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Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 1) (Somatic-type succinyl-CoA:3-oxoacid CoA-transferase) (SCOT-s)

 SCOT1_PIG               Reviewed;         520 AA.
Q29551; F1SMH7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JUL-2012, sequence version 2.
23-MAY-2018, entry version 119.
RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial;
EC=2.8.3.5;
AltName: Full=3-oxoacid CoA-transferase 1;
AltName: Full=Somatic-type succinyl-CoA:3-oxoacid CoA-transferase;
Short=SCOT-s;
Flags: Precursor;
Name=OXCT1; Synonyms=OXCT, SCOT;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 40-70 AND 296-305.
TISSUE=Heart;
PubMed=1730685;
Lin T., Bridger W.A.;
"Sequence of a cDNA clone encoding pig heart mitochondrial CoA
transferase.";
J. Biol. Chem. 267:975-978(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Swine Genome Sequencing Consortium.;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[3]
ACTIVE SITE.
PubMed=7915164; DOI=10.1002/pro.5560030613;
Rochet J.C., Bridger W.A.;
"Identification of glutamate 344 as the catalytic residue in the
active site of pig heart CoA transferase.";
Protein Sci. 3:975-981(1994).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-520, AND SUBUNIT.
TISSUE=Heart;
PubMed=12463743; DOI=10.1021/bi020568f;
Bateman K.S., Brownie E.R., Wolodko W.T., Fraser M.E.;
"Structure of the mammalian CoA transferase from pig heart.";
Biochemistry 41:14455-14462(2002).
[5]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 40-520, AND SUBUNIT.
TISSUE=Heart;
Mitchell E.P., Lloyd A.J., Lewis G., Shoolingin-Jordan P.;
"Succinate:Coenzyme-A transferase deficiency: A structural view of
pathogenic mutations.";
Submitted (DEC-2002) to the PDB data bank.
[6]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 40-520, AND SUBUNIT.
TISSUE=Heart;
PubMed=15388917; DOI=10.1107/S0907444904017974;
Coros A.M., Swenson L., Wolodko W.T., Fraser M.E.;
"Structure of the CoA transferase from pig heart to 1.7 A
resolution.";
Acta Crystallogr. D 60:1717-1725(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 40-520 OF MUTANTS
ALA/SER-67, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF
CYS-67 AND CYS-235, AND REACTION MECHANISM.
TISSUE=Heart;
PubMed=17718512; DOI=10.1021/bi700828h;
Tammam S.D., Rochet J.C., Fraser M.E.;
"Identification of the cysteine residue exposed by the conformational
change in pig heart succinyl-CoA:3-ketoacid coenzyme A transferase on
binding coenzyme A.";
Biochemistry 46:10852-10863(2007).
[8]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 40-520, AND SUBUNIT.
TISSUE=Heart;
PubMed=20606260; DOI=10.1107/S0907444910018366;
Coker S.F., Lloyd A.J., Mitchell E., Lewis G.R., Coker A.R.,
Shoolingin-Jordan P.M.;
"The high-resolution structure of pig heart succinyl-CoA:3-oxoacid
coenzyme A transferase.";
Acta Crystallogr. D 66:797-805(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 40-517 IN COMPLEX WITH
REACTION INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
TISSUE=Heart;
PubMed=20977214; DOI=10.1021/bi100659s;
Fraser M.E., Hayakawa K., Brown W.D.;
"Catalytic role of the conformational change in succinyl-CoA:3-oxoacid
CoA transferase on binding CoA.";
Biochemistry 49:10319-10328(2010).
-!- FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA
moiety from succinate to acetoacetate. Formation of the enzyme-CoA
intermediate proceeds via an unstable anhydride species formed
between the carboxylate groups of the enzyme and substrate.
{ECO:0000269|PubMed:17718512, ECO:0000269|PubMed:20977214}.
-!- CATALYTIC ACTIVITY: Succinyl-CoA + a 3-oxo acid = succinate + a 3-
oxoacyl-CoA. {ECO:0000255|PROSITE-ProRule:PRU10034,
ECO:0000269|PubMed:17718512, ECO:0000269|PubMed:20977214}.
-!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-
CoA from succinyl-CoA: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12463743,
ECO:0000269|PubMed:15388917, ECO:0000269|PubMed:17718512,
ECO:0000269|PubMed:20606260, ECO:0000269|PubMed:20977214,
ECO:0000269|Ref.5}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M80534; AAA31019.1; -; mRNA.
EMBL; CU993811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FP017290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A41771; A41771.
RefSeq; NP_999103.1; NM_213938.1.
UniGene; Ssc.27309; -.
PDB; 1M3E; X-ray; 2.50 A; A/B/C/D=40-520.
PDB; 1O9L; X-ray; 2.40 A; A/B/C/D=40-520.
