P76080 (PAAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative 1,2-phenylacetyl-CoA epoxidase, subunit D

Alternative name(s):
1,2-phenylacetyl-CoA monooxygenase, subunit D

Gene names

Name:	paaD
Synonyms:	ydbQ
Ordered Locus Names:	b1391, JW5217

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5
Pathway	Aromatic compound metabolism; phenylacetate degradation.
Subunit structure	Monomer. Ref.6
Induction	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. Ref.1 Ref.4
Miscellaneous	PaaD component is not essential for the reaction in vitro.
Sequence caution	The sequence CAA66093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phenylacetate catabolic process Inferred from mutant phenotype Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 165	165	Putative 1,2-phenylacetyl-CoA epoxidase, subunit D		PRO_0000058162
Natural variations
	Natural variant	47	1	G → E in strain: W.
	Natural variant	76	1	N → H in strain: W.
	Natural variant	106	1	E → Q in strain: W.

Sequences

	Sequence		Length	Mass (Da)
	P76080 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: 67AE8F04C8F0045B	FASTA	165	18,324
	10 20 30 40 50 60 MQRLATIAPP QVHEIWALLS QIPDPEIPVL TITDLGMVRN VTQMGEGWVI GFTPTYSGCP 70 80 90 100 110 120 ATEHLIGAIR EAMTTNGFTP VQVVLQLDPA WTTDWMTPDA RERLREYGIS PPAGHSCHAH 130 140 150 160 LPPEVRCPRC ASVHTTLISE FGSTACKALY RCDSCREPFD YFKCI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97452 Genomic DNA. Translation: CAA66093.1. Different initiation. U00096 Genomic DNA. Translation: AAC74473.4. AP009048 Genomic DNA. Translation: BAE76426.1.
PIR	B64890.
RefSeq	NP_415909.4. NC_000913.2. YP_489660.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76080.
SMR	P76080. Positions 12-104.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b1391.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74473; AAC74473; b1391. BAE76426; BAE76426; BAE76426.
GeneID	12933892. 945959.
KEGG	ecj:Y75_p1368. eco:b1391.
PATRIC	32118068. VBIEscCol129921_1454.
Organism-specific databases
EchoBASE	EB3501.
EcoGene	EG13738. paaD.
Phylogenomic databases
eggNOG	COG2151.
HOGENOM	HOG000249723.
KO	K02612.
ProtClustDB	CLSK950271.
Enzyme and pathway databases
BioCyc	EcoCyc:G6712-MONOMER. ECOL316407:JW5217-MONOMER.
UniPathway	UPA00930.
Gene expression databases
Genevestigator	P76080.
Family and domain databases
InterPro	IPR002744. DUF59. IPR011883. PA_CoA_Oase4. [Graphical view]
Pfam	PF01883. DUF59. 1 hit. [Graphical view]
TIGRFAMs	TIGR02159. PA_CoA_Oxy4. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAAD_ECOLI

Accession

Primary (citable) accession number: P76080
Secondary accession number(s): O53012, Q2MBD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program