ID A0A0D2CWP5_9EURO Unreviewed; 529 AA.
AC A0A0D2CWP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=PV07_07705 {ECO:0000313|EMBL:KIW28014.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28014.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW28014.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28014.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847043; KIW28014.1; -; Genomic_DNA.
DR RefSeq; XP_016248230.1; XM_016394811.1.
DR AlphaFoldDB; A0A0D2CWP5; -.
DR STRING; 569365.A0A0D2CWP5; -.
DR GeneID; 27346899; -.
DR VEuPathDB; FungiDB:PV07_07705; -.
DR HOGENOM; CLU_019942_1_2_1; -.
DR OrthoDB; 177109at2759; -.
DR UniPathway; UPA00929; UER00894.
DR Proteomes; UP000054466; Unassembled WGS sequence.
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; IPR004164; CoA_transf_AS.
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.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000858};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT ACT_SITE 357
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ SEQUENCE 529 AA; 57042 MW; 9D7094D0D48AB414 CRC64;
MSSFLESSLR IPSHASRSWR TARYFTRDQG KQNLLFARSF SSTLRRHEIN KVVPSAAEAI
KDMKSNSTLL CGGFGLCGVP DTLIDEVAKT PSITGLTAVS NNAGIPGAGL GQLLETKQVR
KMIASYVGEN KVLEQMYLTG EMELELTPQG TLAERCAAGG KGIPAFYTPA AFGTVVQTGE
IPLRHNKDGS IAQFGKPRDV KVFNGKSYVM EEAIAGDYAF VKAYKADKLG NCQFRLAANN
FNGAMGRNAK VTIVEAEHIV EVGEIDPVAV HLPGIYVSKV VQATAEKKIE KYVNRKEEGA
DVKDSLGKGD AASKREQIVR RAAKEFQNGM YANLGIGMPM LAPSFVDASV EVQLQSENGI
LGLGPYPRKG EEDPDLINAG KETVTLLPGA SCFGSEESFG MIRSGRINMS MLGAMQVSAK
GDLANWMLPG KVKGFGGAMD LVSNPEKTRV VALMEHTDKK GNPKILKQCE FPLTGRACVS
RIITELCVFD VDFTDGLTLI ELADGVTVDE IKAKTEAPFK VADNIKPML
//
