PAAC_ECOLI
ID PAAC_ECOLI Reviewed; 248 AA.
AC P76079; O53011; Q2MBD1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=1,2-phenylacetyl-CoA epoxidase, subunit C;
DE AltName: Full=1,2-phenylacetyl-CoA epoxidase, structural subunit beta;
DE AltName: Full=1,2-phenylacetyl-CoA monooxygenase, subunit C;
GN Name=paaC; Synonyms=ydbP; OrderedLocusNames=b1390, JW1385;
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 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 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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-248, AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "The 2 a crystal structure of protein paac from e. coli.";
RL Submitted (JUL-2011) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-248 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, 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 C may be essential
CC for structural integrity of the alpha subunit.
CC {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Forms a stable heterotetramer (dimer of heterodimers) with
CC PaaA and a stable heterodimer with PaaB. {ECO:0000269|PubMed:20823522,
CC ECO:0000269|PubMed:21247899, ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC P76079; P0AEF4: dpiA; NbExp=4; IntAct=EBI-1131666, EBI-1119284;
CC P76079; P76077: paaA; NbExp=6; IntAct=EBI-1131666, EBI-1119536;
CC P76079; P76078: paaB; NbExp=2; IntAct=EBI-1131666, EBI-1123811;
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 ---------------------------------------------------------------------------
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; CAA66092.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74472.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76425.1; -; Genomic_DNA.
DR PIR; A64890; A64890.
DR RefSeq; NP_415908.1; NC_000913.3.
DR RefSeq; WP_001072837.1; NZ_STEB01000005.1.
DR PDB; 1OTK; X-ray; 2.00 A; A/B=2-248.
DR PDB; 3PVR; X-ray; 2.10 A; B/C=2-248.
DR PDB; 3PVT; X-ray; 2.03 A; B/C=2-248.
DR PDB; 3PVY; X-ray; 2.15 A; B/C=2-248.
DR PDB; 3PW1; X-ray; 2.25 A; B/C=2-248.
DR PDB; 3PW8; X-ray; 2.97 A; A/B=2-248.
DR PDB; 3PWQ; X-ray; 2.65 A; A/B/E/G/I/J/K/R=2-248.
DR PDB; 4II4; X-ray; 2.80 A; B/C=2-248.
DR PDBsum; 1OTK; -.
DR PDBsum; 3PVR; -.
DR PDBsum; 3PVT; -.
DR PDBsum; 3PVY; -.
DR PDBsum; 3PW1; -.
DR PDBsum; 3PW8; -.
DR PDBsum; 3PWQ; -.
DR PDBsum; 4II4; -.
DR AlphaFoldDB; P76079; -.
DR SMR; P76079; -.
DR BioGRID; 4260175; 102.
DR BioGRID; 850320; 5.
DR ComplexPortal; CPX-2844; paaABCE phenylacetyl-CoA monooxygenase complex.
DR IntAct; P76079; 9.
DR STRING; 511145.b1390; -.
DR PaxDb; P76079; -.
DR PRIDE; P76079; -.
DR EnsemblBacteria; AAC74472; AAC74472; b1390.
DR EnsemblBacteria; BAE76425; BAE76425; BAE76425.
DR GeneID; 66674753; -.
DR GeneID; 945956; -.
DR KEGG; ecj:JW1385; -.
DR KEGG; eco:b1390; -.
DR PATRIC; fig|1411691.4.peg.881; -.
DR EchoBASE; EB3500; -.
DR eggNOG; COG3396; Bacteria.
DR HOGENOM; CLU_070585_0_0_6; -.
DR InParanoid; P76079; -.
DR OMA; NGDFAHT; -.
DR PhylomeDB; P76079; -.
DR BioCyc; EcoCyc:G6711-MON; -.
DR BioCyc; MetaCyc:G6711-MON; -.
DR BRENDA; 1.14.13.149; 2026.
DR UniPathway; UPA00930; -.
DR EvolutionaryTrace; P76079; -.
DR PRO; PR:P76079; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR007814; PaaA_PaaC.
DR InterPro; IPR011882; PaaC.
DR Pfam; PF05138; PaaA_PaaC; 1.
DR PIRSF; PIRSF037834; PA_CoA_Oase3; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR02158; PA_CoA_Oxy3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..248
FT /note="1,2-phenylacetyl-CoA epoxidase, subunit C"
FT /id="PRO_0000058161"
FT BINDING 76..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 160
FT /note="N -> D (in strain: W)"
FT HELIX 2..23
FT /evidence="ECO:0007829|PDB:1OTK"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:1OTK"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 32..60
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 90..111
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 117..145
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1OTK"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:1OTK"
SQ SEQUENCE 248 AA; 27877 MW; 024AD161DF8E4380 CRC64;
MNQLTAYTLR LGDNCLVLSQ RLGEWCGHAP ELEIDLALAN IGLDLLGQAR NFLSYAAELA
GEGDEDTLAF TRDERQFSNL LLVEQPNGNF ADTIARQYFI DAWHVALFTR LMESRDPQLA
AISAKAIKEA RYHLRFSRGW LERLGNGTDV SGQKMQQAIN KLWRFTAELF DADEIDIALS
EEGIAVDPRT LRAAWEAEVF AGINEATLNV PQEQAYRTGG KKGLHTEHLG PMLAEMQYLQ
RVLPGQQW
