pig-q6q2c2

 
Sus scrofa (Pig) soluble (epoxide hydratase) (cytosolic epoxide hydrolase)

Comment
only c-term homologous PfamA Abhydrolase_1 286 540 N-term HAD haloacid dehalogenase


Relationship
Block X
Sus scrofa position in NCBI Life Tree :
N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain.
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Laurasiatheria: N E > Cetartiodactyla: N E > Suina: N E > Suidae: N E > Sus: N E > Sus scrofa: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
No structure
No kinetic



1 Genbank : AY566232
1 UniProt : Q6Q2C2
1 UniProtTrembl : Q6Q2C2
1 Interpro : Q6Q2C2
1 Prodom : Q6Q2C2
1 Pfam : Q6Q2C2
1 PIRSF : Q6Q2C2
1 SUPERFAM : Q6Q2C2
1 QuickSwissBlast : Q6Q2C2
 
Sequence
Graphical view for this peptide sequence: pig-q6q2c2
Colored MSA for Epoxide_hydrolase (raw)
GVRLHFVEMGSGPAVCLCHGFPESWFSWRYQIPALAQAGFRVLAVDMKGY
GESSAPPEIEEYSLEVLCKDMVTFLNKLGLSQAVFIGHDWGGVLVWNMAL
FYPERVRAVASLNTPFMPSNPNVSPMEIIKANPVFDYQLYFQEPGVAEAE
LEQNLDRTFKNFFRAHDETFLTTNRVRELGGLFVGTPEEPSLSRLVTEED
IQFYVQQFKKSGFRGPLNWYRNMERNWQWGCKGSGRKILIPALMVTAEND
LVLHPKMSKHMENWIPHLKRGHIKDCGHWTQIDKPAELNRILIEWLETDA
RNPLVDSKL
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

GVRLHFVEMGSGPAVCLCHGFPESWFSWRYQIPALAQAGFRVLAVDMKGY
GESSAPPEIEEYSLEVLCKDMVTFLNKLGLSQAVFIGHDWGGVLVWNMAL
FYPERVRAVASLNTPFMPSNPNVSPMEIIKANPVFDYQLYFQEPGVAEAE
LEQNLDRTFKNFFRAHDETFLTTNRVRELGGLFVGTPEEPSLSRLVTEED
IQFYVQQFKKSGFRGPLNWYRNMERNWQWGCKGSGRKILIPALMVTAEND
LVLHPKMSKHMENWIPHLKRGHIKDCGHWTQIDKPAELNRILIEWLETDA
RNPLVDSKL

no DNA




References
    Title: Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules
    Kannai K, Aranyi P, Bocskei Z, Ferenczy G, Harmat V, Simon K, Batori S, Naray-Szabo G, Hermecz I
    Ref: Journal of Medicinal Chemistry, 51:7514, 2008 : PubMed

            

    Title: Cytochrome p450-dependent lipid metabolism in preovulatory follicles
    Newman JW, Stok JE, Vidal JD, Corbin CJ, Huang Q, Hammock BD, Conley AJ
    Ref: Endocrinology, 145:5097, 2004 : PubMed

            

    Title: Concerted structural changes in the peptidase and the propeller domains of prolyl oligopeptidase are required for substrate binding
    Szeltner Z, Rea D, Juhasz T, Renner V, Fulop V, Polgar L
    Ref: Journal of Molecular Biology, 340:627, 2004 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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