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Database: UniProt
Entry: A0A0D6DW60_9LACT
LinkDB: A0A0D6DW60_9LACT
Original site: A0A0D6DW60_9LACT 
ID   A0A0D6DW60_9LACT        Unreviewed;       379 AA.
AC   A0A0D6DW60;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   ORFNames=LACPI_0520 {ECO:0000313|EMBL:CEN27720.1};
OS   Lactococcus piscium MKFS47.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN27720.1, ECO:0000313|Proteomes:UP000033166};
RN   [1] {ECO:0000313|Proteomes:UP000033166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA   Andreevskaya M.;
RL   Submitted (JAN-2015) 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; LN774769; CEN27720.1; -; Genomic_DNA.
DR   RefSeq; WP_047914966.1; NZ_LN774769.1.
DR   AlphaFoldDB; A0A0D6DW60; -.
DR   STRING; 1364.LP2241_20175; -.
DR   KEGG; lpk:LACPI_0520; -.
DR   HOGENOM; CLU_031026_0_0_9; -.
DR   Proteomes; UP000033166; Chromosome I.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
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   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; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CEN27720.1}.
FT   DOMAIN          4..247
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          255..376
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        84
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        364
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   379 AA;  39965 MW;  060E5139ADEB2745 CRC64;
     MERVFIVDSA RTAIGKFGGI FSDILPEYLG GDLLKKLLAR QQLSRVDEVI VGNIIGGGGN
     VGRRLALASG LAVETPALTI DRQCASGLES LVVATAKIKS GMASSIACGG VESTSRSPWL
     IERPAKLFGG PPKIIERAAL SIDAYGDPAM GEACEALASR LQISRLQQDA YAYQSQVKYQ
     QANQSGTFKD EIIGVKHATA DESPRADTNL KKLAALPAVF KENGTLTAGN SSPLNDGAAF
     VIIASESFCK TNQLQPLFEV VDGVSVGTLP ENFGLGPVYA TEKLLAKQGL TISEIDRIEL
     NEAFASQALA CIQTAGWQEA RVNRSGGALA FGHPFGATGA ILVRRLMTEL EKRPTLKTGL
     VTMCVGGGQG TSLLLRKVD
//
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