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Protein

1,2-phenylacetyl-CoA epoxidase, subunit E

Gene

paaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Cofactori

Protein has several cofactor binding sites:

Pathwayi: phenylacetate degradation

This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi299 – 2991Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi304 – 3041Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi307 – 3071Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi337 – 3371Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: EcoCyc
  • electron carrier activity Source: InterPro
  • flavin adenine dinucleotide binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  • phenylacetate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciEcoCyc:G6713-MONOMER.
ECOL316407:JW1387-MONOMER.
MetaCyc:G6713-MONOMER.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
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 namesi
Name:paaE
Synonyms:ydbR
Ordered Locus Names:b1392, JW1387
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13739. paaE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3563561,2-phenylacetyl-CoA epoxidase, subunit EPRO_0000058163Add
BLAST

Proteomic databases

PaxDbiP76081.

Expressioni

Inductioni

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.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4260178. 205 interactions.
IntActiP76081. 1 interaction.
STRINGi511145.b1392.

Structurei

3D structure databases

ProteinModelPortaliP76081.
SMRiP76081. Positions 4-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 106105FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST
Domaini262 – 354932Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 228117OxidoreductaseSequence analysisAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FAD-binding oxidoreductase type 6 family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CJJ. Bacteria.
COG1018. LUCA.
HOGENOMiHOG000141049.
InParanoidiP76081.
KOiK02613.
OMAiYSLEPWE.
OrthoDBiEOG6XWV33.
PhylomeDBiP76081.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
TIGRFAMsiTIGR02160. PA_CoA_Oxy5. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTFHSLTVA KVESETRDAV TITFAVPQPL QEAYRFRPGQ HLTLKASFDG
60 70 80 90 100
EELRRCYSIC RSYLPGEISV AVKAIEGGRF SRYAREHIRQ GMTLEVMVPQ
110 120 130 140 150
GHFGYQPQAE RQGRYLAIAA GSGITPMLAI IATTLQTEPE SQFTLIYGNR
160 170 180 190 200
TSQSMMFRQA LADLKDKYPQ RLQLLCIFSQ ETLDSDLLHG RIDGEKLQSL
210 220 230 240 250
GASLINFRLY DEAFICGPAA MMDDAETALK ALGMPDKTIH LERFNTPGTR
260 270 280 290 300
VKRSVNVQSD GQKVTVRQDG RDREIVLNAD DESILDAALR QGADLPYACK
310 320 330 340 350
GGVCATCKCK VLRGKVAMET NYSLEPDELA AGYVLSCQAL PLTSDVVVDF

DAKGMA
Length:356
Mass (Da):39,320
Last modified:February 1, 1997 - v1
Checksum:iD719C1CA81DA5FFA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141S → P in strain: W.
Natural varianti169 – 1691P → S in strain: W.
Natural varianti224 – 2274DAET → ETEA in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66094.1.
U00096 Genomic DNA. Translation: AAC74474.1.
AP009048 Genomic DNA. Translation: BAA14998.2.
PIRiC64890.
RefSeqiNP_415910.1. NC_000913.3.
WP_000206388.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74474; AAC74474; b1392.
BAA14998; BAA14998; BAA14998.
GeneIDi945962.
KEGGiecj:JW1387.
eco:b1392.
PATRICi32118070. VBIEscCol129921_1455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66094.1.
U00096 Genomic DNA. Translation: AAC74474.1.
AP009048 Genomic DNA. Translation: BAA14998.2.
PIRiC64890.
RefSeqiNP_415910.1. NC_000913.3.
WP_000206388.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP76081.
SMRiP76081. Positions 4-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260178. 205 interactions.
IntActiP76081. 1 interaction.
STRINGi511145.b1392.

Proteomic databases

PaxDbiP76081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74474; AAC74474; b1392.
BAA14998; BAA14998; BAA14998.
GeneIDi945962.
KEGGiecj:JW1387.
eco:b1392.
PATRICi32118070. VBIEscCol129921_1455.

Organism-specific databases

EchoBASEiEB3502.
EcoGeneiEG13739. paaE.

Phylogenomic databases

eggNOGiENOG4105CJJ. Bacteria.
COG1018. LUCA.
HOGENOMiHOG000141049.
InParanoidiP76081.
KOiK02613.
OMAiYSLEPWE.
OrthoDBiEOG6XWV33.
PhylomeDBiP76081.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6713-MONOMER.
ECOL316407:JW1387-MONOMER.
MetaCyc:G6713-MONOMER.

Miscellaneous databases

PROiP76081.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
TIGRFAMsiTIGR02160. PA_CoA_Oxy5. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. 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.

Entry informationi

Entry nameiPAAE_ECOLI
AccessioniPrimary (citable) accession number: P76081
Secondary accession number(s): O53013, P77233
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.