PAAE_ECOLI
ID PAAE_ECOLI Reviewed; 356 AA.
AC P76081; O53013; P77233;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=1,2-phenylacetyl-CoA epoxidase, subunit E;
DE EC=1.-.-.-;
DE AltName: Full=1,2-phenylacetyl-CoA epoxidase, reductase subunit;
DE AltName: Full=1,2-phenylacetyl-CoA monooxygenase, subunit E;
GN Name=paaE; Synonyms=ydbR; OrderedLocusNames=b1392, JW1387;
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 INDUCTION.
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 AS A REDUCTASE.
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 [7]
RP FUNCTION AS A MONOOXYGENASE COMPONENT.
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 FUNCTION AS A REDUCTASE, AND COFACTOR.
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 E is a reductase
CC with a preference for NADPH and FAD, capable of reducing cytochrome c.
CC {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:21247899, ECO:0000269|PubMed:9748275}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:21247899};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:21247899};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21247899};
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 -!- SIMILARITY: In the N-terminal section; belongs to the FAD-binding
CC oxidoreductase type 6 family. {ECO:0000305}.
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DR EMBL; X97452; CAA66094.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74474.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14998.2; -; Genomic_DNA.
DR PIR; C64890; C64890.
DR RefSeq; NP_415910.1; NC_000913.3.
DR RefSeq; WP_000206388.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76081; -.
DR SMR; P76081; -.
DR BioGRID; 4260178; 205.
DR ComplexPortal; CPX-2844; paaABCE phenylacetyl-CoA monooxygenase complex.
DR IntAct; P76081; 2.
DR STRING; 511145.b1392; -.
DR PaxDb; P76081; -.
DR PRIDE; P76081; -.
DR EnsemblBacteria; AAC74474; AAC74474; b1392.
DR EnsemblBacteria; BAA14998; BAA14998; BAA14998.
DR GeneID; 945962; -.
DR KEGG; ecj:JW1387; -.
DR KEGG; eco:b1392; -.
DR PATRIC; fig|1411691.4.peg.879; -.
DR EchoBASE; EB3502; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_1_6; -.
DR InParanoid; P76081; -.
DR OMA; FLCGPFE; -.
DR PhylomeDB; P76081; -.
DR BioCyc; EcoCyc:G6713-MON; -.
DR BioCyc; MetaCyc:G6713-MON; -.
DR UniPathway; UPA00930; -.
DR PRO; PR:P76081; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IC:ComplexPortal.
DR GO; GO:0062077; C:phenylacetyl-CoA 1,2-epoxidase complex; IPI:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0010124; P:phenylacetate catabolic process; IDA:ComplexPortal.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011884; PA_CoA_Oase5.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR02160; PA_CoA_Oxy5; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..356
FT /note="1,2-phenylacetyl-CoA epoxidase, subunit E"
FT /id="PRO_0000058163"
FT DOMAIN 2..106
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 262..354
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT REGION 112..228
FT /note="Oxidoreductase"
FT /evidence="ECO:0000255"
FT BINDING 299
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 304
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 307
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 337
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT VARIANT 14
FT /note="S -> P (in strain: W)"
FT VARIANT 169
FT /note="P -> S (in strain: W)"
FT VARIANT 224..227
FT /note="DAET -> ETEA (in strain: W)"
SQ SEQUENCE 356 AA; 39320 MW; D719C1CA81DA5FFA CRC64;
MTTFHSLTVA KVESETRDAV TITFAVPQPL QEAYRFRPGQ HLTLKASFDG EELRRCYSIC
RSYLPGEISV AVKAIEGGRF SRYAREHIRQ GMTLEVMVPQ GHFGYQPQAE RQGRYLAIAA
GSGITPMLAI IATTLQTEPE SQFTLIYGNR TSQSMMFRQA LADLKDKYPQ RLQLLCIFSQ
ETLDSDLLHG RIDGEKLQSL GASLINFRLY DEAFICGPAA MMDDAETALK ALGMPDKTIH
LERFNTPGTR VKRSVNVQSD GQKVTVRQDG RDREIVLNAD DESILDAALR QGADLPYACK
GGVCATCKCK VLRGKVAMET NYSLEPDELA AGYVLSCQAL PLTSDVVVDF DAKGMA
