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Database: UniProt
Entry: M9LK53_PSEA3
LinkDB: M9LK53_PSEA3
Original site: M9LK53_PSEA3 
ID   M9LK53_PSEA3            Unreviewed;       526 AA.
AC   M9LK53;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=PANT_5d00070 {ECO:0000313|EMBL:GAC71791.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71791.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
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; DF196771; GAC71791.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LK53; -.
DR   STRING; 1151754.M9LK53; -.
DR   OrthoDB; 177109at2759; -.
DR   UniPathway; UPA00929; UER00894.
DR   Proteomes; UP000011976; 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:SF60; 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:UP000011976};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT   ACT_SITE        353
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   526 AA;  56152 MW;  81BCB4306735139A CRC64;
     MLTASLRSRA ACRSAFVATT LPSRTFASSA TRAIASSKVY PSADEAVKDI KSGSTLLSAG
     FGLCGTPETL IGAISRHPHI KDLTVVSNNA GTGEFGLGKL LKSKQIKKMI SSFIGGNKYF
     ENQYLTGQVS LQLTPQGTLV EKCRAGAFGI PAFYTPTGYG TAVQTSDLVV RYEQREEGSK
     EPLKPAEMAK PKEQREFNGR NYILEEAIYG DVAIIHAWKV DEAGNAVFRY AANNFSAPFG
     KNAKMTIVEA EQIVPVGTLN ADEIHLPAIF VDRIVKSQHE KQIEVHTVSD APKAAKSEGA
     DAAKQEARER RIRIAKRAAK EVKDGDYINL GVGMPSLVPN YLPQGVNVVL HSENGILGMG
     PYPKTAEVDA DIVNAGKETV TLLPGASTFD SSESFGMIRG GHINVTMLGA LQVGANGDLA
     NYMIPGKKVS GVGGAMDLVS NPANTKVVVV SDHTDKNGRS KIVADCKLPL TGSRCVSRIV
     TDLCVFDVDR VGDKGLTLID LQDGVTVQQV REKTDAPFNL GPGIKE
//
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