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Protein

Putative 1,2-phenylacetyl-CoA epoxidase, subunit D

Gene

paaD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Possible 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 D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA.2 Publications

Pathway: 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:G6712-MONOMER.
ECOL316407:JW5217-MONOMER.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
Alternative name(s):
1,2-phenylacetyl-CoA monooxygenase, subunit D
Gene namesi
Name:paaD
Synonyms:ydbQ
Ordered Locus Names:b1391, JW5217
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13738. paaD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Putative 1,2-phenylacetyl-CoA epoxidase, subunit DPRO_0000058162Add
BLAST

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

Monomer.1 Publication

Protein-protein interaction databases

IntActiP76080. 4 interactions.
STRINGi511145.b1391.

Structurei

3D structure databases

ProteinModelPortaliP76080.
SMRiP76080. Positions 10-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2151.
HOGENOMiHOG000249723.
InParanoidiP76080.
KOiK02612.
OrthoDBiEOG664CH5.
PhylomeDBiP76080.

Family and domain databases

InterProiIPR002744. DUF59.
IPR011883. PA_CoA_Oase4.
[Graphical view]
PfamiPF01883. DUF59. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02159. PA_CoA_Oxy4. 1 hit.

Sequencei

Sequence statusi: Complete.

P76080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLATIAPP QVHEIWALLS QIPDPEIPVL TITDLGMVRN VTQMGEGWVI
60 70 80 90 100
GFTPTYSGCP ATEHLIGAIR EAMTTNGFTP VQVVLQLDPA WTTDWMTPDA
110 120 130 140 150
RERLREYGIS PPAGHSCHAH LPPEVRCPRC ASVHTTLISE FGSTACKALY
160
RCDSCREPFD YFKCI
Length:165
Mass (Da):18,324
Last modified:November 24, 2009 - v2
Checksum:i67AE8F04C8F0045B
GO

Sequence cautioni

The sequence CAA66093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471G → E in strain: W.
Natural varianti76 – 761N → H in strain: W.
Natural varianti106 – 1061E → Q in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66093.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74473.4.
AP009048 Genomic DNA. Translation: BAE76426.1.
PIRiB64890.
RefSeqiNP_415909.4. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74473; AAC74473; b1391.
BAE76426; BAE76426; BAE76426.
GeneIDi945959.
KEGGiecj:Y75_p1368.
eco:b1391.
PATRICi32118068. VBIEscCol129921_1454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66093.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74473.4.
AP009048 Genomic DNA. Translation: BAE76426.1.
PIRiB64890.
RefSeqiNP_415909.4. NC_000913.3.

3D structure databases

ProteinModelPortaliP76080.
SMRiP76080. Positions 10-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP76080. 4 interactions.
STRINGi511145.b1391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74473; AAC74473; b1391.
BAE76426; BAE76426; BAE76426.
GeneIDi945959.
KEGGiecj:Y75_p1368.
eco:b1391.
PATRICi32118068. VBIEscCol129921_1454.

Organism-specific databases

EchoBASEiEB3501.
EcoGeneiEG13738. paaD.

Phylogenomic databases

eggNOGiCOG2151.
HOGENOMiHOG000249723.
InParanoidiP76080.
KOiK02612.
OrthoDBiEOG664CH5.
PhylomeDBiP76080.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6712-MONOMER.
ECOL316407:JW5217-MONOMER.

Miscellaneous databases

PROiP76080.

Family and domain databases

InterProiIPR002744. DUF59.
IPR011883. PA_CoA_Oase4.
[Graphical view]
PfamiPF01883. DUF59. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02159. PA_CoA_Oxy4. 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 POSSIBLE MONOOXYGENASE COMPONENT.
  6. "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: SUBUNIT.

Entry informationi

Entry nameiPAAD_ECOLI
AccessioniPrimary (citable) accession number: P76080
Secondary accession number(s): O53012, Q2MBD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 24, 2009
Last modified: June 24, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

PaaD component is not essential for the reaction in vitro.

Keywords - Technical termi

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

External Data

Dasty 3

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 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.