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Protein

1,2-phenylacetyl-CoA epoxidase, subunit A

Gene

paaA

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 A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.4 Publications

Catalytic activityi

Phenylacetyl-CoA + NADPH + O2 = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O.1 Publication

Cofactori

Fe cationCurated

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
Binding sitei33 – 331Substrate1 Publication
Binding sitei37 – 371Substrate1 Publication
Binding sitei132 – 1321Substrate1 Publication
Binding sitei193 – 1931Substrate1 Publication
Binding sitei214 – 2141Substrate1 Publication
Binding sitei218 – 2181Substrate1 Publication

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:G6709-MONOMER.
ECOL316407:JW1383-MONOMER.
MetaCyc:G6709-MONOMER.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-phenylacetyl-CoA epoxidase, subunit A (EC:1.14.13.149)
Alternative name(s):
1,2-phenylacetyl-CoA epoxidase, catalytic subunit alpha
1,2-phenylacetyl-CoA monooxygenase, subunit A
Gene namesi
Name:paaA
Synonyms:ydbO
Ordered Locus Names:b1388, JW1383
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13736. paaA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3093091,2-phenylacetyl-CoA epoxidase, subunit APRO_0000058159Add
BLAST

Proteomic databases

PaxDbiP76077.
PRIDEiP76077.

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

Subunit structurei

Forms a stable heterotetramer (dimer of heterodimers) with PaaC.2 Publications

Protein-protein interaction databases

BioGridi4261392. 123 interactions.
IntActiP76077. 1 interaction.
STRINGi511145.b1388.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1211Combined sources
Helixi25 – 4420Combined sources
Helixi46 – 505Combined sources
Helixi51 – 555Combined sources
Helixi59 – 8426Combined sources
Turni85 – 873Combined sources
Helixi90 – 989Combined sources
Helixi106 – 1094Combined sources
Helixi115 – 13420Combined sources
Turni135 – 1384Combined sources
Helixi142 – 17029Combined sources
Helixi174 – 19320Combined sources
Helixi199 – 2013Combined sources
Helixi205 – 2106Combined sources
Helixi218 – 23518Combined sources
Beta strandi246 – 2483Combined sources
Turni249 – 2524Combined sources
Beta strandi253 – 2553Combined sources
Helixi261 – 2688Combined sources
Turni269 – 2713Combined sources
Beta strandi272 – 2743Combined sources
Helixi275 – 28814Combined sources
Helixi290 – 30112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PVRX-ray2.10A2-309[»]
3PVTX-ray2.03A2-309[»]
3PVYX-ray2.15A2-309[»]
3PW1X-ray2.25A2-309[»]
3PW8X-ray2.97C/D2-309[»]
3PWQX-ray2.65C/D/F/H2-309[»]
4II4X-ray2.80A2-309[»]
ProteinModelPortaliP76077.
SMRiP76077. Positions 2-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76077.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1064Substrate binding1 Publication
Regioni202 – 2043Substrate binding1 Publication

Phylogenomic databases

eggNOGiENOG4105CRS. Bacteria.
COG3396. LUCA.
HOGENOMiHOG000249745.
InParanoidiP76077.
KOiK02609.
OMAiQPEANWI.
OrthoDBiEOG6DJXXX.
PhylomeDBiP76077.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR011881. PaaA.
IPR007814. PaaA_PaaC.
[Graphical view]
PfamiPF05138. PaaA_PaaC. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR02156. PA_CoA_Oxy1. 1 hit.

Sequencei

Sequence statusi: Complete.

P76077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQEERFEQR IAQETAIEPQ DWMPDAYRKT LIRQIGQHAH SEIVGMLPEG
60 70 80 90 100
NWITRAPTLR RKAILLAKVQ DEAGHGLYLY SAAETLGCAR EDIYQKMLDG
110 120 130 140 150
RMKYSSIFNY PTLSWADIGV IGWLVDGAAI VNQVALCRTS YGPYARAMVK
160 170 180 190 200
ICKEESFHQR QGFEACMALA QGSEAQKQML QDAINRFWWP ALMMFGPNDD
210 220 230 240 250
NSPNSARSLT WKIKRFTNDE LRQRFVDNTV PQVEMLGMTV PDPDLHFDTE
260 270 280 290 300
SGHYRFGEID WQEFNEVING RGICNQERLD AKRKAWEEGT WVREAALAHA

QKQHARKVA
Length:309
Mass (Da):35,499
Last modified:February 1, 1997 - v1
Checksum:i83AEC6D7AC084073
GO

Sequence cautioni

The sequence CAA66090.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti210 – 2101T → A in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66090.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74470.1.
AP009048 Genomic DNA. Translation: BAE76423.1.
PIRiG64889.
RefSeqiNP_415906.1. NC_000913.3.
WP_000191077.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74470; AAC74470; b1388.
BAE76423; BAE76423; BAE76423.
GeneIDi945833.
KEGGiecj:JW1383.
eco:b1388.
PATRICi32118062. VBIEscCol129921_1451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66090.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74470.1.
AP009048 Genomic DNA. Translation: BAE76423.1.
PIRiG64889.
RefSeqiNP_415906.1. NC_000913.3.
WP_000191077.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PVRX-ray2.10A2-309[»]
3PVTX-ray2.03A2-309[»]
3PVYX-ray2.15A2-309[»]
3PW1X-ray2.25A2-309[»]
3PW8X-ray2.97C/D2-309[»]
3PWQX-ray2.65C/D/F/H2-309[»]
4II4X-ray2.80A2-309[»]
ProteinModelPortaliP76077.
SMRiP76077. Positions 2-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261392. 123 interactions.
IntActiP76077. 1 interaction.
STRINGi511145.b1388.

Proteomic databases

PaxDbiP76077.
PRIDEiP76077.

Protocols and materials databases

DNASUi945833.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74470; AAC74470; b1388.
BAE76423; BAE76423; BAE76423.
GeneIDi945833.
KEGGiecj:JW1383.
eco:b1388.
PATRICi32118062. VBIEscCol129921_1451.

Organism-specific databases

EchoBASEiEB3499.
EcoGeneiEG13736. paaA.

Phylogenomic databases

eggNOGiENOG4105CRS. Bacteria.
COG3396. LUCA.
HOGENOMiHOG000249745.
InParanoidiP76077.
KOiK02609.
OMAiQPEANWI.
OrthoDBiEOG6DJXXX.
PhylomeDBiP76077.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6709-MONOMER.
ECOL316407:JW1383-MONOMER.
MetaCyc:G6709-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP76077.
PROiP76077.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR011881. PaaA.
IPR007814. PaaA_PaaC.
[Graphical view]
PfamiPF05138. PaaA_PaaC. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR02156. PA_CoA_Oxy1. 1 hit.
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 / MG1655 / ATCC 47076.
  3. "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.
  4. "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: TRANSCRIPTIONAL REGULATION.
  5. "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 MONOOXYGENASE.
  6. "Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex."
    Grishin A.M., Ajamian E., Zhang L., Cygler M.
    Acta Crystallogr. F 66:1045-1049(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. Cited for: FUNCTION AS AN EPOXYDASE, CATALYTIC ACTIVITY.
  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: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-309 IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION AS A MONOOXYGENASE, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPAAA_ECOLI
AccessioniPrimary (citable) accession number: P76077
Secondary accession number(s): O53010, Q2MBD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 110 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

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.