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Protein

1,2-phenylacetyl-CoA epoxidase, subunit C

Gene

paaC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 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 C may be essential for structural integrity of the alpha subunit.3 Publications

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 - Biological processi

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

Enzyme and pathway databases

BioCyciEcoCyc:G6711-MONOMER.
ECOL316407:JW1385-MONOMER.
MetaCyc:G6711-MONOMER.
BRENDAi1.14.13.149. 2026.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
1,2-phenylacetyl-CoA epoxidase, subunit C
Alternative name(s):
1,2-phenylacetyl-CoA epoxidase, structural subunit beta
1,2-phenylacetyl-CoA monooxygenase, subunit C
Gene namesi
Name:paaC
Synonyms:ydbP
Ordered Locus Names:b1390, JW1385
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13737. paaC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2482481,2-phenylacetyl-CoA epoxidase, subunit CPRO_0000058161Add
BLAST

Proteomic databases

PaxDbiP76079.

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 PaaA and a stable heterodimer with PaaB.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dpiAP0AEF44EBI-1131666,EBI-1119284

Protein-protein interaction databases

BioGridi4260175. 102 interactions.
IntActiP76079. 7 interactions.
STRINGi511145.b1390.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2322Combined sources
Turni24 – 285Combined sources
Beta strandi29 – 313Combined sources
Helixi32 – 6029Combined sources
Helixi65 – 706Combined sources
Helixi74 – 763Combined sources
Helixi81 – 844Combined sources
Helixi90 – 11122Combined sources
Helixi117 – 14529Combined sources
Helixi149 – 16214Combined sources
Helixi163 – 1653Combined sources
Helixi167 – 1704Combined sources
Helixi174 – 1818Combined sources
Helixi188 – 1914Combined sources
Helixi192 – 20514Combined sources
Helixi220 – 2223Combined sources
Helixi229 – 24214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTKX-ray2.00A/B2-248[»]
3PVRX-ray2.10B/C2-248[»]
3PVTX-ray2.03B/C2-248[»]
3PVYX-ray2.15B/C2-248[»]
3PW1X-ray2.25B/C2-248[»]
3PW8X-ray2.97A/B2-248[»]
3PWQX-ray2.65A/B/E/G/I/J/K/R2-248[»]
4II4X-ray2.80B/C2-248[»]
ProteinModelPortaliP76079.
SMRiP76079. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76079.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 794Substrate bindingBy similarity
Regioni177 – 1793Substrate bindingBy similarity

Phylogenomic databases

eggNOGiENOG4105D9S. Bacteria.
COG3396. LUCA.
HOGENOMiHOG000254959.
InParanoidiP76079.
KOiK02611.
OMAiAWCGHAP.
OrthoDBiEOG64BQ4K.
PhylomeDBiP76079.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR007814. PaaA_PaaC.
IPR011882. PaaC.
[Graphical view]
PfamiPF05138. PaaA_PaaC. 1 hit.
[Graphical view]
PIRSFiPIRSF037834. PA_CoA_Oase3. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR02158. PA_CoA_Oxy3. 1 hit.

Sequencei

Sequence statusi: Complete.

P76079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQLTAYTLR LGDNCLVLSQ RLGEWCGHAP ELEIDLALAN IGLDLLGQAR
60 70 80 90 100
NFLSYAAELA GEGDEDTLAF TRDERQFSNL LLVEQPNGNF ADTIARQYFI
110 120 130 140 150
DAWHVALFTR LMESRDPQLA AISAKAIKEA RYHLRFSRGW LERLGNGTDV
160 170 180 190 200
SGQKMQQAIN KLWRFTAELF DADEIDIALS EEGIAVDPRT LRAAWEAEVF
210 220 230 240
AGINEATLNV PQEQAYRTGG KKGLHTEHLG PMLAEMQYLQ RVLPGQQW
Length:248
Mass (Da):27,877
Last modified:February 1, 1997 - v1
Checksum:i024AD161DF8E4380
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti160 – 1601N → D in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66092.1.
U00096 Genomic DNA. Translation: AAC74472.1.
AP009048 Genomic DNA. Translation: BAE76425.1.
PIRiA64890.
RefSeqiNP_415908.1. NC_000913.3.
WP_001072837.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74472; AAC74472; b1390.
BAE76425; BAE76425; BAE76425.
GeneIDi945956.
KEGGiecj:JW1385.
eco:b1390.
PATRICi32118066. VBIEscCol129921_1453.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66092.1.
U00096 Genomic DNA. Translation: AAC74472.1.
AP009048 Genomic DNA. Translation: BAE76425.1.
PIRiA64890.
RefSeqiNP_415908.1. NC_000913.3.
WP_001072837.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OTKX-ray2.00A/B2-248[»]
3PVRX-ray2.10B/C2-248[»]
3PVTX-ray2.03B/C2-248[»]
3PVYX-ray2.15B/C2-248[»]
3PW1X-ray2.25B/C2-248[»]
3PW8X-ray2.97A/B2-248[»]
3PWQX-ray2.65A/B/E/G/I/J/K/R2-248[»]
4II4X-ray2.80B/C2-248[»]
ProteinModelPortaliP76079.
SMRiP76079. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260175. 102 interactions.
IntActiP76079. 7 interactions.
STRINGi511145.b1390.

Proteomic databases

PaxDbiP76079.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74472; AAC74472; b1390.
BAE76425; BAE76425; BAE76425.
GeneIDi945956.
KEGGiecj:JW1385.
eco:b1390.
PATRICi32118066. VBIEscCol129921_1453.

Organism-specific databases

EchoBASEiEB3500.
EcoGeneiEG13737. paaC.

Phylogenomic databases

eggNOGiENOG4105D9S. Bacteria.
COG3396. LUCA.
HOGENOMiHOG000254959.
InParanoidiP76079.
KOiK02611.
OMAiAWCGHAP.
OrthoDBiEOG64BQ4K.
PhylomeDBiP76079.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6711-MONOMER.
ECOL316407:JW1385-MONOMER.
MetaCyc:G6711-MONOMER.
BRENDAi1.14.13.149. 2026.

Miscellaneous databases

EvolutionaryTraceiP76079.
PROiP76079.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
IPR007814. PaaA_PaaC.
IPR011882. PaaC.
[Graphical view]
PfamiPF05138. PaaA_PaaC. 1 hit.
[Graphical view]
PIRSFiPIRSF037834. PA_CoA_Oase3. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR02158. PA_CoA_Oxy3. 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 COMPONENT.
  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 A MONOOXYGENASE COMPONENT.
  8. "The 2 a crystal structure of protein paac from e. coli."
    Midwest center for structural genomics (MCSG)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-248, SUBUNIT.
  9. "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 (2.25 ANGSTROMS) OF 2-248 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiPAAC_ECOLI
AccessioniPrimary (citable) accession number: P76079
Secondary accession number(s): O53011, Q2MBD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: January 20, 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

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.