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UniProtKB/Swiss-Prot entry P55100

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ECHP_CAVPO
Primary accession number P55100
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 66)
Name and origin of the protein
Protein name Peroxisomal bifunctional enzyme
Synonyms PBE
PBFE
Includes Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
     (EC 4.2.1.17)
     (EC 5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase
     (EC 1.1.1.35)
Gene name
Name: EHHADH
From
Cavia porcellus (Guinea pig) [TaxID: 10141] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/0014-5793(95)01425-X; PubMed=8549802 [NCBI, ExPASy, EBI, Israel, Japan]
Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N.;
"Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver.";
FEBS Lett. 378:57-60(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X92742; CAA63403.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X85112; CAA59431.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S68697; S57651.
3D structure databases
HSSP P14604; 1MJ3. [HSSP ENTRY / PDB]
SMR P55100; 264-720.
ModBase P55100.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0003857; Molecular function: 3-hydroxyacyl-CoA dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004165; Molecular function: dodecenoyl-CoA delta-isomerase activity (inferred from electronic annotation from EC).
GO:0004300; Molecular function: enoyl-CoA hydratase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
IPR006108; 3HC_DHase_C.
IPR001753; Crotonase_core.
IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 2.
Pfam PF00725; 3HCDH; 2.
PF02737; 3HCDH_N; 1.
PF00378; ECH; 1.
Pfam graphical view of domain structure.
PROSITE PS00166; ENOYL_COA_HYDRATASE; 1.
BLOCKS P55100.
ProtoNet P55100.
Phylogenomic databases
HOVERGEN P55100; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   726  725     Peroxisomal bifunctional enzyme. PRO_0000109246
REGION   2   284  283     Enoyl-CoA hydratase / isomerase. 
REGION   285   575  291     3-hydroxyacyl-CoA dehydrogenase. 
MOTIF   724   726  3     Microbody targeting signal (Potential). 
ACT_SITE   106   106        Proton acceptor (By similarity). 
ACT_SITE   126   126        Proton donor (By similarity). 
MOD_RES   333   333        N6-acetyllysine (By similarity). 
MOD_RES   362   362        Phosphoserine (By similarity). 
Sequence information
Length: 726 AA [This is the length of the unprocessed precursor] Molecular weight: 79375 Da [This is the MW of the unprocessed precursor] CRC64: F1702122D62C5FF3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI SGANNIFCAG 

        70         80         90        100        110        120 
ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA LGGGLELSLG CHYRIAHAEA 

       130        140        150        160        170        180 
RIGFPEVTLG ILPGARGTQL LPRLIGVPAA LDLITSGRHI TAGEALKLGI LDKVVNSAPV 

       190        200        210        220        230        240 
EEAIKFAQKI LNQPLEPRRI LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ 

       250        260        270        280        290        300 
ASVQYPYEGG IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS 

       310        320        330        340        350        360 
SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA SKSRQQCGQQ 

       370        380        390        400        410        420 
RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS AVCKPEAFLC TNTSALDVDE 

       430        440        450        460        470        480 
IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY 

       490        500        510        520        530        540 
GFVGNRMLRS YYEQTNFLLE DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ 

       550        560        570        580        590        600 
GLTGPSLQGT APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS 

       610        620        630        640        650        660 
KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID VIYLHGYGWP 

       670        680        690        700        710        720 
RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY LKKLASQGNP PLKEWQSLAG 


LPSSKL
P55100 in FASTA format

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