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Database: UniProt
Entry: A0A084J887_9CLOT
LinkDB: A0A084J887_9CLOT
Original site: A0A084J887_9CLOT 
ID   A0A084J887_9CLOT        Unreviewed;       392 AA.
AC   A0A084J887;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE   AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN   ORFNames=IO99_16295 {ECO:0000313|EMBL:KEZ85171.1};
OS   Clostridium sulfidigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=318464 {ECO:0000313|EMBL:KEZ85171.1, ECO:0000313|Proteomes:UP000028542};
RN   [1] {ECO:0000313|EMBL:KEZ85171.1, ECO:0000313|Proteomes:UP000028542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=113A {ECO:0000313|EMBL:KEZ85171.1,
RC   ECO:0000313|Proteomes:UP000028542};
RA   Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT   "Draft genome of Clostridium sulfidigenes 113A isolated from sediments
RT   associated with methane hydrate from Krishna Godavari basin.";
RL   Submitted (JUL-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEZ85171.1}.
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DR   EMBL; JPMD01000041; KEZ85171.1; -; Genomic_DNA.
DR   RefSeq; WP_035135088.1; NZ_JPMD01000041.1.
DR   AlphaFoldDB; A0A084J887; -.
DR   STRING; 318464.IO99_16295; -.
DR   GeneID; 84602508; -.
DR   eggNOG; COG0183; Bacteria.
DR   Proteomes; UP000028542; 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; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KEZ85171.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028542};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KEZ85171.1}.
FT   DOMAIN          4..263
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          272..392
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        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  41107 MW;  F2F4430014521297 CRC64;
     MKEVVIVSAA RTAVGSFGGS LSKLSAAEIG AVAAKEAIKR AGIDPAIIDE AIIGNVISAG
     LGQNVGRQVA LKAGLKEEST AISINKVCGS GIKAVTLAAQ AIKSGDADVI LCGGTESMSN
     APYVLPTSRW GQRMGDSTMV DTMIKDGLWD AFYDYHMGVT AENIAEKWGL TREMQDEFAL
     NSQLKAEKAV KEGRFKDEIV PVEIPQRKGD PIVFDTDEFP KFGSTIEKLG KLKPAFKKGG
     TVTAGNASGI NDGAAMFIVM SKEKAEQLGV NYLATIKSYA SAGLDPQIMG YGPFEATSKA
     LSKAGLTVED LDLIEANEAF AAQSLAVAKD LKFDMNKVNV NGGAIAIGHP VGASGARILT
     TLIYEMIKRD NKKGLATLCI GGGQGIAIVI ER
//
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