ID   CAT1_CLOK5              Reviewed;         538 AA.
AC   P38946; A5N1M8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Succinyl-CoA:coenzyme A transferase;
DE            EC=2.8.3.-;
GN   Name=cat1; OrderedLocusNames=CKL_3016;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8550525; DOI=10.1128/jb.178.3.871-880.1996;
RA   Soehling B., Gottschalk G.;
RT   "Molecular analysis of the anaerobic succinate degradation pathway in
RT   Clostridium kluyveri.";
RL   J. Bacteriol. 178:871-880(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC   -!- FUNCTION: Forms succinyl-CoA from succinate and acetyl-CoA.
CC   -!- INDUCTION: Efficiently transcribed only during growth on ethanol plus
CC       succinate.
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000305}.
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DR   EMBL; L21902; AAA92346.1; -; Genomic_DNA.
DR   EMBL; CP000673; EDK35024.1; -; Genomic_DNA.
DR   RefSeq; WP_012103359.1; NC_009706.1.
DR   AlphaFoldDB; P38946; -.
DR   SMR; P38946; -.
DR   STRING; 431943.CKL_3016; -.
DR   PRIDE; P38946; -.
DR   EnsemblBacteria; EDK35024; EDK35024; CKL_3016.
DR   KEGG; ckl:CKL_3016; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_9; -.
DR   OMA; DEALSWH; -.
DR   OrthoDB; 319106at2; -.
DR   BioCyc; MetaCyc:MON-13465; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:InterPro.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 3.40.1080.20; -; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR003702; ActCoA_hydro.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR017821; Succinate_CoA_transferase.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR03458; YgfH_subfam; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..538
FT                   /note="Succinyl-CoA:coenzyme A transferase"
FT                   /id="PRO_0000215525"
FT   ACT_SITE        330
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         305..309
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         420
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         424
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   538 AA;  58853 MW;  D595BAACD087B484 CRC64;
     MSKGIKNSQL KKKNVKASNV AEKIEEKVEK TDKVVEKAAE VTEKRIRNLK LQEKVVTADV
     AADMIENGMI VAISGFTPSG YPKEVPKALT KKVNALEEEF KVTLYTGSST GADIDGEWAK
     AGIIERRIPY QTNSDMRKKI NDGSIKYADM HLSHMAQYIN YSVIPKVDIA IIEAVAITEE
     GDIIPSTGIG NTATFVENAD KVIVEINEAQ PLELEGMADI YTLKNPPRRE PIPIVNAGNR
     IGTTYVTCGS EKICAIVMTN TQDKTRPLTE VSPVSQAISD NLIGFLNKEV EEGKLPKNLL
     PIQSGVGSVA NAVLAGLCES NFKNLSCYTE VIQDSMLKLI KCGKADVVSG TSISPSPEML
     PEFIKDINFF REKIVLRPQE ISNNPEIARR IGVISINTAL EVDIYGNVNS THVMGSKMMN
     GIGGSGDFAR NAYLTIFTTE SIAKKGDISS IVPMVSHVDH TEHDVMVIVT EQGVADLRGL
     SPREKAVAII ENCVHPDYKD MLMEYFEEAC KSSGGNTPHN LEKALSWHTK FIKTGSMK