SCOT_DICDI
ID SCOT_DICDI Reviewed; 509 AA.
AC Q54JD9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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 Name=oxct1; ORFNames=DDB_G0288105;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000109; EAL63397.1; -; Genomic_DNA.
DR RefSeq; XP_636911.1; XM_631819.1.
DR AlphaFoldDB; Q54JD9; -.
DR SMR; Q54JD9; -.
DR STRING; 44689.DDB0235256; -.
DR PaxDb; Q54JD9; -.
DR PRIDE; Q54JD9; -.
DR EnsemblProtists; EAL63397; EAL63397; DDB_G0288105.
DR GeneID; 8626466; -.
DR KEGG; ddi:DDB_G0288105; -.
DR dictyBase; DDB_G0288105; oxct.
DR eggNOG; KOG3822; Eukaryota.
DR HOGENOM; CLU_019942_1_2_1; -.
DR InParanoid; Q54JD9; -.
DR OMA; GTDYNKR; -.
DR PhylomeDB; Q54JD9; -.
DR Reactome; R-DDI-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR PRO; PR:Q54JD9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; ISS:dictyBase.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; ISS:dictyBase.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..509
FT /note="Probable succinyl-CoA:3-ketoacid coenzyme A
FT transferase, mitochondrial"
FT /id="PRO_0000327840"
FT ACT_SITE 335
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ SEQUENCE 509 AA; 54935 MW; AF85B9619C361755 CRC64;
MLSRNLKTLV KNKNILYFTT STSKSNKIYE NAKEAVKDIP NGSKLLVGGF GLCGIPENLI
SAVRDTGVKD LTVVSNNAGV DDFGLGVLLK SRQIKRMISS YVGENATFES QYLKGELEVE
LTPQGNLAER LRAGGAGIPA FYTSTGVGTV LVEEGGFPIK YANDGSGKVE IKSEPRPTQL
YNGRKYCLEE SITGDYALIK AWKADTRGNL VFRNTARNFN PPMATAAKIT IAEVEEIVDA
GEIKPDEVHV PGIYIQRIVK GPSFEKRIER LTVQKEKTGE AAAKPKDEAA AKRERIVRRA
ALEFEDGMYC NLGIGMPTLA SNFIPKGIRI ELQSENGLLG MGPFPKMGEH DADLINAGKE
TVTTIPGSSI FSSADSFAMI RGGHVDLTIL GGMQVSGNGD LANWVIPGSM VKGPGGAMDL
TSSGSRVVVI MEHTTKHGKP KILKNCTLPL TGKSCVNRII TELAVFDVVN GKLELIEVVD
GQTVDDIKSK TEAEFTVSKN LKPLQQVEI
