ID FADA_ECOLI Reviewed; 387 AA.
AC P21151; P78130; Q2M8E8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 3.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=3-ketoacyl-CoA thiolase FadA;
DE EC=2.3.1.16 {ECO:0000269|PubMed:8454629};
DE AltName: Full=Acetyl-CoA acyltransferase;
DE AltName: Full=Beta-ketothiolase;
DE AltName: Full=Fatty acid oxidation complex subunit beta;
GN Name=fadA; Synonyms=oldA; OrderedLocusNames=b3845, JW5578;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1699931; DOI=10.1128/jb.172.11.6459-6468.1990;
RA Dirusso C.C.;
RT "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty
RT acid-oxidizing multienzyme complex, indicates a high degree of homology to
RT eucaryotic enzymes.";
RL J. Bacteriol. 172:6459-6468(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=2191949; DOI=10.1016/s0021-9258(18)86963-0;
RA Yang S.-Y., Yang X.-Y.H., Healy-Louie G., Schulz H., Elzinga M.;
RT "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-
RT coenzyme A thiolase from Escherichia coli and the structural organization
RT of the fadAB operon.";
RL J. Biol. Chem. 265:10424-10429(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2204034; DOI=10.1093/nar/18.16.4937;
RA Nakahigashi K., Inokuchi H.;
RT "Nucleotide sequence of the fadA and fadB genes from Escherichia coli.";
RL Nucleic Acids Res. 18:4937-4937(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP SEQUENCE REVISION TO 37.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=368024; DOI=10.1128/jb.137.1.469-473.1979;
RA Pramanik A., Pawar S., Antonian E., Schulz H.;
RT "Five different enzymatic activities are associated with the multienzyme
RT complex of fatty acid oxidation from Escherichia coli.";
RL J. Bacteriol. 137:469-473(1979).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8454629; DOI=10.1016/s0021-9258(18)53291-9;
RA Yang S.Y., Elzinga M.;
RT "Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme
RT A epimerase with an active site in the amino-terminal domain of the
RT multifunctional fatty acid oxidation protein from Escherichia coli.";
RL J. Biol. Chem. 268:6588-6592(1993).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [11]
RP FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
RA Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
RT "A new Escherichia coli metabolic competency: growth on fatty acids by a
RT novel anaerobic beta-oxidation pathway.";
RL Mol. Microbiol. 47:793-805(2003).
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. {ECO:0000269|PubMed:12535077,
CC ECO:0000269|PubMed:368024, ECO:0000269|PubMed:8454629}.
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:0000269|PubMed:8454629};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000269|PubMed:8454629};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96 uM for acetoacetyl-CoA {ECO:0000269|PubMed:8454629};
CC KM=102 uM for CoASH {ECO:0000269|PubMed:8454629};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC (FadA). {ECO:0000269|PubMed:368024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of,
CC at least, 12 carbon atoms). When LCFAs are present in the medium, they
CC are converted to long-chain acyl-CoAs which bind to FadR resulting in
CC its release from the DNA and thus derepression of the transcription.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; M59368; AAA23751.1; -; Genomic_DNA.
DR EMBL; M74164; AAA62778.1; -; Genomic_DNA.
DR EMBL; X52837; CAB40810.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67642.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48230.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77458.1; -; Genomic_DNA.
DR PIR; F65189; XUEC.
DR RefSeq; WP_000438725.1; NZ_SSZK01000046.1.
DR RefSeq; YP_026272.1; NC_000913.3.
DR AlphaFoldDB; P21151; -.
DR SASBDB; P21151; -.
DR SMR; P21151; -.
DR BioGRID; 4263456; 162.
DR ComplexPortal; CPX-3964; fadBA fatty acid oxidation complex, aerobic conditions.
DR DIP; DIP-9559N; -.
DR STRING; 511145.b3845; -.
DR jPOST; P21151; -.
DR PaxDb; 511145-b3845; -.
DR EnsemblBacteria; AAT48230; AAT48230; b3845.
DR GeneID; 948324; -.
DR KEGG; ecj:JW5578; -.
DR KEGG; eco:b3845; -.
DR PATRIC; fig|511145.12.peg.3959; -.
DR EchoBASE; EB0274; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_6; -.
DR InParanoid; P21151; -.
DR OMA; RWCASSM; -.
DR OrthoDB; 9764638at2; -.
DR PhylomeDB; P21151; -.
DR BioCyc; EcoCyc:FADA-MONOMER; -.
DR BioCyc; MetaCyc:FADA-MONOMER; -.
DR BRENDA; 2.3.1.16; 2026.
DR SABIO-RK; P21151; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:P21151; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IDA:EcoCyc.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:ComplexPortal.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:EcoCyc.
DR GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR NCBIfam; TIGR02445; fadA; 1.
DR PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Fatty acid metabolism; Lipid degradation; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="3-ketoacyl-CoA thiolase FadA"
FT /id="PRO_0000206372"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="S -> T (in Ref. 3; CAB40810 and 4; AAA67642)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> G (in Ref. 3; CAB40810)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..374
FT /note="TMCI -> DGCVS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 40876 MW; 1A60EF1E6C351704 CRC64;
MEQVVIVDAI RTPMGRSKGG AFRNVRAEDL SAHLMRSLLA RNPALEAAAL DDIYWGCVQQ
TLEQGFNIAR NAALLAEVPH SVPAVTVNRL CGSSMQALHD AARMIMTGDA QACLVGGVEH
MGHVPMSHGV DFHPGLSRNV AKAAGMMGLT AEMLARMHGI SREMQDAFAA RSHARAWAAT
QSAAFKNEII PTGGHDADGV LKQFNYDEVI RPETTVEALA TLRPAFDPVN GMVTAGTSSA
LSDGAAAMLV MSESRAHELG LKPRARVRSM AVVGCDPSIM GYGPVPASKL ALKKAGLSAS
DIGVFEMNEA FAAQILPCIK DLGLIEQIDE KINLNGGAIA LGHPLGCSGA RISTTLLNLM
ERKDVQFGLA TMCIGLGQGI ATVFERV
//
