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Database: UniProt
Entry: U4LQ29_PYROM
LinkDB: U4LQ29_PYROM
Original site: U4LQ29_PYROM 
ID   U4LQ29_PYROM            Unreviewed;       520 AA.
AC   U4LQ29;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=PCON_04056 {ECO:0000313|EMBL:CCX17127.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX17127.1};
RN   [1] {ECO:0000313|EMBL:CCX17127.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX17127.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX17127.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(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; HF936576; CCX17127.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4LQ29; -.
DR   STRING; 1076935.U4LQ29; -.
DR   eggNOG; KOG3822; Eukaryota.
DR   OMA; NWGLPGR; -.
DR   OrthoDB; 177109at2759; -.
DR   UniPathway; UPA00929; UER00894.
DR   Proteomes; UP000018144; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT   ACT_SITE        347
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   520 AA;  55366 MW;  3351B7A3F87B874F CRC64;
     MVSTASLLLR TARNFSKDGS KHSLLFARTF ASSSRRYEIN KVYPSAAEAI KDMKSGSTLL
     SGGFGLCGVP DTLINELEKN THINELTCVS NNAGVDGGGL GKLLATGQVK KMIASYVGEN
     KTFERKYLTG EIELELTPQG TLAERCRAGG AGIPAFYTPA AFGTWVQTGE LPTKYNADGT
     VAQYSKPREV RVFDGKSYIM EEAIKGDYAF VKAWKADPLG NCQFRFSGAN FNGAMGRNAA
     ITIVEAEEIV PAGSIEPAAV NLPGIYVQRV VQSTTEKGIE KRVYAKDPAE AAAAALGSGD
     AASKRERIVK RAAKEFKNGM YANLGIGMPM LAPSFVDPSV TVQLQSENGI LGLGPYPQKG
     QEDPDLINAG KETVTLNAGA AVFGSDESFG MIRSGRVDLT ILGAMQVSQY GDLASWALPG
     KIKGMGGAMD LVSNPTKTKV VVTMEHTDKK GNPKILQQCA FPLTGPTCVS RIITELAVFD
     VHPTEGLTLI EHAEDATVDE IKSKTGAPFK VSADLKPMQI
//
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