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Protein

1,2-epoxyphenylacetyl-CoA isomerase

Gene

paaG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

  • enoyl-CoA hydratase activity Source: GO_Central
  • identical protein binding Source: EcoCyc
  • isomerase activity Source: UniProtKB

GO - Biological processi

  • fatty acid beta-oxidation Source: GO_Central
  • phenylacetate catabolic process Source: EcoCyc

Keywordsi

Molecular functionIsomerase, Lyase

Enzyme and pathway databases

BioCyciEcoCyc: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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13741 paaG

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001093311 – 2621,2-epoxyphenylacetyl-CoA isomeraseAdd BLAST262

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 interactors
IntActiP77467, 9 interactors
STRINGi316385.ECDH10B_1519

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi13 – 18Combined sources6
Turni21 – 24Combined sources4
Helixi29 – 44Combined sources16
Beta strandi50 – 58Combined sources9
Helixi80 – 86Combined sources7
Helixi88 – 97Combined sources10
Beta strandi102 – 106Combined sources5
Helixi113 – 119Combined sources7
Beta strandi121 – 127Combined sources7
Beta strandi131 – 133Combined sources3
Helixi136 – 138Combined sources3
Turni144 – 146Combined sources3
Helixi147 – 154Combined sources8
Helixi157 – 166Combined sources10
Helixi172 – 177Combined sources6
Beta strandi180 – 185Combined sources6
Helixi187 – 189Combined sources3
Helixi190 – 201Combined sources12
Helixi206 – 219Combined sources14
Helixi224 – 238Combined sources15
Helixi242 – 252Combined sources11

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108UKI Bacteria
COG1024 LUCA
HOGENOMiHOG000027949
InParanoidiP77467
KOiK15866
OMAiNSFTRAM
PhylomeDBiP77467

Family and domain databases

Gene3Di1.10.12.10, 1 hit
InterProiView protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR001753 Enoyl-CoA_hydra/iso
IPR014748 enoyl-CoA_hydra_C
IPR011968 PaaB1
PfamiView protein in Pfam
PF00378 ECH_1, 1 hit
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)DescriptionActionsGraphical viewLength
Natural varianti121G → C in strain: W. 1

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
PATRICifig|1411691.4.peg.877

Similar proteinsi

Entry informationi

Entry nameiPAAG_ECOLI
AccessioniPrimary (citable) accession number: P77467
Secondary accession number(s): O53015
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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