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P55100 (ECHP_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxisomal bifunctional enzyme
Short name=PBE
Short name=PBFE

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
    EC=4.2.1.17
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:EHHADH
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Enzyme regulation

Enzyme activity enhanced by acetylation By similarity.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome.

Post-translational modification

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-348. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 726726Peroxisomal bifunctional enzyme
PRO_0000109246

Regions

Region1 – 284284Enoyl-CoA hydratase / isomerase
Region285 – 5752913-hydroxyacyl-CoA dehydrogenase
Motif724 – 7263Microbody targeting signal By similarity

Sites

Binding site1031Substrate; via amide nitrogen By similarity
Site1061Important for catalytic activity By similarity
Site1261Important for catalytic activity By similarity

Amino acid modifications

Modified residue1671N6-acetyllysine By similarity
Modified residue1731N6-acetyllysine By similarity
Modified residue3331N6-acetyllysine By similarity
Modified residue3481N6-acetyllysine By similarity
Modified residue5871N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P55100 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F1702122D62C5FF3

FASTA72679,375
        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

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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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X92742 mRNA. Translation: CAA63403.1.
X85112 mRNA. Translation: CAA59431.1.
PIRS57651. S68697.
RefSeqNP_001166417.1. NM_001172946.1.

3D structure databases

ProteinModelPortalP55100.
SMRP55100. Positions 264-720.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000019312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135519.

Organism-specific databases

CTD1962.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidP55100.
OrthoDBEOG47PX5F.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 2 hits.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameECHP_CAVPO
AccessionPrimary (citable) accession number: P55100
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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