ID   ECHP_CAVPO              Reviewed;         726 AA.
AC   P55100;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 67.
DE   RecName: Full=Peroxisomal bifunctional enzyme;
DE            Short=PBE;
DE            Short=PBFE;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase;
DE              EC=4.2.1.17;
DE              EC=5.3.3.8;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=EHHADH;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=96140708; PubMed=8549802; DOI=10.1016/0014-5793(95)01425-X;
RA   Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N.;
RT   "Cloning and tissue expression of two cDNAs encoding the peroxisomal
RT   2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea
RT   pig liver.";
RL   FEBS Lett. 378:57-60(1996).
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family.
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DR   EMBL; X92742; CAA63403.1; -; mRNA.
DR   EMBL; X85112; CAA59431.1; -; mRNA.
DR   PIR; S68697; S57651.
DR   HSSP; P14604; 1MJ3.
DR   SMR; P55100; 264-720.
DR   HOVERGEN; P55100; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:EC.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DHase_NAD-bd.
DR   InterPro; IPR006108; 3HC_DHase_C.
DR   InterPro; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 2.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism;
KW   Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Peroxisome;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    726       Peroxisomal bifunctional enzyme.
FT                                /FTId=PRO_0000109246.
FT   REGION        2    284       Enoyl-CoA hydratase / isomerase.
FT   REGION      285    575       3-hydroxyacyl-CoA dehydrogenase.
FT   MOTIF       724    726       Microbody targeting signal (Potential).
FT   ACT_SITE    106    106       Proton acceptor (By similarity).
FT   ACT_SITE    126    126       Proton donor (By similarity).
FT   MOD_RES     333    333       N6-acetyllysine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
SQ   SEQUENCE   726 AA;  79375 MW;  F1702122D62C5FF3 CRC64;
     MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI SGANNIFCAG
     ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA LGGGLELSLG CHYRIAHAEA
     RIGFPEVTLG ILPGARGTQL LPRLIGVPAA LDLITSGRHI TAGEALKLGI LDKVVNSAPV
     EEAIKFAQKI LNQPLEPRRI LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ
     ASVQYPYEGG IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS
     SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA SKSRQQCGQQ
     RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS AVCKPEAFLC TNTSALDVDE
     IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY
     GFVGNRMLRS YYEQTNFLLE DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ
     GLTGPSLQGT APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS
     KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID VIYLHGYGWP
     RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY LKKLASQGNP PLKEWQSLAG
     LPSSKL
//