Escherichia coli K-12 substr. MG1655 Polypeptide: ring 1,2-phenylacetyl-CoA epoxidase, structural subunit

Gene: paaC Accession Numbers: G6711 (EcoCyc), b1390, ECK1387

Synonyms: ydbP

Regulation Summary Diagram: ?

Regulation summary diagram for paaC

Component of: ring 1,2-phenylacetyl-CoA epoxidase (summary available)

PaaC is the structural β subunit of the catalytic core of the enzyme [Grishin11].

PaaC: "phenylacetic acid degradation" [Ferrandez98]

Locations: cytosol

Map Position: [1,453,188 -> 1,453,934] (31.32 centisomes, 113°)
Length: 747 bp / 248 aa

Molecular Weight of Polypeptide: 27.877 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004653 , EchoBASE:EB3500 , EcoGene:EG13737 , EcoliWiki:b1390 , ModBase:P76079 , OU-Microarray:b1390 , PortEco:paaC , PR:PRO_000023477 , Pride:P76079 , Protein Model Portal:P76079 , RefSeq:NP_415908 , RegulonDB:G6711 , SMR:P76079 , String:511145.b1390 , UniProt:P76079

Relationship Links: InterPro:IN-FAMILY:IPR007814 , InterPro:IN-FAMILY:IPR009078 , InterPro:IN-FAMILY:IPR011882 , InterPro:IN-FAMILY:IPR012347 , PDB:Structure:1OTK , PDB:Structure:3PVR , PDB:Structure:3PVT , PDB:Structure:3PVY , PDB:Structure:3PW1 , PDB:Structure:3PW8 , PDB:Structure:3PWQ , PDB:Structure:4II4 , Pfam:IN-FAMILY:PF05138

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for paaC

GO Terms:

Biological Process: GO:0010124 - phenylacetate catabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, Ferrandez98]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Zhang07]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for paaC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Subunit of: ring 1,2-phenylacetyl-CoA epoxidase

Subunit composition of ring 1,2-phenylacetyl-CoA epoxidase = [PaaE][PaaA][PaaC][PaaB]
         ring 1,2-phenylacetyl-CoA epoxidase, reductase subunit = PaaE (summary available)
         ring 1,2-phenylacetyl-CoA epoxidase, monooxygenase subunit = PaaA (summary available)
         ring 1,2-phenylacetyl-CoA epoxidase, structural subunit = PaaC (summary available)
         ring 1,2-phenylacetyl-CoA epoxidase subunit = PaaB (summary available)

The ring 1,2-phenylacetyl-CoA epoxidase, comprised of the PaaA, PaaB, PaaC, and PaaE polypeptides, catalyzes the second step in the aerobic degradation of phenylacetate [Grishin11].

Stable subcomplexes composed of PaaABC, PaaAC and PaaBC can be purified, but only the combination of the PaaABC complex together with PaaE has full activity [Grishin11]. Crystal structures of the PaaAC subcomplex alone and together with a variety of ligands have been solved [Grishin10, Grishin11].

GO Terms:

Biological Process: GO:0010124 - phenylacetate catabolic process Inferred from experiment [Grishin11]
Molecular Function: GO:0016709 - oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Inferred from experiment [Grishin11]

Last-Curated ? 25-Jan-2011 by Keseler I , SRI International

Enzymatic reaction of: ring 1,2-phenylacetyl-CoA epoxidase

Synonyms: phenylacetyl-CoA monooxygenase

EC Number:

phenylacetyl-CoA + NADPH + oxygen + H+ <=> 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of phenylethylamine degradation , phenylacetate degradation I (aerobic)

Cofactors or Prosthetic Groups: a [2Fe-2S] iron-sulfur cluster [Grishin11], FAD [Grishin11]

Sequence Features

Protein sequence of ring 1,2-phenylacetyl-CoA epoxidase, structural subunit with features indicated

Feature Class Location Citations Comment
Protein-Segment 76 -> 79
UniProt: Substrate; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Extrinsic-Sequence-Variant 160
UniProt: In strain: W..
Protein-Segment 177 -> 179
UniProt: Substrate; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Ferrandez98: Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E (1998). "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." J Biol Chem 1998;273(40);25974-86. PMID: 9748275

Grishin10: Grishin AM, Ajamian E, Zhang L, Cygler M (2010). "Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex." Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 9);1045-9. PMID: 20823522

Grishin11: Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M (2011). "Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex." J Biol Chem 286(12);10735-43. PMID: 21247899

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Teufel10: Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G (2010). "Bacterial phenylalanine and phenylacetate catabolic pathway revealed." Proc Natl Acad Sci U S A 107(32):14390-5. PMID: 20660314

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-09 released on 2012-09-12 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Other References Related to Gene Regulation

Beisel12: Beisel CL, Updegrove TB, Janson BJ, Storz G (2012). "Multiple factors dictate target selection by Hfq-binding small RNAs." EMBO J 31(8);1961-74. PMID: 22388518

Ferrandez00: Ferrandez A, Garcia JL, Diaz E (2000). "Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli." J Biol Chem 275(16);12214-22. PMID: 10766858

Kim04b: Kim HS, Kang TS, Hyun JS, Kang HS (2004). "Regulation of penicillin G acylase gene expression in Escherichia coli by repressor PaaX and the cAMP-cAMP receptor protein complex." J Biol Chem 279(32);33253-62. PMID: 15159386

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Fri Oct 9, 2015, BIOCYC14B.