ID F4CZ71_PSEUX Unreviewed; 393 AA.
AC F4CZ71;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AEA24775.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:AEA24775.1};
GN OrderedLocusNames=Psed_2572 {ECO:0000313|EMBL:AEA24775.1};
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:AEA24775.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA24775.1, 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; AEA24775.1; -; Genomic_DNA.
DR RefSeq; WP_013674699.1; NC_015312.1.
DR AlphaFoldDB; F4CZ71; -.
DR STRING; 675635.Psed_2572; -.
DR KEGG; pdx:Psed_2572; -.
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:AEA24775.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AEA24775.1}.
FT DOMAIN 5..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..391
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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40173 MW; 2FEAFC16472D7818 CRC64;
MDEPFVIDAV RSPMGRGKPG GALSGVHAVD LLAATVAALL ERTGVDPGRI DDVVTGCVSQ
AGEQSGNVGR MAWLAAGFPE HVPSVTVERK CGSSQQAVHF AAQGILAGAY DLVVVAGVES
MSRVPMGSAR LGADPYGPSV AARYAPGLVA QGVSAELVAA RWKLSREQLD DYAARSHARA
AAAADSGGFD REIVPIPLPD GGAVTADESI RRGTTPAKLA TLAPAFADDA TAARFPEIRW
SITAGNSSQI TDGASAMLLA SGRAAAELGL TPRARFRGFA VCGDDPVEML TAPIPATRRL
LDRAGLTIAD VDLYEVNEAF ASVPLAWQAA FDADPDRLNV RGGAIALGHP LGASGARVAT
TLLGALEARG GGLGLQTMCE AGGMANAMLL ETV
//
