ID Q0QWD6_LEPMC Unreviewed; 513 AA.
AC Q0QWD6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=Succinyl-CoA:3-ketoacid-coenzyme A transferase {ECO:0000256|PIRNR:PIRNR000858};
DE EC=2.8.3.5 {ECO:0000256|PIRNR:PIRNR000858};
GN Name=SCOT {ECO:0000313|EMBL:ABB55461.1};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022 {ECO:0000313|EMBL:ABB55461.1};
RN [1] {ECO:0000313|EMBL:ABB55461.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBCN18 {ECO:0000313|EMBL:ABB55461.1};
RX PubMed=16776292; DOI=10.1094/MPMI-19-0588;
RA Elliott C.E., Howlett B.J.;
RT "Overexpression of a 3-ketoacyl-CoA thiolase in Leptosphaeria maculans
RT causes reduced pathogenicity on Brassica napus.";
RL Mol. Plant Microbe Interact. 19:588-596(2006).
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 {ECO:0000256|PIRNR:PIRNR000858}.
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:0000256|PIRNR:PIRNR000858};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000256|PIRNR:PIRNR000858}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000256|ARBA:ARBA00007154, ECO:0000256|PIRNR:PIRNR000858}.
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DR EMBL; DQ206623; ABB55461.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0QWD6; -.
DR UniPathway; UPA00929; UER00894.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0008260; F:succinyl-CoA:3-oxo-acid CoA-transferase activity; IEA:UniProtKB-EC.
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:SF58; 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 Mitochondrion {ECO:0000256|PIRNR:PIRNR000858};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 340
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 513 AA; 55262 MW; 8FD04D4C61EFB0F3 CRC64;
MQRSFLFSAR RHGPPTGLRF LSSTPSRLAI NKIVSSAEEA LKDMKPGTTV LVGGFGFSGV
PNTLINALRD RKDLTNFTVV SNNAGMPGVG LGQLLETKQI GTMIASYIGD NKVFEQMYLK
GQLSLQLTPQ GTIAEKCAAG AAGVPAFYTP AAYGTIVQTG ELPVRYNTDG TIAVMAPPKE
TREFNGKQYV LEEAIHGDYA FVKVAKADRL GNCQFRKAQN NFNEAMGKNA KMTIVEADEI
VEDGAIAPED IHLQGIYVKK VIKSTVGKAI ERLVHYKDPE AQKKAILEGG SSEAAQKRER
IIKRAAQELK DGMYVNLGIG MPLAAPAFLP EGTEIVLESE NGILGMGRYP MPGEEDPDLI
NAGKETVTLI KGASTFGSHE SFGMIRSGRI DVAMLGAMQV NQYGDLANFM LPGKVKGIGG
AMDLVANPTQ TKVVITMEHV DKKGNPKILN KCSFPLTGQK CVSTIITDLA VFDVDRVEGL
TLKEVAKGVS VEEVRSKTEA PFKVAEDLKE MSI
//
