PAAJ_ECOLI
ID PAAJ_ECOLI Reviewed; 401 AA.
AC P0C7L2; O53017; P77525;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase;
DE EC=2.3.1.174 {ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314};
DE EC=2.3.1.223 {ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314};
GN Name=paaJ; Synonyms=paaE, ydbW; OrderedLocusNames=b1397, JW1392;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN PHENYLACETATE CATABOLISM, AND INDUCTION.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA Garcia J.L., Diaz E.;
RT "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT new aerobic hybrid pathway.";
RL J. Biol. Chem. 273:25974-25986(1998).
RN [5]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10766858; DOI=10.1074/jbc.275.16.12214;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Transcriptional regulation of the divergent paa catabolic operons for
RT phenylacetic acid degradation in Escherichia coli.";
RL J. Biol. Chem. 275:12214-12222(2000).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12846838; DOI=10.1046/j.1432-1033.2003.03683.x;
RA Ismail W., El-Said Mohamed M., Wanner B.L., Datsenko K.A., Eisenreich W.,
RA Rohdich F., Bacher A., Fuchs G.;
RT "Functional genomics by NMR spectroscopy. Phenylacetate catabolism in
RT Escherichia coli.";
RL Eur. J. Biochem. 270:3047-3054(2003).
RN [7]
RP FUNCTION AS A 3-OXOADIPYL-COA THIOLASE, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17259607; DOI=10.1099/mic.0.2006/002444-0;
RA Nogales J., Macchi R., Franchi F., Barzaghi D., Fernandez C., Garcia J.L.,
RA Bertoni G., Diaz E.;
RT "Characterization of the last step of the aerobic phenylacetic acid
RT degradation pathway.";
RL Microbiology 153:357-365(2007).
RN [8]
RP FUNCTION AS A BETA-KETOADIPYL-COA THIOLASE, AND CATALYTIC ACTIVITY.
RX PubMed=20660314; DOI=10.1073/pnas.1005399107;
RA Teufel R., Mascaraque V., Ismail W., Voss M., Perera J., Eisenreich W.,
RA Haehnel W., Fuchs G.;
RT "Bacterial phenylalanine and phenylacetate catabolic pathway revealed.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14390-14395(2010).
CC -!- FUNCTION: Catalyzes the thiolytic cleavage of the beta-keto C8
CC intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6
CC intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes
CC also the last step of the pathway, in which 3-oxoadipyl-CoA similarly
CC is cleaved to acetyl-CoA and succinyl-CoA.
CC {ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA;
CC Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174;
CC Evidence={ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-didehydroadipoyl-CoA + acetyl-CoA = 3-oxo-5,6-
CC didehydrosuberyl-CoA + CoA; Xref=Rhea:RHEA:34799, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:63255, ChEBI:CHEBI:71044;
CC EC=2.3.1.223; Evidence={ECO:0000269|PubMed:17259607,
CC ECO:0000269|PubMed:20660314};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP), integration host
CC factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX
CC from binding its target sequences. Inhibited by PaaX.
CC {ECO:0000269|PubMed:10766858, ECO:0000269|PubMed:9748275}.
CC -!- DISRUPTION PHENOTYPE: Mutants are unable to use phenylacetate as a
CC carbon source. {ECO:0000269|PubMed:12846838}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; U00096; AAC74479.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15002.1; -; Genomic_DNA.
DR PIR; H64890; H64890.
DR RefSeq; NP_415915.1; NC_000913.3.
DR RefSeq; WP_001206197.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P0C7L2; -.
DR SMR; P0C7L2; -.
DR BioGRID; 4263012; 239.
DR IntAct; P0C7L2; 5.
DR STRING; 511145.b1397; -.
DR PaxDb; P0C7L2; -.
DR PRIDE; P0C7L2; -.
DR EnsemblBacteria; AAC74479; AAC74479; b1397.
DR EnsemblBacteria; BAA15002; BAA15002; BAA15002.
DR GeneID; 946121; -.
DR KEGG; ecj:JW1392; -.
DR KEGG; eco:b1397; -.
DR PATRIC; fig|1411691.4.peg.874; -.
DR EchoBASE; EB3507; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_2_6; -.
DR InParanoid; P0C7L2; -.
DR OMA; MSRVPMW; -.
DR PhylomeDB; P0C7L2; -.
DR BioCyc; EcoCyc:G6718-MON; -.
DR BioCyc; MetaCyc:G6718-MON; -.
DR UniPathway; UPA00930; -.
DR PRO; PR:P0C7L2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IDA:UniProtKB.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IDA:EcoCyc.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:UniProtKB.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012793; PcaF.
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; TIGR02430; pcaF; 1.
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; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA
FT thiolase"
FT /id="PRO_0000206421"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 401 AA; 42277 MW; 6B8C26ECB4CFEC00 CRC64;
MREAFICDGI RTPIGRYGGA LSSVRADDLA AIPLRELLVR NPRLDAECID DVILGCANQA
GEDNRNVARM ATLLAGLPQS VSGTTINRLC GSGLDALGFA ARAIKAGDGD LLIAGGVESM
SRAPFVMGKA ASAFSRQAEM FDTTIGWRFV NPLMAQQFGT DSMPETAENV AELLKISRED
QDSFALRSQQ RTAKAQSSGI LAEEIVPVVL KNKKGVVTEI QHDEHLRPET TLEQLRGLKA
PFRANGVITA GNASGVNDGA AALIIASEQM AAAQGLTPRA RIVAMATAGV EPRLMGLGPV
PATRRVLERA GLSIHDMDVI ELNEAFAAQA LGVLRELGLP DDAPHVNPNG GAIALGHPLG
MSGARLALAA SHELHRRNGR YALCTMCIGV GQGIAMILER V
