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Database: UniProt
Entry: A0A1T1ICF3_9PSED
LinkDB: A0A1T1ICF3_9PSED
Original site: A0A1T1ICF3_9PSED 
ID   A0A1T1ICF3_9PSED        Unreviewed;       425 AA.
AC   A0A1T1ICF3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OOV99897.1};
GN   ORFNames=MF4836_06590 {ECO:0000313|EMBL:OOV99897.1};
OS   Pseudomonas sp. MF4836.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV99897.1, ECO:0000313|Proteomes:UP000190183};
RN   [1] {ECO:0000313|Proteomes:UP000190183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA   Fagerlund A.;
RT   "Genome sequencing of bacteria from food industry.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {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:OOV99897.1}.
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DR   EMBL; MVOL01000002; OOV99897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1ICF3; -.
DR   STRING; 1960827.MF4836_06590; -.
DR   Proteomes; UP000190183; Unassembled WGS sequence.
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; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR   PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OOV99897.1}.
FT   DOMAIN          7..274
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          284..425
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        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        412
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   425 AA;  45391 MW;  67E22E0E4FFD7277 CRC64;
     MTQLRRVAII GGNRIPFARS NGPYATASNQ AMLTAALEGL IERYNLHGLR LGEVAAGAVL
     KHSRDFNLTR ECVLGSRLAP TTPAYDIQQA CGTGLEAALL VANKIALGQI ECGIAGGVDT
     TSDAPIGVNE GLRKILLQAN REKSLGDKLK TFLQLRPHHL KPELPRNGEP RTGLSMGEHC
     ELMAQTWNIP RAEQDQLALE SHQKMAAAYA EGWHNDLITP FLGLTRDNNL RPDLTLEKLA
     SLKPAFERSA KGTLTAGNST PLTDGASLVL LGSEAWAKER GLPVLAYLRD GEAAAVDFVN
     GAEGLLMAPV YAVPRLLARN GLTLQDFDYY EIHEAFAAQV LCTLKAWEDA DYCKNRLGLE
     APLGAIDRSR LNVKGSSLAA GHPFAATGGR IVANLAKLLE VAGQGRGLIS ICAAGGQGVT
     AIIER
//
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