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FADI_ECO5E
ID   FADI_ECO5E              Reviewed;         436 AA.
AC   B5YXY5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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};
GN   OrderedLocusNames=ECH74115_3485;
OS   Escherichia coli O157:H7 (strain EC4115 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=444450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC4115 / EHEC;
RX   PubMed=22135463; DOI=10.1073/pnas.1107176108;
RA   Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Genomic anatomy of Escherichia coli O157:H7 outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011).
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; CP001164; ACI39254.1; -; Genomic_DNA.
DR   RefSeq; WP_000531969.1; NC_011353.1.
DR   AlphaFoldDB; B5YXY5; -.
DR   SMR; B5YXY5; -.
DR   KEGG; ecf:ECH74115_3485; -.
DR   HOGENOM; CLU_031026_2_0_6; -.
DR   OMA; MTAFPEP; -.
DR   UniPathway; UPA00659; -.
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_1000185960"
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;  46515 MW;  CAF29933A8282D5E CRC64;
     MGQVLPLVTR QGDRIAIVSG LRTPFARQAT AFHGIPAVDL GKMVVGELLA RSEIPAEVIE
     QLVFGQVVQM PEAPNIAREI VLGTGMNVHT DAYSVSRACA TSFQAVANVV ESLMAGTIRA
     GIAGGADSSS VLPIGVSKKL ARVLVDVNKA RTMSQRLKLF SRLRLRDLMP VPPAVAEYST
     GLRMGDTAEQ MAKTYGITRE QQDALAHRSH QRAAQAWSDG KLKEEVMTAF IPPYKQLLAE
     DNNIRGNSSL ADFAKLRPAF DRKHGTVTAA NSTPLTDGAA AVILMTESRA KELGLVPLGY
     LRSYAFTAID VWQDMLLGPA WSTPLALERA GLTMADLTLI DMHEAFAAQT LANIQLLGSE
     RFAREALGRA HATGEVDDSK FNVLGGSIAY GHPFAATGAR MITQTLHELR RRGGGFGLVT
     ACAAGGLGAA MVLEAE
 
 
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