PAAA_ECOLI
ID PAAA_ECOLI Reviewed; 309 AA.
AC P76077; O53010; Q2MBD3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=1,2-phenylacetyl-CoA epoxidase, subunit A;
DE EC=1.14.13.149;
DE AltName: Full=1,2-phenylacetyl-CoA epoxidase, catalytic subunit alpha;
DE AltName: Full=1,2-phenylacetyl-CoA monooxygenase, subunit A;
GN Name=paaA; Synonyms=ydbO; OrderedLocusNames=b1388, JW1383;
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 / 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 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 [5]
RP FUNCTION AS A MONOOXYGENASE.
RX PubMed=16997993; DOI=10.1128/aem.01550-06;
RA Fernandez C., Ferrandez A., Minambres B., Diaz E., Garcia J.L.;
RT "Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the
RT aerobic phenylacetic acid degradation pathway of Escherichia coli.";
RL Appl. Environ. Microbiol. 72:7422-7426(2006).
RN [6]
RP SUBUNIT.
RX PubMed=20823522; DOI=10.1107/s174430911002748x;
RA Grishin A.M., Ajamian E., Zhang L., Cygler M.;
RT "Crystallization and preliminary X-ray analysis of PaaAC, the main
RT component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme
RT A oxygenase complex.";
RL Acta Crystallogr. F 66:1045-1049(2010).
RN [7]
RP FUNCTION AS AN EPOXYDASE, 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-309 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, FUNCTION AS A MONOOXYGENASE, COFACTOR, AND SUBUNIT.
RX PubMed=21247899; DOI=10.1074/jbc.m110.194423;
RA Grishin A.M., Ajamian E., Tao L., Zhang L., Menard R., Cygler M.;
RT "Structural and functional studies of the Escherichia coli phenylacetyl-CoA
RT monooxygenase complex.";
RL J. Biol. Chem. 286:10735-10743(2011).
CC -!- FUNCTION: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent
CC enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-
CC CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic
CC subunit involved in the incorporation of one atom of molecular oxygen
CC into phenylacetyl-CoA. {ECO:0000269|PubMed:16997993,
CC ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:21247899,
CC ECO:0000269|PubMed:9748275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + phenylacetyl-CoA = 2-(1,2-epoxy-1,2-
CC dihydrophenyl)acetyl-CoA + H2O + NADP(+); Xref=Rhea:RHEA:32171,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57390, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:63458; EC=1.14.13.149;
CC Evidence={ECO:0000269|PubMed:20660314};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Forms a stable heterotetramer (dimer of heterodimers) with
CC PaaC. {ECO:0000269|PubMed:20823522, ECO:0000269|PubMed:21247899}.
CC -!- INTERACTION:
CC P76077; P76079: paaC; NbExp=6; IntAct=EBI-1119536, EBI-1131666;
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA66090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97452; CAA66090.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74470.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76423.1; -; Genomic_DNA.
DR PIR; G64889; G64889.
DR RefSeq; NP_415906.1; NC_000913.3.
DR RefSeq; WP_000191077.1; NZ_SSZK01000012.1.
DR PDB; 3PVR; X-ray; 2.10 A; A=2-309.
DR PDB; 3PVT; X-ray; 2.03 A; A=2-309.
DR PDB; 3PVY; X-ray; 2.15 A; A=2-309.
DR PDB; 3PW1; X-ray; 2.25 A; A=2-309.
DR PDB; 3PW8; X-ray; 2.97 A; C/D=2-309.
DR PDB; 3PWQ; X-ray; 2.65 A; C/D/F/H=2-309.
DR PDB; 4II4; X-ray; 2.80 A; A=2-309.
DR PDBsum; 3PVR; -.
DR PDBsum; 3PVT; -.
DR PDBsum; 3PVY; -.
DR PDBsum; 3PW1; -.
DR PDBsum; 3PW8; -.
DR PDBsum; 3PWQ; -.
DR PDBsum; 4II4; -.
DR AlphaFoldDB; P76077; -.
DR SMR; P76077; -.
DR BioGRID; 4261392; 123.
DR ComplexPortal; CPX-2844; paaABCE phenylacetyl-CoA monooxygenase complex.
DR IntAct; P76077; 4.
DR STRING; 511145.b1388; -.
DR PaxDb; P76077; -.
DR PRIDE; P76077; -.
DR DNASU; 945833; -.
DR EnsemblBacteria; AAC74470; AAC74470; b1388.
DR EnsemblBacteria; BAE76423; BAE76423; BAE76423.
DR GeneID; 945833; -.
DR KEGG; ecj:JW1383; -.
DR KEGG; eco:b1388; -.
DR PATRIC; fig|1411691.4.peg.883; -.
DR EchoBASE; EB3499; -.
DR eggNOG; COG3396; Bacteria.
DR HOGENOM; CLU_879733_0_0_6; -.
DR InParanoid; P76077; -.
DR OMA; MQPEANW; -.
DR PhylomeDB; P76077; -.
DR BioCyc; EcoCyc:G6709-MON; -.
DR BioCyc; MetaCyc:G6709-MON; -.
DR UniPathway; UPA00930; -.
DR EvolutionaryTrace; P76077; -.
DR PRO; PR:P76077; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0062077; C:phenylacetyl-CoA 1,2-epoxidase complex; IPI:ComplexPortal.
DR GO; GO:0097266; F:phenylacetyl-CoA 1,2-epoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010124; P:phenylacetate catabolic process; IDA:ComplexPortal.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011881; PaaA.
DR InterPro; IPR007814; PaaA_PaaC.
DR Pfam; PF05138; PaaA_PaaC; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR02156; PA_CoA_Oxy1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..309
FT /note="1,2-phenylacetyl-CoA epoxidase, subunit A"
FT /id="PRO_0000058159"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21247899"
FT VARIANT 210
FT /note="T -> A (in strain: W)"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 25..44
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 59..84
FT /evidence="ECO:0007829|PDB:3PVT"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:3PVT"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 142..170
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 174..193
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 218..235
FT /evidence="ECO:0007829|PDB:3PVT"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3PVT"
FT TURN 249..252
FT /evidence="ECO:0007829|PDB:3PVT"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:3PVT"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3PWQ"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:3PVT"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:3PVT"
SQ SEQUENCE 309 AA; 35499 MW; 83AEC6D7AC084073 CRC64;
MTQEERFEQR IAQETAIEPQ DWMPDAYRKT LIRQIGQHAH SEIVGMLPEG NWITRAPTLR
RKAILLAKVQ DEAGHGLYLY SAAETLGCAR EDIYQKMLDG RMKYSSIFNY PTLSWADIGV
IGWLVDGAAI VNQVALCRTS YGPYARAMVK ICKEESFHQR QGFEACMALA QGSEAQKQML
QDAINRFWWP ALMMFGPNDD NSPNSARSLT WKIKRFTNDE LRQRFVDNTV PQVEMLGMTV
PDPDLHFDTE SGHYRFGEID WQEFNEVING RGICNQERLD AKRKAWEEGT WVREAALAHA
QKQHARKVA
