ID Q128W3_POLSJ Unreviewed; 401 AA.
AC Q128W3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:ABE44929.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABE44929.1};
GN OrderedLocusNames=Bpro_3015 {ECO:0000313|EMBL:ABE44929.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44929.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE44929.1; -; Genomic_DNA.
DR RefSeq; WP_011483927.1; NC_007948.1.
DR AlphaFoldDB; Q128W3; -.
DR STRING; 296591.Bpro_3015; -.
DR KEGG; pol:Bpro_3015; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_4; -.
DR OrthoDB; 8523144at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase 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; 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; 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 ECO:0000313|EMBL:ABE44929.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABE44929.1}.
FT DOMAIN 5..269
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 279..400
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 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 401 AA; 42121 MW; 672E60810DAFC804 CRC64;
MTEAFIYDAI RTPRGKGKKD GSLHEVKPVN LLAGVLTELQ RRNGFDTAAI DDVVMGVVSP
VGEQGAVIAK VAALRAGWDF RASGVQVNRF CASGLEAVNL AAQKVRSGWE DLVVAGGVES
MSRVPIGSDG GAWAQDPETN SATLFVPQGI GADLIATIEG FSRAEVDAFA LQSQQRAAAA
RSAGHFFNSV VPVKDPLGQI ILGEDEFIKP HTTLEGLAQL KPAFEQLGAM GFDAVALQRY
PQVERIQHVH HAGNSSGIVD GAAAVLIGSD AAGRTHGLQP RARIVAAALS GADPTIMLTG
PMPATRKVLA KAGMTVEQID LFEVNEAFAA VVMRFMKEMQ VPHEKINVNG GAIAMGHPLG
ATGAMILGTL VDELHRRQLR YGLATLCVGG GMGIATIVER V
//
