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MetaCyc Polypeptide: ring 1,2-phenylacetyl-CoA epoxidase, reductase subunit

Gene: paaE Accession Numbers: G6713 (MetaCyc), b1392, ECK1389

Synonyms: ydbR

Species: Escherichia coli K-12 substr. MG1655

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

Summary:
PaaE has similarity to class IA-like reductases, members of the ferredoxin-NADP+ reductase (FNR) family of proteins [Ferrandez98]. PaaE carries a [2Fe-2S] cluster similar to that of spinach ferredoxin [Grishin11].

PaaE: "phenylacetic acid degradation" [Ferrandez98]

Locations: cytosol

Map Position: [1,454,454 -> 1,455,524]

Molecular Weight of Polypeptide: 39.32 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004657 , EchoBASE:EB3502 , EcoGene:EG13739 , EcoliWiki:b1392 , ModBase:P76081 , OU-Microarray:b1392 , PortEco:paaE , Protein Model Portal:P76081 , RefSeq:NP_415910 , RegulonDB:G6713 , SMR:P76081 , String:511145.b1392 , Swiss-Model:P76081 , UniProt:P76081

Relationship Links: InterPro:IN-FAMILY:IPR001041 , InterPro:IN-FAMILY:IPR001221 , InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR001709 , InterPro:IN-FAMILY:IPR006058 , InterPro:IN-FAMILY:IPR008333 , InterPro:IN-FAMILY:IPR011884 , InterPro:IN-FAMILY:IPR012675 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , Pfam:IN-FAMILY:PF00111 , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00970 , Prints:IN-FAMILY:PR00371 , Prints:IN-FAMILY:PR00410 , Prosite:IN-FAMILY:PS00197 , Prosite:IN-FAMILY:PS51085 , Prosite:IN-FAMILY:PS51384

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0010124 - phenylacetate catabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA01, Ferrandez98]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01]
Molecular Function: GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment [Grishin11]
GO:0051537 - 2 iron, 2 sulfur cluster binding Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01, Grishin11]
GO:0009055 - electron carrier activity Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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

Species: Escherichia coli K-12 substr. MG1655

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)

Summary:
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]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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

Synonyms: phenylacetyl-CoA monooxygenase

EC Number: 1.14.13.149

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 of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

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


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 2 -> 106
[UniProt09]
UniProt: FAD-binding FR-type;
Extrinsic-Sequence-Variant 14
[UniProt10a]
Alternate sequence: P; UniProt: (in strain: W);
Protein-Segment 112 -> 228
[UniProt10]
UniProt: Oxidoreductase; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: potential;
Extrinsic-Sequence-Variant 169
[UniProt10a]
Alternate sequence: S; UniProt: (in strain: W);
Extrinsic-Sequence-Variant 224 -> 227
[UniProt10a]
Alternate sequence: ETEA; UniProt: (in strain: W);
Conserved-Region 262 -> 354
[UniProt09]
UniProt: 2Fe-2S ferredoxin-type;
Metal-Binding-Site 299
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 304
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 307
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 337
[UniProt10]
UniProt: Iron-sulfur (2Fe-2S); Non-Experimental Qualifier: by similarity;

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


References

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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Nov 24, 2014, BIOCYC13A.