PAAD_ECOLI
ID PAAD_ECOLI Reviewed; 165 AA.
AC P76080; O53012; Q2MBD0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative 1,2-phenylacetyl-CoA epoxidase, subunit D;
DE AltName: Full=1,2-phenylacetyl-CoA monooxygenase, subunit D;
GN Name=paaD; Synonyms=ydbQ; OrderedLocusNames=b1391, JW5217;
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 POSSIBLE MONOOXYGENASE COMPONENT.
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=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: Possible component of 1,2-phenylacetyl-CoA epoxidase
CC multicomponent enzyme system which catalyzes the reduction of
CC phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The
CC subunit D may have a function related to the maturation of the
CC monooxygenase complex, rather than direct involvement in catalysis.
CC PaaD could assist either in maturation of PaaE or PaaA.
CC {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:9748275}.
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21247899}.
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 -!- MISCELLANEOUS: PaaD component is not essential for the reaction in
CC vitro.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66093.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97452; CAA66093.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74473.4; -; Genomic_DNA.
DR EMBL; AP009048; BAE76426.1; -; Genomic_DNA.
DR PIR; B64890; B64890.
DR RefSeq; NP_415909.4; NC_000913.3.
DR RefSeq; WP_001189201.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76080; -.
DR SMR; P76080; -.
DR BioGRID; 4262886; 119.
DR BioGRID; 850322; 4.
DR IntAct; P76080; 4.
DR STRING; 511145.b1391; -.
DR PaxDb; P76080; -.
DR PRIDE; P76080; -.
DR EnsemblBacteria; AAC74473; AAC74473; b1391.
DR EnsemblBacteria; BAE76426; BAE76426; BAE76426.
DR GeneID; 945959; -.
DR KEGG; ecj:JW5217; -.
DR KEGG; eco:b1391; -.
DR PATRIC; fig|1411691.4.peg.880; -.
DR EchoBASE; EB3501; -.
DR eggNOG; COG2151; Bacteria.
DR HOGENOM; CLU_082133_0_0_6; -.
DR InParanoid; P76080; -.
DR OMA; EPFDHFK; -.
DR PhylomeDB; P76080; -.
DR BioCyc; EcoCyc:G6712-MON; -.
DR UniPathway; UPA00930; -.
DR PRO; PR:P76080; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR002744; MIP18-like.
DR InterPro; IPR011883; PA_CoA_Oase4.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
DR TIGRFAMs; TIGR02159; PA_CoA_Oxy4; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..165
FT /note="Putative 1,2-phenylacetyl-CoA epoxidase, subunit D"
FT /id="PRO_0000058162"
FT VARIANT 47
FT /note="G -> E (in strain: W)"
FT VARIANT 76
FT /note="N -> H (in strain: W)"
FT VARIANT 106
FT /note="E -> Q (in strain: W)"
SQ SEQUENCE 165 AA; 18324 MW; 67AE8F04C8F0045B CRC64;
MQRLATIAPP QVHEIWALLS QIPDPEIPVL TITDLGMVRN VTQMGEGWVI GFTPTYSGCP
ATEHLIGAIR EAMTTNGFTP VQVVLQLDPA WTTDWMTPDA RERLREYGIS PPAGHSCHAH
LPPEVRCPRC ASVHTTLISE FGSTACKALY RCDSCREPFD YFKCI
