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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//