ID A0A010RTW9_PSEFL Unreviewed; 394 AA.
AC A0A010RTW9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:EXF95746.1};
GN ORFNames=HK44_020230 {ECO:0000313|EMBL:EXF95746.1};
OS Pseudomonas fluorescens HK44.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF95746.1, ECO:0000313|Proteomes:UP000022611};
RN [1] {ECO:0000313|EMBL:EXF95746.1, ECO:0000313|Proteomes:UP000022611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK44 {ECO:0000313|EMBL:EXF95746.1,
RC ECO:0000313|Proteomes:UP000022611};
RX PubMed=21742869; DOI=10.1128/JB.05530-11;
RA Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA Karpinets T.V., Brown S.D., Sayler G.S.;
RT "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT HK44.";
RL J. Bacteriol. 193:5009-5010(2011).
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:EXF95746.1}.
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DR EMBL; AFOY02000004; EXF95746.1; -; Genomic_DNA.
DR RefSeq; WP_019689865.1; NZ_AFOY02000004.1.
DR AlphaFoldDB; A0A010RTW9; -.
DR PATRIC; fig|1042209.11.peg.569; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_6; -.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000022611; 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; -; 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; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000022611};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 6..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..393
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 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40817 MW; 536313A3FB1BAC21 CRC64;
MNPSDIFVVS AVRSAIGSFG GSLKDVPPIQ LATDVCRAAI ERSGLAPELI GHAVMGHVIP
TEARDAYISR AVAMNAGLPK ETPAFNVNRL CGSGLQAIVS AAQSLMLGDA GAALAGGVES
MSRGAYLLPQ ARWGARMGDI QGIDYMLGVL QDPFAGFHMG ITAENIAEHY GISRQTQDQL
ALLSQQRAAR AIAEGRFAGQ IVPIEVASRK GTVSFSTDEH VRAEVSFEQL SGMKPAFKKD
GSVTAGNASG LNDGAGALIM ATGQVVQEQG LKPMARLVGY AHAGVEPSMM GLGPIPATRL
VLKRAGLTVA DLDVIESNEA FAAQACAVAQ ELGFDPEKVN PNGSGISLGH PVGATGAIIA
TKAIHELHRI QGRYALATMC IGGGQGIAVL FERV
//
