ID   A0A0V1D0N7_TRIBR        Unreviewed;       548 AA.
AC   A0A0V1D0N7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   SubName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial {ECO:0000313|EMBL:KRY54563.1};
DE   Flags: Fragment;
GN   Name=Oxct1 {ECO:0000313|EMBL:KRY54563.1};
GN   ORFNames=T03_3052 {ECO:0000313|EMBL:KRY54563.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54563.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY54563.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY54563.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC       {ECO:0000256|ARBA:ARBA00007154}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY54563.1}.
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DR   EMBL; JYDI01000067; KRY54563.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1D0N7; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
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; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02429; pcaI_scoA_fam; 1.
DR   NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF23; SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE; 1.
DR   Pfam; PF01144; CoA_trans; 2.
DR   PIRSF; PIRSF000858; SCOT-t; 1.
DR   SMART; SM00882; CoA_trans; 2.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY54563.1}.
FT   REGION          14..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        373
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY54563.1"
SQ   SEQUENCE   548 AA;  60493 MW;  7A0E7765D9A91C46 CRC64;
     LTWRRVVGVE VCSENVDEKT RPSEREGAST VPRRTHWRGP EGRSAGPTRQ RVVTHLLFEM
     RKNCFSCTTF LKKDKVYPNP LEAVKDVPSG ATLLVGGFGI CGTPAGLLKA LVQTKIKDLT
     IISNNCGLEN FGIGWLLTNR QIKRMVSSYV GENEEFMRQY KDGELELEII PQGTLAERIR
     AGGAGIPAFY TPTGRSTLIE EGGWPIKFKK EGGVMMISEG KERRSFNGMP YIMETAIKSD
     FALIKAFKAD RSGNLIFRKS ARNFNPPMCK AGTISIVEVE ELVEVGELDP EDIDVSGIYV
     DRIVKSNYEK PIENLILSAK NLEINATSEI HHRIARRAVA EFKKGMYVNL GIGIPSICAS
     YISKNMDITF QCENGVLGMG PYPKKDEEDA DLINAAQESI TVLKGASYFS SDESFAMIRG
     GHLDVAVLDG MQVSQYGDLA NWFNPKKMNK GMGSAMDLVS SPNSRIIVCM EHLTPDGEPK
     IVQSCELPLT GEKCVDMIIT ERCVFTVDKL NGLTLVELGD NVSIENVIES TGCEFQVADV
     VMPMKDIN
//