FADA_ECOL6
ID FADA_ECOL6 Reviewed; 387 AA.
AC Q8FBI3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01620};
GN Name=fadA {ECO:0000255|HAMAP-Rule:MF_01620}; OrderedLocusNames=c4792;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. Involved in the aerobic and anaerobic degradation of
CC long-chain fatty acids (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_01620}.
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_01620};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01620}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01620}.
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DR EMBL; AE014075; AAN83225.1; -; Genomic_DNA.
DR RefSeq; WP_000438745.1; NC_004431.1.
DR AlphaFoldDB; Q8FBI3; -.
DR SMR; Q8FBI3; -.
DR STRING; 199310.c4792; -.
DR EnsemblBacteria; AAN83225; AAN83225; c4792.
DR KEGG; ecc:c4792; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_6; -.
DR OMA; DYYWGMG; -.
DR BioCyc; ECOL199310:C4792-MON; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001410; 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; -; 2.
DR HAMAP; MF_01620; FadA; 1.
DR InterPro; IPR012805; FadA.
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; TIGR02445; fadA; 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..387
FT /note="3-ketoacyl-CoA thiolase"
FT /id="PRO_0000206374"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ SEQUENCE 387 AA; 40775 MW; 505E4A821C40C007 CRC64;
MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ
TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT
QSGAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVS GTVTAGTSSA
LSDGAAAMLV MSESRARDLG LKPRACVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS
DIGVFEMNEA FAAQILPCIK DLGLMEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM
ERKDVQFGLA TMCIGLGQGI ATVFERV