PAAF_ECOLI
ID PAAF_ECOLI Reviewed; 255 AA.
AC P76082; O53014; P78288;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=2,3-dehydroadipyl-CoA hydratase;
DE EC=4.2.1.17;
DE AltName: Full=Enoyl-CoA hydratase;
GN Name=paaF; Synonyms=ydbR; OrderedLocusNames=b1393, JW1388;
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 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 ENOYL-COA HYDRATASE, 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 reversible conversion of enzymatically produced
CC 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA.
CC {ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000269|PubMed:20660314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000269|PubMed:20660314};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- INTERACTION:
CC P76082; P77467: paaG; NbExp=3; IntAct=EBI-1115747, EBI-1118484;
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 delta3-dehydroadipate and are
CC unable to use phenylacetate as a carbon source.
CC {ECO:0000269|PubMed:12846838}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; X97452; CAA66095.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74475.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14999.2; -; Genomic_DNA.
DR PIR; D64890; D64890.
DR RefSeq; NP_415911.1; NC_000913.3.
DR RefSeq; WP_001292353.1; NZ_STEB01000005.1.
DR PDB; 4FZW; X-ray; 2.55 A; A/B=1-255.
DR PDBsum; 4FZW; -.
DR AlphaFoldDB; P76082; -.
DR SMR; P76082; -.
DR BioGRID; 4260970; 248.
DR ComplexPortal; CPX-5681; Enoyl CoA hydratase/isomerase complex.
DR DIP; DIP-10425N; -.
DR IntAct; P76082; 2.
DR STRING; 511145.b1393; -.
DR PaxDb; P76082; -.
DR PRIDE; P76082; -.
DR EnsemblBacteria; AAC74475; AAC74475; b1393.
DR EnsemblBacteria; BAA14999; BAA14999; BAA14999.
DR GeneID; 946011; -.
DR KEGG; ecj:JW1388; -.
DR KEGG; eco:b1393; -.
DR PATRIC; fig|1411691.4.peg.878; -.
DR EchoBASE; EB3503; -.
DR eggNOG; COG1024; Bacteria.
DR HOGENOM; CLU_009834_7_6_6; -.
DR InParanoid; P76082; -.
DR OMA; GLRFERH; -.
DR PhylomeDB; P76082; -.
DR BioCyc; EcoCyc:G6714-MON; -.
DR BRENDA; 4.2.1.17; 2026.
DR UniPathway; UPA00930; -.
DR PRO; PR:P76082; -.
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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="2,3-dehydroadipyl-CoA hydratase"
FT /id="PRO_0000109330"
FT VARIANT 11
FT /note="R -> Q (in strain: W)"
FT VARIANT 32
FT /note="M -> T (in strain: W)"
FT VARIANT 45
FT /note="T -> S (in strain: W)"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:4FZW"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4FZW"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 217..232
FT /evidence="ECO:0007829|PDB:4FZW"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:4FZW"
SQ SEQUENCE 255 AA; 27237 MW; 828C45DD658CAD1D CRC64;
MSELIVSRQQ RVLLLTLNRP AARNALNNAL LMQLVNELEA AATDTSISVC VITGNARFFA
AGADLNEMAE KDLAATLNDT RPQLWARLQA FNKPLIAAVN GYALGAGCEL ALLCDVVVAG
ENARFGLPEI TLGIMPGAGG TQRLIRSVGK SLASKMVLSG ESITAQQAQQ AGLVSDVFPS
DLTLEYALQL ASKMARHSPL ALQAAKQALR QSQEVALQAG LAQERQLFTL LAATEDRHEG
ISAFLQKRTP DFKGR
