ID   FADI_ECO27              Reviewed;         436 AA.
AC   B7UFZ9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01618};
DE            EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01618};
DE   AltName: Full=ACSs {ECO:0000255|HAMAP-Rule:MF_01618};
DE   AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01618};
DE   AltName: Full=Acyl-CoA ligase {ECO:0000255|HAMAP-Rule:MF_01618};
DE   AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01618};
DE   AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01618};
GN   Name=fadI {ECO:0000255|HAMAP-Rule:MF_01618}; OrderedLocusNames=E2348C_2481;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC       acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC       shorter is formed. {ECO:0000255|HAMAP-Rule:MF_01618}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01618};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01618}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC       (FadI). {ECO:0000255|HAMAP-Rule:MF_01618}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01618}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01618}.
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DR   EMBL; FM180568; CAS10029.1; -; Genomic_DNA.
DR   RefSeq; WP_000531916.1; NC_011601.1.
DR   AlphaFoldDB; B7UFZ9; -.
DR   SMR; B7UFZ9; -.
DR   EnsemblBacteria; CAS10029; CAS10029; E2348C_2481.
DR   KEGG; ecg:E2348C_2481; -.
DR   HOGENOM; CLU_031026_2_0_6; -.
DR   OMA; MTAFPEP; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   HAMAP; MF_01618; FadI; 1.
DR   InterPro; IPR012806; Ac-CoA_C-AcTrfase_FadI.
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   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   TIGRFAMs; TIGR02446; FadI; 1.
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; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..436
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_1000185957"
FT   ACT_SITE        99
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
FT   ACT_SITE        422
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01618"
SQ   SEQUENCE   436 AA;  46531 MW;  95F6EEE8E7CA8C25 CRC64;
     MGQVLPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAGDL GKMVVGELLA RTEIPAEVIE
     QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA TSFQAVANVA ESLMAGTIRA
     GIAGGADSSS VLPIGVSKKL ARVLVDVNKA RTMSQRLKLF SRLRLRDLMP VPPAVAEYST
     GLRMGDTAEQ MAKTYGITRE QQDALAHRSH QRAAQAWSEG KLKEEVMTAF IPPYKQPLVE
     DNNIRGNSSL ADYAKLRPAF DRKHGTVTAA NSTPLTDGAA AVILMTESRA KELGLVPLGY
     LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMSDLTLI DMHEAFAAQT LANIQLLGSE
     RFARDVLGRA HATGEVDDSK FNVLGGSIAY GHPFAATGAR MITQTLHELR RRGGGFGLVT
     ACAAGGLGAA MVLEAE