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P76080

- PAAD_ECOLI

UniProt

P76080 - PAAD_ECOLI

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Protein

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

Gene
paaD, ydbQ, b1391, JW5217
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Pathwayi

GO - Biological processi

  1. 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: Chromosome, UP000000625: 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

Gene expression databases

GenevestigatoriP76080.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP76080. 4 interactions.
STRINGi511145.b1391.

Structurei

3D structure databases

ProteinModelPortaliP76080.
SMRiP76080. Positions 12-104.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2151.
HOGENOMiHOG000249723.
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

MQRLATIAPP QVHEIWALLS QIPDPEIPVL TITDLGMVRN VTQMGEGWVI    50
GFTPTYSGCP ATEHLIGAIR EAMTTNGFTP VQVVLQLDPA WTTDWMTPDA 100
RERLREYGIS PPAGHSCHAH LPPEVRCPRC ASVHTTLISE FGSTACKALY 150
RCDSCREPFD YFKCI 165
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.

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:
EMBL
GenBank
DDBJ
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.
YP_489660.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74473; AAC74473; b1391.
BAE76426; BAE76426; BAE76426.
GeneIDi12933892.
945959.
KEGGiecj:Y75_p1368.
eco:b1391.
PATRICi32118068. VBIEscCol129921_1454.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97452 Genomic DNA. Translation: CAA66093.1 . Different initiation.
U00096 Genomic DNA. Translation: AAC74473.4 .
AP009048 Genomic DNA. Translation: BAE76426.1 .
PIRi B64890.
RefSeqi NP_415909.4. NC_000913.3.
YP_489660.1. NC_007779.1.

3D structure databases

ProteinModelPortali P76080.
SMRi P76080. Positions 12-104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P76080. 4 interactions.
STRINGi 511145.b1391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74473 ; AAC74473 ; b1391 .
BAE76426 ; BAE76426 ; BAE76426 .
GeneIDi 12933892.
945959.
KEGGi ecj:Y75_p1368.
eco:b1391.
PATRICi 32118068. VBIEscCol129921_1454.

Organism-specific databases

EchoBASEi EB3501.
EcoGenei EG13738. paaD.

Phylogenomic databases

eggNOGi COG2151.
HOGENOMi HOG000249723.
KOi K02612.
OrthoDBi EOG664CH5.
PhylomeDBi P76080.

Enzyme and pathway databases

UniPathwayi UPA00930 .
BioCyci EcoCyc:G6712-MONOMER.
ECOL316407:JW5217-MONOMER.

Miscellaneous databases

PROi P76080.

Gene expression databases

Genevestigatori P76080.

Family and domain databases

InterProi IPR002744. DUF59.
IPR011883. PA_CoA_Oase4.
[Graphical view ]
Pfami PF01883. DUF59. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02159. PA_CoA_Oxy4. 1 hit.
ProtoNeti Search...

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: May 14, 2014
This is version 87 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

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