ID A0A2S2BTP3_9NOCA Unreviewed; 397 AA.
AC A0A2S2BTP3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=CBI38_10710 {ECO:0000313|EMBL:AWK71981.1};
OS Rhodococcus oxybenzonivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK71981.1, ECO:0000313|Proteomes:UP000245711};
RN [1] {ECO:0000313|EMBL:AWK71981.1, ECO:0000313|Proteomes:UP000245711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-17 {ECO:0000313|EMBL:AWK71981.1,
RC ECO:0000313|Proteomes:UP000245711};
RA Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL Submitted (MAY-2017) 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; CP021354; AWK71981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2BTP3; -.
DR KEGG; roz:CBI38_10710; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000245711; Chromosome.
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; 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 PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000245711};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AWK71981.1}.
FT DOMAIN 5..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 397 AA; 40779 MW; 8B4D360BCA3BC0DB CRC64;
MTSSVIVAGA RTPMGRLMGS LKDLSGSDLG GIAIKGALEK AGVAPDQVEY VIMGQVLTAG
AGQMPARQAA VAAGIPMDVP ALTVNKVCLS GIDAIALADQ LIRAGEFEVV VAGGQESMSR
APHLLEKSRA GFKYGDVTMR DHMAFDGLHD IFTDQAMGNL TEARNKSDSV PVSREDQDAF
AAASHENAAR AWKDGLFADE VVPVSIPQRR GEPIVFGQDE GVRADTTVET LGRLRPAFAK
DGTVTAGSAS QISDGAAAVV VMSKAKAEEL GLEWLAEIGS HGVVAGPDST LQSQPARAIA
KACAKEGIDP KDLDLVEINE AFAAVGIVST RELGLDPAKV NVNGGAIAVG HPLGMSGARI
TLHLALELQR RGGGVGVAAL CGGGGQGDAL IVRVPKK
//
