ID A0A0T6UIC2_9PSED Unreviewed; 383 AA.
AC A0A0T6UIC2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KRW57446.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KRW57446.1};
GN ORFNames=AO726_19675 {ECO:0000313|EMBL:KRW57446.1};
OS Pseudomonas sp. TTU2014-080ASC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW57446.1, ECO:0000313|Proteomes:UP000051864};
RN [1] {ECO:0000313|EMBL:KRW57446.1, ECO:0000313|Proteomes:UP000051864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW57446.1,
RC ECO:0000313|Proteomes:UP000051864};
RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA Loneragan G.H.;
RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT Cattle.";
RL Submitted (SEP-2015) 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:KRW57446.1}.
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DR EMBL; LKKK01000016; KRW57446.1; -; Genomic_DNA.
DR RefSeq; WP_058069835.1; NZ_LKKK01000016.1.
DR AlphaFoldDB; A0A0T6UIC2; -.
DR STRING; 1729724.AO726_19675; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000051864; 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; 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; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KRW57446.1}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 261..382
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 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 383 AA; 40696 MW; ABBA22494EAE95AB CRC64;
MTQAYIVDAL RTPTGKRKGS LAHVHAIDLG AHVLKALVER NSIPADEYDD VIFGCVDTIG
SQAGDIARTS WLAAGLPLCV PGTTVDRQCG SSQQALHFAA QAVMSGTQDV VAVGGVQTMT
QIPISSAMVA GQALGFSDPF SGSKGWQARF ADQPVNQFYA AQRIADHWSI SRAEMEAFAL
ESHRRALAAI EAGRFAREIV ACEGLQVDET PRATSLEKMA SLEPVDPAFP GITAAVSSQT
CDASAALLVV SEAALKRYNL TPRARIHTLS VRGDDPIWHL TAPIEATRFA LKKAGMSMAD
IDRVEINEAF ASVVMAWAKE LDYDPAQTNV NGGAIALGHP LGATGARLMT TLLHELERSG
GRYGLQTMCE GGGQANVTII ERL
//
