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   27-MAR-2024, entry version 130.
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; Pseudomonadota; 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};
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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; 511145-b1391; -.
DR   EnsemblBacteria; AAC74473; AAC74473; b1391.
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   OrthoDB; 3684942at2; -.
DR   PhylomeDB; P76080; -.
DR   BioCyc; EcoCyc:G6712-MONOMER; -.
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; Fe-S cluster assembly (FSCA); 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR002744; MIP18-like.
DR   InterPro; IPR011883; PaaD-like.
DR   NCBIfam; TIGR02159; PA_CoA_Oxy4; 1.
DR   PANTHER; PTHR42831:SF3; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT D-RELATED; 1.
DR   PANTHER; PTHR42831; FE-S PROTEIN MATURATION AUXILIARY FACTOR YITW; 1.
DR   Pfam; PF01883; FeS_assembly_P; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 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
//