ID F4CPY3_PSEUX Unreviewed; 381 AA.
AC F4CPY3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AEA26166.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:AEA26166.1};
GN OrderedLocusNames=Psed_4000 {ECO:0000313|EMBL:AEA26166.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA26166.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA26166.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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; CP002593; AEA26166.1; -; Genomic_DNA.
DR RefSeq; WP_013676082.1; NC_015312.1.
DR AlphaFoldDB; F4CPY3; -.
DR STRING; 675635.Psed_4000; -.
DR KEGG; pdx:Psed_4000; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_11; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
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:AEA26166.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AEA26166.1}.
FT DOMAIN 5..249
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 258..379
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 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 381 AA; 39406 MW; 1F3E1B2CCB188492 CRC64;
MRDAVIVEAV RTPVGRRKGG LAGVHPADLS AHVLRSLAER SGVDPAVVDD VIWGCVSQSG
EQTFDIGRTA VLSAGWPETV PGVTVDRQCG SSQQSIHFAA AGLIAGQYDV VVAGGVESMT
RVPMGSASNG ARPFGTDFDA RYGGVTPDQG IGAEMIAERW GFSRTQVDEF SLASHEKAAH
AQDEGRFEGQ IAPVTTPDGT VVSADEGIRR GGTLETLGAL KTVFREDGVV TAGNASQISD
GSAALLMTTS EKAAELGLTP IARIHTAVLA AADPVIMLTA PMPATEKALS RSGLSMDQIG
VFEVNEAFAS VPLAWLADIG ADPKTLNPNG GAIALGHPLG ASGARIMTTM VHHMRDNGIR
YGLQTMCEGG GQANATIVEL L
//