PDB; 1OOY; X-ray; 1.70 A; A/B=40-520.
PDB; 1OOZ; X-ray; 2.10 A; A/B=40-520.
PDB; 1OPE; X-ray; 2.50 A; A/B=40-520.
PDB; 2NRB; X-ray; 2.00 A; A/B/C/D=40-520.
PDB; 2NRC; X-ray; 2.05 A; A/B/C/D=40-520.
PDB; 3K6M; X-ray; 1.50 A; A/B/C/D=40-520.
PDB; 3OXO; X-ray; 2.30 A; A/B/C/D/E/F/G/H=40-517.
PDBsum; 1M3E; -.
PDBsum; 1O9L; -.
PDBsum; 1OOY; -.
PDBsum; 1OOZ; -.
PDBsum; 1OPE; -.
PDBsum; 2NRB; -.
PDBsum; 2NRC; -.
PDBsum; 3K6M; -.
PDBsum; 3OXO; -.
SMR; Q29551; -.
STRING; 9823.ENSSSCP00000017870; -.
PaxDb; Q29551; -.
PeptideAtlas; Q29551; -.
PRIDE; Q29551; -.
Ensembl; ENSSSCT00000037432; ENSSSCP00000055212; ENSSSCG00000016863.
Ensembl; ENSSSCT00000044789; ENSSSCP00000052664; ENSSSCG00000016863.
GeneID; 396978; -.
KEGG; ssc:396978; -.
CTD; 5019; -.
eggNOG; KOG3822; Eukaryota.
eggNOG; COG1788; LUCA.
eggNOG; COG2057; LUCA.
GeneTree; ENSGT00390000009130; -.
HOVERGEN; HBG002310; -.
InParanoid; Q29551; -.
KO; K01027; -.
OrthoDB; EOG091G0D3X; -.
BRENDA; 2.8.3.5; 6170.
Reactome; R-SSC-77108; Utilization of Ketone Bodies.
UniPathway; UPA00929; UER00894.
EvolutionaryTrace; Q29551; -.
Proteomes; UP000008227; Chromosome 16.
ExpressionAtlas; Q29551; baseline and differential.
Genevisible; Q29551; SS.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0046950; P:cellular ketone body metabolic process; ISS:UniProtKB.
GO; GO:0046952; P:ketone body catabolic process; IEA:Ensembl.
GO; GO:0042182; P:ketone catabolic process; IEA:Ensembl.
InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
InterPro; IPR014388; 3-oxoacid_CoA-transferase.
InterPro; IPR004165; CoA_trans_fam_I.
InterPro; IPR004164; CoA_transf_AS.
InterPro; IPR004163; CoA_transf_BS.
InterPro; IPR037171; NagB/RpiA_transferase-like.
PANTHER; PTHR13707; PTHR13707; 1.
Pfam; PF01144; CoA_trans; 2.
PIRSF; PIRSF000858; SCOT-t; 1.
SMART; SM00882; CoA_trans; 2.
SUPFAM; SSF100950; SSF100950; 2.
TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
PROSITE; PS01273; COA_TRANSF_1; 1.
PROSITE; PS01274; COA_TRANSF_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 39 Mitochondrion.
{ECO:0000269|PubMed:1730685}.
CHAIN 40 520 Succinyl-CoA:3-ketoacid coenzyme A
transferase 1, mitochondrial.
/FTId=PRO_0000002415.
ACT_SITE 344 344 5-glutamyl coenzyme A thioester
intermediate. {ECO:0000255|PROSITE-
ProRule:PRU10034,
ECO:0000269|PubMed:7915164}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:P55809}.
MOD_RES 185 185 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9D0K2}.
MOD_RES 418 418 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9D0K2}.
MOD_RES 421 421 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9D0K2}.
MOD_RES 455 455 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9D0K2}.
MUTAGEN 67 67 C->A: Decreases KM for acetoacetyl-CoA 3-
fold. No effect on KM for acetoacetate,
succinyl-CoA and succinate.
{ECO:0000269|PubMed:17718512}.
MUTAGEN 67 67 C->S: Decreases KM for acetoacetate and
acetoacetyl-CoA 2-fold. Increases KM for
succinate 2-fold. Decreases KM for
succinyl-CoA nearly 4-fold. Strongly
reduces catalytic activity.
{ECO:0000269|PubMed:17718512}.
MUTAGEN 235 235 C->S: Similar specific activity to wild-
type. {ECO:0000269|PubMed:17718512}.
CONFLICT 480 480 S -> R (in Ref. 1; AAA31019).
{ECO:0000305}.
STRAND 41 44 {ECO:0000244|PDB:3K6M}.
HELIX 46 50 {ECO:0000244|PDB:3K6M}.
STRAND 58 61 {ECO:0000244|PDB:3K6M}.
