PAAG_ECOLI
ID PAAG_ECOLI Reviewed; 262 AA.
AC P77467; O53015;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1,2-epoxyphenylacetyl-CoA isomerase;
DE EC=5.3.3.18;
GN Name=paaG; Synonyms=ydbT; OrderedLocusNames=b1394, JW1389;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM,
RP 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 [2]
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 [3]
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 [4]
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 [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 FUNCTION IN PHENYLACETATE CATABOLISM, AND 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 AN ISOMERASE.
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 reversible conversion of the epoxide to 2-
CC oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).
CC {ECO:0000269|PubMed:12846838, ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-oxepin-2(3H)-
CC ylideneacetyl-CoA; Xref=Rhea:RHEA:31843, ChEBI:CHEBI:63252,
CC ChEBI:CHEBI:63458; EC=5.3.3.18;
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- INTERACTION:
CC P77467; P76082: paaF; NbExp=3; IntAct=EBI-1118484, EBI-1115747;
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 accumulate ring-1,2-dihydroxy-1,2-
CC dihydrophenylacetyl lactone and are unable to use phenylacetate as a
CC carbon source. {ECO:0000269|PubMed:12846838}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; X97452; CAA66096.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74476.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15000.1; -; Genomic_DNA.
DR PIR; E64890; E64890.
DR RefSeq; NP_415912.1; NC_000913.3.
DR RefSeq; WP_000969777.1; NZ_STEB01000005.1.
DR RefSeq; WP_000969784.1; NZ_SSZK01000012.1.
DR PDB; 4FZW; X-ray; 2.55 A; C/D=1-262.
DR PDBsum; 4FZW; -.
DR AlphaFoldDB; P77467; -.
DR SMR; P77467; -.
DR BioGRID; 4260969; 375.
DR BioGRID; 850622; 7.
DR ComplexPortal; CPX-5681; Enoyl CoA hydratase/isomerase complex.
DR IntAct; P77467; 10.
DR STRING; 511145.b1394; -.
DR PaxDb; P77467; -.
DR PRIDE; P77467; -.
DR EnsemblBacteria; AAC74476; AAC74476; b1394.
DR EnsemblBacteria; BAA15000; BAA15000; BAA15000.
DR GeneID; 946263; -.
DR KEGG; ecj:JW1389; -.
DR KEGG; eco:b1394; -.
DR PATRIC; fig|1411691.4.peg.877; -.
DR EchoBASE; EB3504; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_2_6; -.
DR InParanoid; P77467; -.
DR OMA; DPDLHWK; -.
DR PhylomeDB; P77467; -.
DR BioCyc; EcoCyc:G6715-MON; -.
DR BRENDA; 5.3.3.18; 2026.
DR UniPathway; UPA00930; -.
DR PRO; PR:P77467; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902494; C:catalytic complex; IPI:ComplexPortal.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0016853; F:isomerase activity; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:EcoCyc.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR InterPro; IPR011968; PaaB1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR02280; PaaB1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Lyase; Reference proteome.
FT CHAIN 1..262
FT /note="1,2-epoxyphenylacetyl-CoA isomerase"
FT /id="PRO_0000109331"
FT VARIANT 121
FT /note="G -> C (in strain: W)"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4FZW"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4FZW"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4FZW"
SQ SEQUENCE 262 AA; 28405 MW; DD7B95B30D88660C CRC64;
MMEFILSHVE KGVMTLTLNR PERLNSFNDE MHAQLAECLK QVERDDTIRC LLLTGAGRGF
CAGQDLNDRN VDPTGPAPDL GMSVERFYNP LVRRLAKLPK PVICAVNGVA AGAGATLALG
GDIVIAARSA KFVMAFSKLG LIPDCGGTWL LPRVAGRARA MGLALLGNQL SAEQAHEWGM
IWQVVDDETL ADTAQQLARH LATQPTFGLG LIKQAINSAE TNTLDTQLDL ERDYQRLAGR
SADYREGVSA FLAKRSPQFT GK
