PAAB_ECOLI
ID PAAB_ECOLI Reviewed; 95 AA.
AC P76078; Q2MBD2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=1,2-phenylacetyl-CoA epoxidase, subunit B;
DE AltName: Full=1,2-phenylacetyl-CoA monooxygenase, subunit B;
GN Name=paaB; Synonyms=ynbF; OrderedLocusNames=b1389, JW1384;
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 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 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 [7]
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: 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 B may play a
CC regulatory role or be directly involved in electron transport.
CC {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Homotrimer. Forms a stable heterodimer with PaaC. Probably
CC forms an oligomer with PaaAC. {ECO:0000269|PubMed:21247899}.
CC -!- INTERACTION:
CC P76078; P76079: paaC; NbExp=2; IntAct=EBI-1123811, 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}.
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DR EMBL; X97452; CAA66091.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74471.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76424.1; -; Genomic_DNA.
DR PIR; H64889; H64889.
DR RefSeq; NP_415907.1; NC_000913.3.
DR RefSeq; WP_000073393.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P76078; -.
DR SMR; P76078; -.
DR BioGRID; 4261630; 132.
DR ComplexPortal; CPX-2844; paaABCE phenylacetyl-CoA monooxygenase complex.
DR IntAct; P76078; 14.
DR STRING; 511145.b1389; -.
DR PaxDb; P76078; -.
DR PRIDE; P76078; -.
DR EnsemblBacteria; AAC74471; AAC74471; b1389.
DR EnsemblBacteria; BAE76424; BAE76424; BAE76424.
DR GeneID; 66674754; -.
DR GeneID; 947595; -.
DR KEGG; ecj:JW1384; -.
DR KEGG; eco:b1389; -.
DR PATRIC; fig|1411691.4.peg.882; -.
DR EchoBASE; EB4046; -.
DR eggNOG; COG3460; Bacteria.
DR HOGENOM; CLU_141459_2_0_6; -.
DR InParanoid; P76078; -.
DR OMA; PYRHPTF; -.
DR PhylomeDB; P76078; -.
DR BioCyc; EcoCyc:G6710-MON; -.
DR BioCyc; MetaCyc:G6710-MON; -.
DR UniPathway; UPA00930; -.
DR PRO; PR:P76078; -.
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:0010124; P:phenylacetate catabolic process; IDA:ComplexPortal.
DR Gene3D; 3.10.20.520; -; 1.
DR InterPro; IPR009359; PaaB.
DR InterPro; IPR038693; PaaB_sf.
DR Pfam; PF06243; PaaB; 1.
DR PIRSF; PIRSF030200; PaaB; 1.
DR TIGRFAMs; TIGR02157; PA_CoA_Oxy2; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..95
FT /note="1,2-phenylacetyl-CoA epoxidase, subunit B"
FT /id="PRO_0000058160"
SQ SEQUENCE 95 AA; 10942 MW; D2866DB428CF90AF CRC64;
MSNVYWPLYE VFVRGKQGLS HRHVGSLHAA DERMALENAR DAYTRRSEGC SIWVVKASEI
VASQPEERGE FFDPAESKVY RHPTFYTIPD GIEHM
