2,3-dehydroadipyl-CoA hydratase - Escherichia coli (strain K12)

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P76082 (PAAF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
2,3-dehydroadipyl-CoA hydratase
EC=4.2.1.17

Alternative name(s):
Enoyl-CoA hydratase

Gene names

Name:	paaF
Synonyms:	ydbR
Ordered Locus Names:	b1393, JW1388

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. Ref.1 Ref.7
Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O. Ref.7
Pathway	Aromatic compound metabolism; phenylacetate degradation.
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.5
Disruption phenotype	Mutants accumulate delta3-dehydroadipate and are unable to use phenylacetate as a carbon source. Ref.6
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW phenylacetate catabolic process Inferred from mutant phenotype Ref.6. Source: EcoCyc
Molecular_function	enoyl-CoA hydratase activity Inferred from direct assay Ref.7. Source: UniProtKB identical protein binding Inferred from direct assay PubMed 22961985. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 255

255

2,3-dehydroadipyl-CoA hydratase

PRO_0000109330

Natural variations

Natural variant

R → Q in strain: W.

Natural variant

M → T in strain: W.

Natural variant

T → S in strain: W.

Secondary structure

255

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P76082 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 828C45DD658CAD1D
Show »

FASTA

255

27,237

        10         20         30         40         50         60 
MSELIVSRQQ RVLLLTLNRP AARNALNNAL LMQLVNELEA AATDTSISVC VITGNARFFA 

        70         80         90        100        110        120 
AGADLNEMAE KDLAATLNDT RPQLWARLQA FNKPLIAAVN GYALGAGCEL ALLCDVVVAG 

       130        140        150        160        170        180 
ENARFGLPEI TLGIMPGAGG TQRLIRSVGK SLASKMVLSG ESITAQQAQQ AGLVSDVFPS 

       190        200        210        220        230        240 
DLTLEYALQL ASKMARHSPL ALQAAKQALR QSQEVALQAG LAQERQLFTL LAATEDRHEG 

       250 
ISAFLQKRTP DFKGR

« Hide

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]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli." Ismail W., El-Said Mohamed M., Wanner B.L., Datsenko K.A., Eisenreich W., Rohdich F., Bacher A., Fuchs G. Eur. J. Biochem. 270:3047-3054(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[7]	"Bacterial phenylalanine and phenylacetate catabolic pathway revealed." Teufel R., Mascaraque V., Ismail W., Voss M., Perera J., Eisenreich W., Haehnel W., Fuchs G. Proc. Natl. Acad. Sci. U.S.A. 107:14390-14395(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ENOYL-COA HYDRATASE, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97452 Genomic DNA. Translation: CAA66095.1.
U00096 Genomic DNA. Translation: AAC74475.1.
AP009048 Genomic DNA. Translation: BAA14999.2.

PIR

D64890.

RefSeq

NP_415911.1. NC_000913.2.
YP_489662.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FZW	X-ray	2.55	A/B	1-255	[»]

ProteinModelPortal

P76082.

SMR

P76082. Positions 1-255.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10425N.

IntAct

P76082. 1 interaction.

STRING

511145.b1393.

Proteomic databases

PaxDb

P76082.

PRIDE

P76082.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74475; AAC74475; b1393.
BAA14999; BAA14999; BAA14999.

GeneID

12931976.
946011.

KEGG

ecj:Y75_p1370.
eco:b1393.

PATRIC

32118072. VBIEscCol129921_1456.

Organism-specific databases

EchoBASE

EB3503.

EcoGene

EG13740. paaF.

Phylogenomic databases

eggNOG

COG1024.

HOGENOM

HOG000027939.

K01692.

OMA

MCADIVI.

ProtClustDB

PRK09674.

Enzyme and pathway databases

BioCyc

EcoCyc:G6714-MONOMER.
ECOL316407:JW1388-MONOMER.

UniPathway

UPA00930.

Gene expression databases

Genevestigator

P76082.

Family and domain databases

InterPro

IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PAAF_ECOLI

Accession

Primary (citable) accession number: P76082
Secondary accession number(s): O53014, P78288

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents