -.
DR PaxDb; Q09450; -.
DR PeptideAtlas; Q09450; -.
DR EnsemblMetazoa; C05C10.3.1; C05C10.3.1; WBGene00007330.
DR GeneID; 174548; -.
DR KEGG; cel:CELE_C05C10.3; -.
DR UCSC; C05C10.3.1; c. elegans.
DR CTD; 174548; -.
DR WormBase; C05C10.3; CE01467; WBGene00007330; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR HOGENOM; CLU_019942_1_3_1; -.
DR InParanoid; Q09450; -.
DR OMA; GTDYNKR; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; Q09450; -.
DR Reactome; R-CEL-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR PRO; PR:Q09450; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007330; Expressed in larva and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IBA:GO_Central.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
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 3: Inferred from homology;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..521
FT /note="Probable succinyl-CoA:3-ketoacid coenzyme A
FT transferase, mitochondrial"
FT /id="PRO_0000002417"
FT ACT_SITE 342
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ SEQUENCE 521 AA; 56114 MW; 3190B54C8A1708A7 CRC64;
MPILSKIWAA PAAGILRKTP RNAHQMRLIS MTSSMKAKVF NSAEEAVKDI PDNAKLLVGG
FGLCGIPENL IQAITKTGQK GLTCVSNNAG VDNWGLGLLL QTRQIKKMIS SYVGENGEFA
RQYLSGELEL EFTPQGTLAE RIRAAGAGVP AFYTPTGYGT QIQEGGAPIK YSKTEKGKIE
VASKAKETRQ FNGINYVMEE AIWGDFALIK AWRADTLGNI QFRHAAGNFN NPMCKASKCT
IVEVEEIVEP GVIAPNDVHI PSIYCHRLVL GKNYKKPIER PMFAHEGPIK PSTSAAGKSR
EIIAARAALE FTDGMYANLG IGIPTLAPNY IPNGFTVHLQ SENGIIGVGP YPRKGTEDAD
LINAGKEPIT LLKGASIVGS DESFAMIRGS HMDITVLGAL QCSQFGDLAN WMIPGKLVKG
MGGAMDLVSA PGARVIVVME HVSKNGEPKI LEHCELPLTG KGVISRIITD MAVFDVDTKN
GLTLIEVRKD LTVDDIKKLT ACKFEISENL KPMGQAPLNQ G
