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Database: UniProt
Entry: G7CEW1_MYCT3
LinkDB: G7CEW1_MYCT3
Original site: G7CEW1_MYCT3 
ID   G7CEW1_MYCT3            Unreviewed;       386 AA.
AC   G7CEW1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EHI13040.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:EHI13040.1};
GN   ORFNames=KEK_07652 {ECO:0000313|EMBL:EHI13040.1};
OS   Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI13040.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI13040.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) 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:EHI13040.1}.
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DR   EMBL; AGVE01000042; EHI13040.1; -; Genomic_DNA.
DR   RefSeq; WP_003925028.1; NZ_AGVE01000042.1.
DR   AlphaFoldDB; G7CEW1; -.
DR   PATRIC; fig|1078020.3.peg.1505; -.
DR   eggNOG; COG0183; Bacteria.
DR   Proteomes; UP000004915; 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; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR   PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:EHI13040.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004915};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EHI13040.1}.
FT   DOMAIN          5..255
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          263..385
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        342
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   386 AA;  41278 MW;  ED9D1EAE742A7FBB CRC64;
     MSEAYVIDAV RTPTGKRNGS LAALHPIDLG VHAFRGIFDR NDVDPAAVDD VVVGCVDAIG
     GQAGNIGRLM WLAAGYPEEV PGVTVDRQCG SSQQAISFGA QAIMSGTADI ILAGGVQNMS
     QIPISSAMIV GKEFGFTSPT NESKYWLHRY GDQEISQFRG AEMIAERWEI SREDMERYAL
     TSHERALAAI RAGRFDNEII GVPVDGGEFR IDETPRETSL EKMAALPTLT EGGRMTAAVA
     SQISDGASAV LLASEKAVKE HKLKPRARIH HISARGDDPV LMLTGPIPAT RYALEKTGLS
     MDDIDVVEIN EAFAPVVIAW EKELKVDHAK VNPNGGAIAL GHPLGATGAK LFATMLNELE
     RTGGRYGLQT MCEGGGTANV TIIERL
//
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