ID A0A091CCA7_9ENTE Unreviewed; 691 AA.
AC A0A091CCA7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=TMU3MR103_1736 {ECO:0000313|EMBL:KFN90003.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN90003.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN90003.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN90003.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00007661}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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:KFN90003.1}.
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DR EMBL; JPVT01000183; KFN90003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CCA7; -.
DR PATRIC; fig|1302648.3.peg.1698; -.
DR Proteomes; UP000029381; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR CDD; cd00644; HMG-CoA_reductase_classII; 1.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 1.10.8.660; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
DR InterPro; IPR004553; HMG_CoA_Rdtase_bac-typ.
DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR NCBIfam; TIGR00532; HMG_CoA_R_NAD; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:KFN90003.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KFN90003.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381};
KW Transferase {ECO:0000313|EMBL:KFN90003.1}.
FT DOMAIN 1..138
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 148..268
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 691 AA; 75103 MW; 1B94F20E43AA7B91 CRC64;
MSQAPHLTYY DQQSDTYSQP NPVMLSDGLT DVFSGQHMGF TAENVAEKYN ITRKMQDAFA
LQSHKKAADA QEKGYFAEEI LPVELKDGLM EQDEGVRKNT SMEKLAKLGP VFKQTGSVTA
GNASTINDGA SAVMLATKNF ALENDLSYLA VLKDTIEVGI DPKIMGVSPV KAISQLLERN
ELKSEDIDLF EINEAFASSS IAVQQELNIP EEKINLCGSG ISIGHAIGAT GARIMTTACH
QLGRINGRYA VVSLCVGGGL GLAALIERPT EKKSSRFYEL SRQERLDQLV SQQRITTQMQ
NELNQNVLSE KIASNLIENQ ISETSIPMGV VENIKVNQKE YLVPMTTEEP SVIAACNNGA
QLVKRAGGFA ATMTQKNVRG QIVFMNIQDK EGIVRQIKEN QTSIMEKAKQ AYPSIVKRGG
GLKDIEIRDF TEDPSFLSVD LIVDTQDAMG ANMINTVLEA VATLFRQWFS EEILFSILSN
YATEAIVSAN CYVSFTDLGK GDAAKGEQIA KKISAASDFA QIDPYRAVTH NKGIMNGVEA
VVLATGNDTR SMSSAVHAYA ARNGKYQGLS QWKIEEKYLK GTIELPLVVA TAGGATKVLP
KAQVALQIMD VNNAKELAKV IAAVGLAQNL AAIKALVTEG IQKGHMALQA RSLALNAGAK
ASEVQKVANR LKKKQMNEEN ARKILQELRN K
//
