Reviewed, UniProtKB/Swiss-Prot P55100 (ECHP_CAVPO)

Names and origin

Protein names

Recommended name:
    Peroxisomal bifunctional enzyme
      Short name=PBE
      Short name=PBFE
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
              EC=4.2.1.17
              EC=5.3.3.8
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:

EHHADH

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	726 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Monomer By similarity.
Subcellular location	Peroxisome.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: EC enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 726	725	Peroxisomal bifunctional enzyme		PRO_0000109246
Regions
	Region	2 – 284	283	Enoyl-CoA hydratase / isomerase
	Region	285 – 575	291	3-hydroxyacyl-CoA dehydrogenase
	Motif	724 – 726	3	Microbody targeting signal Potential
Sites
	Active site	106	1	Proton acceptor By similarity
	Active site	126	1	Proton donor By similarity
Amino acid modifications
	Modified residue	333	1	N6-acetyllysine By similarity
	Modified residue	362	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55100-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F1702122D62C5FF3	FASTA	726	79,375
	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

References

[1]

"Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver." Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N. FEBS Lett. 378:57-60(1996) [PubMed: 8549802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X92742 mRNA. Translation: CAA63403.1. X85112 mRNA. Translation: CAA59431.1.
PIR	S57651. S68697.
3D structure databases
HSSP	HSSP built from PDB template 1MJ3 based on UniProtKB P14604.
SMR	P55100. Positions 264-720.
ModBase	Search...
Genome annotation databases
Ensembl	ENSCPOG00000005685. Cavia porcellus. [Contig view]
Phylogenomic databases
HOVERGEN	P55100.
Enzyme and pathway databases
BRENDA	1.1.1.35. 44. 4.2.1.17. 44. 5.3.3.8. 44.
Family and domain databases
InterPro	IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 2 hits.
Pfam	PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
PROSITE	PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ECHP_CAVPO

Accession

Primary (citable) accession number: P55100

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)