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Protein

2,3-dehydroadipyl-CoA hydratase

Gene

paaF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA.2 Publications

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.1 Publication

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 - Molecular functioni

  • enoyl-CoA hydratase activity Source: UniProtKB
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • fatty acid metabolic process Source: UniProtKB-KW
  • phenylacetate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:G6714-MONOMER.
ECOL316407:JW1388-MONOMER.
BRENDAi4.2.1.17. 2026.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-dehydroadipyl-CoA hydratase (EC:4.2.1.17)
Alternative name(s):
Enoyl-CoA hydratase
Gene namesi
Name:paaF
Synonyms:ydbR
Ordered Locus Names:b1393, JW1388
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13740. paaF.

Pathology & Biotechi

Disruption phenotypei

Mutants accumulate delta3-dehydroadipate and are unable to use phenylacetate as a carbon source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2552552,3-dehydroadipyl-CoA hydratasePRO_0000109330Add
BLAST

Proteomic databases

PaxDbiP76082.
PRIDEiP76082.

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

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260970. 248 interactions.
DIPiDIP-10425N.
IntActiP76082. 1 interaction.
STRINGi511145.b1393.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi12 – 187Combined sources
Helixi20 – 223Combined sources
Helixi28 – 4215Combined sources
Beta strandi49 – 535Combined sources
Beta strandi56 – 616Combined sources
Helixi65 – 695Combined sources
Helixi73 – 775Combined sources
Helixi81 – 899Combined sources
Beta strandi95 – 995Combined sources
Beta strandi101 – 1044Combined sources
Helixi106 – 1138Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi124 – 1263Combined sources
Helixi129 – 1324Combined sources
Helixi140 – 1489Combined sources
Helixi150 – 15910Combined sources
Helixi165 – 1717Combined sources
Beta strandi175 – 1784Combined sources
Turni180 – 1823Combined sources
Helixi183 – 19412Combined sources
Helixi199 – 21214Combined sources
Helixi217 – 23216Combined sources
Helixi235 – 24511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FZWX-ray2.55A/B1-255[»]
ProteinModelPortaliP76082.
SMRiP76082. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E39. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
InParanoidiP76082.
KOiK01692.
OMAiDLLIHRH.
OrthoDBiEOG6M9F0M.
PhylomeDBiP76082.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76082-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELIVSRQQ RVLLLTLNRP AARNALNNAL LMQLVNELEA AATDTSISVC
60 70 80 90 100
VITGNARFFA AGADLNEMAE KDLAATLNDT RPQLWARLQA FNKPLIAAVN
110 120 130 140 150
GYALGAGCEL ALLCDVVVAG ENARFGLPEI TLGIMPGAGG TQRLIRSVGK
160 170 180 190 200
SLASKMVLSG ESITAQQAQQ AGLVSDVFPS DLTLEYALQL ASKMARHSPL
210 220 230 240 250
ALQAAKQALR QSQEVALQAG LAQERQLFTL LAATEDRHEG ISAFLQKRTP

DFKGR
Length:255
Mass (Da):27,237
Last modified:February 1, 1997 - v1
Checksum:i828C45DD658CAD1D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111R → Q in strain: W.
Natural varianti32 – 321M → T in strain: W.
Natural varianti45 – 451T → S in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66095.1.
U00096 Genomic DNA. Translation: AAC74475.1.
AP009048 Genomic DNA. Translation: BAA14999.2.
PIRiD64890.
RefSeqiNP_415911.1. NC_000913.3.
WP_001292353.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74475; AAC74475; b1393.
BAA14999; BAA14999; BAA14999.
GeneIDi946011.
KEGGiecj:JW1388.
eco:b1393.
PATRICi32118072. VBIEscCol129921_1456.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66095.1.
U00096 Genomic DNA. Translation: AAC74475.1.
AP009048 Genomic DNA. Translation: BAA14999.2.
PIRiD64890.
RefSeqiNP_415911.1. NC_000913.3.
WP_001292353.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FZWX-ray2.55A/B1-255[»]
ProteinModelPortaliP76082.
SMRiP76082. Positions 1-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260970. 248 interactions.
DIPiDIP-10425N.
IntActiP76082. 1 interaction.
STRINGi511145.b1393.

Proteomic databases

PaxDbiP76082.
PRIDEiP76082.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74475; AAC74475; b1393.
BAA14999; BAA14999; BAA14999.
GeneIDi946011.
KEGGiecj:JW1388.
eco:b1393.
PATRICi32118072. VBIEscCol129921_1456.

Organism-specific databases

EchoBASEiEB3503.
EcoGeneiEG13740. paaF.

Phylogenomic databases

eggNOGiENOG4105E39. Bacteria.
COG1024. LUCA.
HOGENOMiHOG000027939.
InParanoidiP76082.
KOiK01692.
OMAiDLLIHRH.
OrthoDBiEOG6M9F0M.
PhylomeDBiP76082.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6714-MONOMER.
ECOL316407:JW1388-MONOMER.
BRENDAi4.2.1.17. 2026.

Miscellaneous databases

PROiP76082.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
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 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. Cited for: FUNCTION AS AN ENOYL-COA HYDRATASE, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiPAAF_ECOLI
AccessioniPrimary (citable) accession number: P76082
Secondary accession number(s): O53014, P78288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 20, 2016
This is version 114 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
  4. SIMILARITY comments
    Index of protein domains and families

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.