ID   SCO2A_RAT               Reviewed;         520 AA.
AC   Q5XIJ9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial;
DE            EC=2.8.3.5;
DE   AltName: Full=3-oxoacid CoA-transferase 2A;
DE   AltName: Full=Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1;
DE            Short=SCOT-t1;
DE   Flags: Precursor;
GN   Name=Oxct2a;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=19423663; DOI=10.1530/rep-09-0052;
RA   Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT   "Identification of novel immunodominant epididymal sperm proteins using
RT   combinatorial approach.";
RL   Reproduction 138:81-93(2009).
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 (By similarity).
CC       Probably play and important roles in the energy metabolism of
CC       spermatozoa (By similarity). {ECO:0000250}.
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   -!- TISSUE SPECIFICITY: Expressed in flagella of epididymal sperm.
CC       {ECO:0000269|PubMed:19423663}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC083681; AAH83681.1; -; mRNA.
DR   RefSeq; NP_001012221.1; NM_001012221.1.
DR   AlphaFoldDB; Q5XIJ9; -.
DR   SMR; Q5XIJ9; -.
DR   iPTMnet; Q5XIJ9; -.
DR   PhosphoSitePlus; Q5XIJ9; -.
DR   GeneID; 366463; -.
DR   KEGG; rno:366463; -.
DR   UCSC; RGD:1306953; rat.
DR   CTD; 353371; -.
DR   RGD; 1306953; Oxct2a.
DR   InParanoid; Q5XIJ9; -.
DR   OrthoDB; 460209at2759; -.
DR   PhylomeDB; Q5XIJ9; -.
DR   UniPathway; UPA00929; UER00894.
DR   PRO; PR:Q5XIJ9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; ISO:RGD.
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   1: Evidence at protein level;
KW   Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           40..520
FT                   /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 2A,
FT                   mitochondrial"
FT                   /id="PRO_0000366210"
FT   REGION          280..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ   SEQUENCE   520 AA;  56900 MW;  46ED83083EB83399 CRC64;
     MAALRLLAWA FSRRVSAHRP QPTLPHHLIR HYPTTRCGKV KFYTDPVKAV EGIKDGASVM
     LGGFGLCGIP ENLIGALKTK GVKDLKIISS NVGVDDFGLG ILLASKQVRR VVCSYLGENK
     LCEQLYLAGK LELEMTPQGT LAERIRAGGT GVPAFYTPTG YGTQVQEGGV PIRYSPEGHL
     ITLSQPREVR EFEGQHHLLE RAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI
     SVVEVEEIVD VGTFAPEDIH IPNIYVKRVI KGPRFEKRIE RLTTRDSPPA PGSKDQDPKR
     TRIIKRAALE FKDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP FPLKKEVDPD
     IINAGKQTVT VIPGGCFFAS DDSFAMIRGG HIQLTMLGAM QVSKYGDLAN WMVPGKKVKG
     MGGAMDLVSS KKTKVVVTME HCTKTKQPKI LEKCTMPLTG KSCVDLIITE KAVFEVDRSK
     GLKLVELWEG SSLDEVKATT GCSFKVCPNL KPMQQIKSDA