ID G2E4R5_9GAMM Unreviewed; 394 AA.
AC G2E4R5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EGV29541.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EGV29541.1};
GN ORFNames=ThidrDRAFT_3278 {ECO:0000313|EMBL:EGV29541.1};
OS Thiorhodococcus drewsii AZ1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiorhodococcus.
OX NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV29541.1, ECO:0000313|Proteomes:UP000004200};
RN [1] {ECO:0000313|EMBL:EGV29541.1, ECO:0000313|Proteomes:UP000004200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ1 {ECO:0000313|EMBL:EGV29541.1,
RC ECO:0000313|Proteomes:UP000004200};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT "The draft genome of Thiorhodococcus drewsii AZ1.";
RL Submitted (JUN-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:EGV29541.1}.
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DR EMBL; AFWT01000026; EGV29541.1; -; Genomic_DNA.
DR RefSeq; WP_007041991.1; NZ_AFWT01000026.1.
DR AlphaFoldDB; G2E4R5; -.
DR STRING; 765913.ThidrDRAFT_3278; -.
DR PATRIC; fig|765913.3.peg.3344; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000004200; 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 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EGV29541.1}.
FT DOMAIN 6..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41029 MW; 7D88A15E047C604E CRC64;
MPTPNVVILS AVRSPIGTFG GSLSGMEPTE LAGIVMKEAV ARSGADPQQL QYVTVGNCIP
TEARYPYVAR VASIQAGLPM ESVAMAVNRL CGSGMQGILG TAQAIMTGEC EFGVGGGVEV
MSRGAYLSPS MRSGARMGDT QMIDAMVATL TDPFGVGHMG VTAENLAEKW GIEREEQDRY
ALESQRRACA AIAEGRFSKQ IVPIEVESRK GVMVFDTDEH PRANVTIEAL AKMRPIFKKG
GTVTAGNASG INDGAAFLVL AEAEAAERAG YRPIARLVSS AVAGVPNHIM GEGPIPASKK
ALERAGLSLD QMDIVESNEA FAAQAITVAR GLELDPAKTN PNGGAIALGH PVGCTGAFLA
TKAIHELERV GGRYALVTMC IGGGQGIAAI FERP
//
