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Entry version 160 (07 Oct 2020)
Sequence version 1 (01 Feb 1997)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi299Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi304Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi307Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi337Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • phenylacetate catabolic process Source: UniProtKB

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6713-MONOMER
MetaCyc:G6713-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00930

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:paaE
Synonyms:ydbR
Ordered Locus Names:b1392, JW1387
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000581631 – 3561,2-phenylacetyl-CoA epoxidase, subunit EAdd BLAST356

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P76081

PRoteomics IDEntifications database

More...
PRIDEi
P76081

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260178, 205 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2844, paaABCE phenylacetyl-CoA monooxygenase complex

Protein interaction database and analysis system

More...
IntActi
P76081, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1392

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 106FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST105
Domaini262 – 3542Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST93

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni112 – 228OxidoreductaseSequence analysisAdd BLAST117

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the FAD-binding oxidoreductase type 6 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1018, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003827_14_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P76081

KEGG Orthology (KO)

More...
KOi
K02613

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P76081

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00207, fer2, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.30, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR011884, PA_CoA_Oase5
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00371, FPNCR

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02160, PA_CoA_Oxy5, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD719C1CA81DA5FFA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti14S → P in strain: W. 1
Natural varianti169P → S in strain: W. 1
Natural varianti224 – 227DAET → ETEA in strain: W. 4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X97452 Genomic DNA Translation: CAA66094.1
U00096 Genomic DNA Translation: AAC74474.1
AP009048 Genomic DNA Translation: BAA14998.2

Protein sequence database of the Protein Information Resource

More...
PIRi
C64890

NCBI Reference Sequences

More...
RefSeqi
NP_415910.1, NC_000913.3
WP_000206388.1, NZ_SSZK01000012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74474; AAC74474; b1392
BAA14998; BAA14998; BAA14998

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945962

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1387
eco:b1392

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.879

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_SSZK01000012.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi4260178, 205 interactors
ComplexPortaliCPX-2844, paaABCE phenylacetyl-CoA monooxygenase complex
IntActiP76081, 2 interactors
STRINGi511145.b1392

Proteomic databases

PaxDbiP76081
PRIDEiP76081

Genome annotation databases

EnsemblBacteriaiAAC74474; AAC74474; b1392
BAA14998; BAA14998; BAA14998
GeneIDi945962
KEGGiecj:JW1387
eco:b1392
PATRICifig|1411691.4.peg.879

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB3502

Phylogenomic databases

eggNOGiCOG1018, Bacteria
HOGENOMiCLU_003827_14_1_6
InParanoidiP76081
KOiK02613
PhylomeDBiP76081

Enzyme and pathway databases

UniPathwayiUPA00930
BioCyciEcoCyc:G6713-MONOMER
MetaCyc:G6713-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P76081

Family and domain databases

CDDicd00207, fer2, 1 hit
Gene3Di3.10.20.30, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR036010, 2Fe-2S_ferredoxin-like_sf
IPR001041, 2Fe-2S_ferredoxin-type
IPR006058, 2Fe2S_fd_BS
IPR012675, Beta-grasp_dom_sf
IPR008333, Cbr1-like_FAD-bd_dom
IPR017927, FAD-bd_FR_type
IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR039261, FNR_nucleotide-bd
IPR001433, OxRdtase_FAD/NAD-bd
IPR011884, PA_CoA_Oase5
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00970, FAD_binding_6, 1 hit
PF00111, Fer2, 1 hit
PF00175, NAD_binding_1, 1 hit
PRINTSiPR00371, FPNCR
SUPFAMiSSF52343, SSF52343, 1 hit
SSF54292, SSF54292, 1 hit
SSF63380, SSF63380, 1 hit
TIGRFAMsiTIGR02160, PA_CoA_Oxy5, 1 hit
PROSITEiView protein in PROSITE
PS00197, 2FE2S_FER_1, 1 hit
PS51085, 2FE2S_FER_2, 1 hit
PS51384, FAD_FR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAAE_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P76081
Secondary accession number(s): O53013, P77233
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: February 1, 1997
Last modified: October 7, 2020
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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
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