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Protein

1,2-epoxyphenylacetyl-CoA isomerase

Gene

paaG

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

Functioni

Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA).3 Publications

Catalytic activityi

2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA = 2-oxepin-2(3H)-ylideneacetyl-CoA.

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.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • isomerase activity Source: UniProtKB
  • lyase activity Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, Lyase

Enzyme and pathway databases

BioCyciEcoCyc:G6715-MONOMER.
ECOL316407:JW1389-MONOMER.
MetaCyc:G6715-MONOMER.
BRENDAi5.3.3.18. 2026.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-epoxyphenylacetyl-CoA isomerase (EC:5.3.3.18)
Gene namesi
Name:paaG
Synonyms:ydbT
Ordered Locus Names:b1394, JW1389
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13741. paaG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutants accumulate ring-1,2-dihydroxy-1,2-dihydrophenylacetyl lactone and are unable to use phenylacetate as a carbon source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2622621,2-epoxyphenylacetyl-CoA isomerasePRO_0000109331Add
BLAST

Proteomic databases

PaxDbiP77467.
PRIDEiP77467.

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

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260969. 375 interactions.
IntActiP77467. 9 interactions.
STRINGi511145.b1394.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi13 – 186Combined sources
Turni21 – 244Combined sources
Helixi29 – 4416Combined sources
Beta strandi50 – 589Combined sources
Helixi80 – 867Combined sources
Helixi88 – 9710Combined sources
Beta strandi102 – 1065Combined sources
Helixi113 – 1197Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi131 – 1333Combined sources
Helixi136 – 1383Combined sources
Turni144 – 1463Combined sources
Helixi147 – 1548Combined sources
Helixi157 – 16610Combined sources
Helixi172 – 1776Combined sources
Beta strandi180 – 1856Combined sources
Helixi187 – 1893Combined sources
Helixi190 – 20112Combined sources
Helixi206 – 21914Combined sources
Helixi224 – 23815Combined sources
Helixi242 – 25211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FZWX-ray2.55C/D1-262[»]
ProteinModelPortaliP77467.
SMRiP77467. Positions 4-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108UKI. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027949.
InParanoidiP77467.
KOiK15866.
OMAiNTAMHLE.
PhylomeDBiP77467.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR011968. PaaB1.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02280. PaaB1. 1 hit.

Sequencei

Sequence statusi: Complete.

P77467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMEFILSHVE KGVMTLTLNR PERLNSFNDE MHAQLAECLK QVERDDTIRC
60 70 80 90 100
LLLTGAGRGF CAGQDLNDRN VDPTGPAPDL GMSVERFYNP LVRRLAKLPK
110 120 130 140 150
PVICAVNGVA AGAGATLALG GDIVIAARSA KFVMAFSKLG LIPDCGGTWL
160 170 180 190 200
LPRVAGRARA MGLALLGNQL SAEQAHEWGM IWQVVDDETL ADTAQQLARH
210 220 230 240 250
LATQPTFGLG LIKQAINSAE TNTLDTQLDL ERDYQRLAGR SADYREGVSA
260
FLAKRSPQFT GK
Length:262
Mass (Da):28,405
Last modified:February 1, 1997 - v1
Checksum:iDD7B95B30D88660C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211G → C in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66096.1.
U00096 Genomic DNA. Translation: AAC74476.1.
AP009048 Genomic DNA. Translation: BAA15000.1.
PIRiE64890.
RefSeqiNP_415912.1. NC_000913.3.
WP_000969784.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74476; AAC74476; b1394.
BAA15000; BAA15000; BAA15000.
GeneIDi946263.
KEGGiecj:JW1389.
eco:b1394.
PATRICi32118074. VBIEscCol129921_1457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66096.1.
U00096 Genomic DNA. Translation: AAC74476.1.
AP009048 Genomic DNA. Translation: BAA15000.1.
PIRiE64890.
RefSeqiNP_415912.1. NC_000913.3.
WP_000969784.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FZWX-ray2.55C/D1-262[»]
ProteinModelPortaliP77467.
SMRiP77467. Positions 4-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260969. 375 interactions.
IntActiP77467. 9 interactions.
STRINGi511145.b1394.

Proteomic databases

PaxDbiP77467.
PRIDEiP77467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74476; AAC74476; b1394.
BAA15000; BAA15000; BAA15000.
GeneIDi946263.
KEGGiecj:JW1389.
eco:b1394.
PATRICi32118074. VBIEscCol129921_1457.

Organism-specific databases

EchoBASEiEB3504.
EcoGeneiEG13741. paaG.

Phylogenomic databases

eggNOGiENOG4108UKI. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027949.
InParanoidiP77467.
KOiK15866.
OMAiNTAMHLE.
PhylomeDBiP77467.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6715-MONOMER.
ECOL316407:JW1389-MONOMER.
MetaCyc:G6715-MONOMER.
BRENDAi5.3.3.18. 2026.

Miscellaneous databases

PROiP77467.

Family and domain databases

Gene3Di1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR011968. PaaB1.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02280. PaaB1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPAAG_ECOLI
AccessioniPrimary (citable) accession number: P77467
Secondary accession number(s): O53015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 119 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.