HELIX 71 80 {ECO:0000244|PDB:3K6M}.
STRAND 84 88 {ECO:0000244|PDB:3K6M}.
HELIX 100 104 {ECO:0000244|PDB:3K6M}.
STRAND 108 114 {ECO:0000244|PDB:3K6M}.
HELIX 120 127 {ECO:0000244|PDB:3K6M}.
STRAND 130 135 {ECO:0000244|PDB:3K6M}.
HELIX 138 149 {ECO:0000244|PDB:3K6M}.
STRAND 154 158 {ECO:0000244|PDB:3K6M}.
TURN 159 162 {ECO:0000244|PDB:3K6M}.
HELIX 164 167 {ECO:0000244|PDB:3K6M}.
STRAND 171 174 {ECO:0000244|PDB:3K6M}.
STRAND 178 183 {ECO:0000244|PDB:3K6M}.
STRAND 189 192 {ECO:0000244|PDB:3K6M}.
STRAND 195 201 {ECO:0000244|PDB:3K6M}.
STRAND 205 216 {ECO:0000244|PDB:3K6M}.
HELIX 225 227 {ECO:0000244|PDB:3K6M}.
HELIX 231 234 {ECO:0000244|PDB:3K6M}.
STRAND 237 249 {ECO:0000244|PDB:3K6M}.
HELIX 256 258 {ECO:0000244|PDB:3K6M}.
HELIX 263 265 {ECO:0000244|PDB:3K6M}.
STRAND 268 271 {ECO:0000244|PDB:3K6M}.
HELIX 302 309 {ECO:0000244|PDB:3K6M}.
HELIX 310 312 {ECO:0000244|PDB:3K6M}.
STRAND 317 321 {ECO:0000244|PDB:3K6M}.
HELIX 325 329 {ECO:0000244|PDB:3K6M}.
HELIX 330 332 {ECO:0000244|PDB:3K6M}.
STRAND 339 343 {ECO:0000244|PDB:3K6M}.
TURN 344 346 {ECO:0000244|PDB:3K6M}.
STRAND 347 350 {ECO:0000244|PDB:3K6M}.
HELIX 356 358 {ECO:0000244|PDB:3K6M}.
STRAND 368 370 {ECO:0000244|PDB:3K6M}.
STRAND 373 379 {ECO:0000244|PDB:3K6M}.
HELIX 382 390 {ECO:0000244|PDB:3K6M}.
STRAND 395 399 {ECO:0000244|PDB:3K6M}.
STRAND 402 405 {ECO:0000244|PDB:3K6M}.
STRAND 413 415 {ECO:0000244|PDB:2NRC}.
TURN 416 418 {ECO:0000244|PDB:3K6M}.
HELIX 426 429 {ECO:0000244|PDB:3K6M}.
STRAND 435 440 {ECO:0000244|PDB:3K6M}.
STRAND 443 445 {ECO:0000244|PDB:2NRB}.
HELIX 446 448 {ECO:0000244|PDB:3K6M}.
STRAND 450 455 {ECO:0000244|PDB:3K6M}.
STRAND 461 464 {ECO:0000244|PDB:3K6M}.
STRAND 468 470 {ECO:0000244|PDB:3K6M}.
STRAND 472 479 {ECO:0000244|PDB:3K6M}.
TURN 480 482 {ECO:0000244|PDB:3K6M}.
STRAND 483 489 {ECO:0000244|PDB:3K6M}.
HELIX 495 500 {ECO:0000244|PDB:3K6M}.
STRAND 502 504 {ECO:0000244|PDB:1M3E}.
STRAND 507 514 {ECO:0000244|PDB:3K6M}.
SEQUENCE 520 AA; 56338 MW; 3DCFE430FE78C222 CRC64;
MAALTLLSSR LRLCASAYRS GGAWSQGCAG YFSTSTRRHT KFYTDAVEAV KDIPNGATVL
VGGFGLCGIP ENLIGALLKT GVKELTAVSN NAGVDNFGLG LLLQSKQIKR MISSYVGENA
EFERQYLAGE LEVELTPQGT LAERIRAGGA GVPAFYTSTG YGTLVQEGGS PIKYNKDGSI
AIASKPREVR EFNGQHFILE EAIRGDFALV KAWKADQAGN VTFRKSARNF NLPMCKAAET
TVVEVEEIVD IGSFAPEDIH IPKIYVHRLV KGEKYEKRIE RLSVRKEEDV KTRSGKLGDN
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNMTVH LQSENGILGL GPYPLQNEVD
ADLINAGKET VTVLPGASYF SSDESFAMIR GGHVNLTMLG AMQVSKYGDL ANWMIPGKLV
KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKAVFDVDS
KKGLTLIELW EGLTVDDIKK STGCDFAVSP KLIPMQQVTT


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