P76081 (PAAE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,2-phenylacetyl-CoA epoxidase, subunit E
EC=1.-.-.-

Alternative name(s):
1,2-phenylacetyl-CoA epoxidase, reductase subunit
1,2-phenylacetyl-CoA monooxygenase, subunit E

Gene names

Name:	paaE
Synonyms:	ydbR
Ordered Locus Names:	b1392, JW1387

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a reductase with a preference for NADPH and FAD, capable of reducing cytochrome c. Ref.1 Ref.6 Ref.7 Ref.8
Cofactor	Binds 1 2Fe-2S cluster. Ref.8 FAD. Ref.8
Pathway	Aromatic compound metabolism; phenylacetate degradation.
Induction	Activated by cAMP receptor protein (CRP), integration host factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX from binding its target sequences. Inhibited by PaaX. Ref.1 Ref.5
Sequence similarities	In the N-terminal section; belongs to the FAD-binding oxidoreductase type 6 family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW phenylacetate catabolic process Inferred from mutant phenotype Ref.1. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from direct assay Ref.8. Source: EcoCyc electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from direct assay Ref.8. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	1,2-phenylacetyl-CoA epoxidase, subunit E		PRO_0000058163
Regions
	Domain	2 – 106	105	FAD-binding FR-type
	Domain	262 – 354	93	2Fe-2S ferredoxin-type
	Region	112 – 228	117	Oxidoreductase Potential
Sites
	Metal binding	299	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	304	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	307	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	337	1	Iron-sulfur (2Fe-2S) By similarity
Natural variations
	Natural variant	14	1	S → P in strain: W.
	Natural variant	169	1	P → S in strain: W.
	Natural variant	224 – 227	4	DAET → ETEA in strain: W.

Sequences

	Sequence		Length	Mass (Da)
	P76081 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: D719C1CA81DA5FFA	FASTA	356	39,320
	10 20 30 40 50 60 MTTFHSLTVA KVESETRDAV TITFAVPQPL QEAYRFRPGQ HLTLKASFDG EELRRCYSIC 70 80 90 100 110 120 RSYLPGEISV AVKAIEGGRF SRYAREHIRQ GMTLEVMVPQ GHFGYQPQAE RQGRYLAIAA 130 140 150 160 170 180 GSGITPMLAI IATTLQTEPE SQFTLIYGNR TSQSMMFRQA LADLKDKYPQ RLQLLCIFSQ 190 200 210 220 230 240 ETLDSDLLHG RIDGEKLQSL GASLINFRLY DEAFICGPAA MMDDAETALK ALGMPDKTIH 250 260 270 280 290 300 LERFNTPGTR VKRSVNVQSD GQKVTVRQDG RDREIVLNAD DESILDAALR QGADLPYACK 310 320 330 340 350 GGVCATCKCK VLRGKVAMET NYSLEPDELA AGYVLSCQAL PLTSDVVVDF DAKGMA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., Diaz E. J. Biol. Chem. 273:25974-25986(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM, INDUCTION. Strain: W / ATCC 11105 / DSM 1900.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli." Ferrandez A., Garcia J.L., Diaz E. J. Biol. Chem. 275:12214-12222(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[6]	"Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli." Fernandez C., Ferrandez A., Minambres B., Diaz E., Garcia J.L. Appl. Environ. Microbiol. 72:7422-7426(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A REDUCTASE.
[7]	"Bacterial phenylalanine and phenylacetate catabolic pathway revealed." Teufel R., Mascaraque V., Ismail W., Voss M., Perera J., Eisenreich W., Haehnel W., Fuchs G. Proc. Natl. Acad. Sci. U.S.A. 107:14390-14395(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A MONOOXYGENASE COMPONENT.
[8]	"Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex." Grishin A.M., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. J. Biol. Chem. 286:10735-10743(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A REDUCTASE, COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97452 Genomic DNA. Translation: CAA66094.1. U00096 Genomic DNA. Translation: AAC74474.1. AP009048 Genomic DNA. Translation: BAA14998.2.
PIR	C64890.
RefSeq	NP_415910.1. NC_000913.2. YP_489661.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76081.
SMR	P76081. Positions 4-350.
ModBase	Search...
Protein-protein interaction databases
IntAct	P76081. 1 interaction.
STRING	511145.b1392.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74474; AAC74474; b1392. BAA14998; BAA14998; BAA14998.
GeneID	12931184. 945962.
KEGG	ecj:Y75_p1369. eco:b1392.
PATRIC	32118070. VBIEscCol129921_1455.
Organism-specific databases
EchoBASE	EB3502.
EcoGene	EG13739. paaE.
Phylogenomic databases
eggNOG	COG1018.
HOGENOM	HOG000141049.
KO	K02613.
OMA	DHVFICG.
ProtClustDB	CLSK891747.
Enzyme and pathway databases
BioCyc	EcoCyc:G6713-MONOMER. ECOL316407:JW1387-MONOMER. MetaCyc:G6713-MONOMER.
UniPathway	UPA00930.
Gene expression databases
Genevestigator	P76081.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_dom. IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR011884. PA_CoA_Oase5. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00111. Fer2. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00410. PHEHYDRXLASE.
SUPFAM	SSF54292. Ferredoxin. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMs	TIGR02160. PA_CoA_Oxy5. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PAAE_ECOLI

Accession

Primary (citable) accession number: P76081
Secondary accession number(s): O53013, P77233

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program