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Database: UniProt
Entry: G0S2K1_CHATD
LinkDB: G0S2K1_CHATD
Original site: G0S2K1_CHATD 
ID   G0S2K1_CHATD            Unreviewed;       523 AA.
AC   G0S2K1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=CTHT_0017510 {ECO:0000313|EMBL:EGS22234.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS22234.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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; GL988040; EGS22234.1; -; Genomic_DNA.
DR   RefSeq; XP_006692253.1; XM_006692190.1.
DR   AlphaFoldDB; G0S2K1; -.
DR   STRING; 759272.G0S2K1; -.
DR   GeneID; 18255789; -.
DR   KEGG; cthr:CTHT_0017510; -.
DR   eggNOG; KOG3822; Eukaryota.
DR   HOGENOM; CLU_019942_1_2_1; -.
DR   OMA; VKTMGQI; -.
DR   OrthoDB; 177109at2759; -.
DR   UniPathway; UPA00929; UER00894.
DR   Proteomes; UP000008066; 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:UP000008066};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000858}.
FT   ACT_SITE        351
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000858-1"
SQ   SEQUENCE   523 AA;  56344 MW;  93DD2F68686D54C7 CRC64;
     MVSAGLCMRT LRAYAKYGNN HAALFARAFS VTARRPEINK IYPSAAEALK DMKPNTTLLC
     GGFGLCGVPD TLIDELLNKP EITGLTAVSN NAGTDNSGLG KLLKTKQIKK MIASYIGENK
     TFEQMYLKGE IELELTPQGT LAERCAAGGK GIPAFYTPAA FGTVVQTGEL PLRNNPDGTP
     AEFSYPKDVK VFNGKPYLLE HAIEGDYAFV KAYKADRLGN CQFRLAAHNF NGAMGRNAKM
     TIVEAEHIVE PGEIPPEAVH LPGIYVQRVI KSTAPKNIEK YTWTLDPEEA AQDPKAAAAL
     GSGETKAKRE RIVRRAAKEF QNGMYANLGI GMPMLAPAFV AEGIEVMLQS ENGILGLGPY
     PRKGEEDPDL INAGKETVTL KPGASVFGSE ESFGMIRSGR INLTILGAMQ VSANGDLANW
     MLPGKVKGFG GAMDLVSNPS KTKVVVTMEH TDKKGNPKIV KQCAFPLTGR QCVSRIITEL
     GVFDVDFAQG LTLIEIADGV TVDEIRAKTE APFKVADDLK PML
//
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