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Database: UniProt
Entry: A0A143XG76_9FIRM
LinkDB: A0A143XG76_9FIRM
Original site: A0A143XG76_9FIRM 
ID   A0A143XG76_9FIRM        Unreviewed;       399 AA.
AC   A0A143XG76;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE   AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN   Name=thlA_1 {ECO:0000313|EMBL:CVI66193.1};
GN   ORFNames=BN3660_00445 {ECO:0000313|EMBL:CVI66193.1};
OS   Eubacteriaceae bacterium CHKCI004.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX   NCBI_TaxID=1780380 {ECO:0000313|EMBL:CVI66193.1, ECO:0000313|Proteomes:UP000199324};
RN   [1] {ECO:0000313|EMBL:CVI66193.1, ECO:0000313|Proteomes:UP000199324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC4 {ECO:0000313|EMBL:CVI66193.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; FCNR01000017; CVI66193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143XG76; -.
DR   STRING; 1780380.BN3660_00445; -.
DR   Proteomes; UP000199324; Unassembled WGS sequence.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:CVI66193.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199324};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CVI66193.1}.
FT   DOMAIN          4..260
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..394
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   399 AA;  42735 MW;  A4D3DB5EDF8627C1 CRC64;
     MKDVVIVSAC RTPIGKFLGM FKDVSARELA MTAGKEAINR AGIEPAMIDN VVVGQVYAGM
     QGSLPAKQIS YRLGCPAESN ACVVNQNCAS GMRALEIACD NIAMGKSEIG LVIGVENMTQ
     APYMLPKARG GYRMGNAEVV DSMLHDALID ELSGGHMGVT AENVAKLYGI TREECDELAL
     RSHRLACKAI DEGKFKEEIV PVEVKMKKKT ILATEDEHPI RDCNMETLSK LRPAFIKDGV
     VTAANASGIN DAAAAVVVMS LDKAKELGVT PLLKMINICA AGVKPEIMGV GPAEAIPKAL
     KLAGLKYEDV DYWEINEAFA PQFIGCGRQL EKNYGIKINM DRTNVNGSGI ALGHPIGCTA
     LRIIVSMYYE MKRNDYKIGG AALCVGTGPA MASLWTTEI
//
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