ID Q4KEA5_PSEF5 Unreviewed; 392 AA.
AC Q4KEA5;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AAY91594.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:AAY91594.1};
GN OrderedLocusNames=PFL_2321 {ECO:0000313|EMBL:AAY91594.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91594.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY91594.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY91594.1; -; Genomic_DNA.
DR RefSeq; WP_011060619.1; NC_004129.6.
DR AlphaFoldDB; Q4KEA5; -.
DR SMR; Q4KEA5; -.
DR STRING; 220664.PFL_2321; -.
DR KEGG; pfl:PFL_2321; -.
DR PATRIC; fig|220664.5.peg.2361; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_6; -.
DR Proteomes; UP000008540; Chromosome.
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; 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; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AAY91594.1}.
FT DOMAIN 4..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
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 392 AA; 40409 MW; EC99B5725B8F31BF CRC64;
MQDVVIVAAT RTAVGSFQGS LANIPAVDLG AAVIRQLLAQ TGIDPAQVDE VLMGQVLTAG
AGQNPARQAA IKAGLPHVVP AMTLNKVCGS GLKALHLGAQ AIRCGDAEVI IAGGQENMSL
SNYVLPGART GLRMGHSQMV DSMISDGLWD AFNDYHMGIT AENLVEKYGI SREAQDAFAA
ASQHKAAAAI EAGRFVDEIT PIQIPQRKGE PLTFATDEQP RPSTTAEALA KLKPAFKKDG
SVTAGNASAL NDGAAAVMLM SASKARALGL PVLAKIAAYA NAGVDPAIMG IGPVSATRRC
LDKAGWTLDQ LDLIEANEAF AAQSLSVAKE LEWDASKVNV NGGAIAIGHP IGASGCRVLV
TLLHEMIKRD AKKGLATLCI GGGQGVALAI ER
//
