FADI_ECO57
ID FADI_ECO57 Reviewed; 436 AA.
AC Q8XCN9; Q7ABX4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Z3605, ECs3225;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57470.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36648.1; -; Genomic_DNA.
DR PIR; A98032; A98032.
DR PIR; B85876; B85876.
DR RefSeq; NP_311252.1; NC_002695.1.
DR RefSeq; WP_000531969.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XCN9; -.
DR SMR; Q8XCN9; -.
DR STRING; 155864.EDL933_3510; -.
DR EnsemblBacteria; AAG57470; AAG57470; Z3605.
DR EnsemblBacteria; BAB36648; BAB36648; ECs_3225.
DR GeneID; 915678; -.
DR KEGG; ece:Z3605; -.
DR KEGG; ecs:ECs_3225; -.
DR PATRIC; fig|386585.9.peg.3367; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_6; -.
DR OMA; MTAFPEP; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transferase.
FT CHAIN 1..436
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206438"
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
