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P07896 (ECHP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.6

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-345. 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 – 722722Peroxisomal bifunctional enzyme
PRO_0000109249

Regions

Region1 – 281281Enoyl-CoA hydratase / isomerase
Region282 – 5712903-hydroxyacyl-CoA dehydrogenase
Motif720 – 7223Microbody targeting signal

Sites

Binding site1001Substrate; via amide nitrogen By similarity
Site1031Important for catalytic activity By similarity
Site1231Important for catalytic activity By similarity

Amino acid modifications

Modified residue21Blocked amino end (Ala)
Modified residue381N6-succinyllysine By similarity
Modified residue1731N6-acetyllysine; alternate By similarity
Modified residue1731N6-succinyllysine; alternate By similarity
Modified residue1821N6-succinyllysine By similarity
Modified residue1901N6-acetyllysine; alternate By similarity
Modified residue1901N6-succinyllysine; alternate By similarity
Modified residue2181N6-acetyllysine; alternate By similarity
Modified residue2181N6-succinyllysine; alternate By similarity
Modified residue2411N6-succinyllysine By similarity
Modified residue2491N6-acetyllysine By similarity
Modified residue2531N6-succinyllysine By similarity
Modified residue2751N6-acetyllysine; alternate By similarity
Modified residue2751N6-succinyllysine; alternate By similarity
Modified residue2791N6-succinyllysine By similarity
Modified residue2891N6-succinyllysine By similarity
Modified residue3301N6-succinyllysine By similarity
Modified residue3451N6-acetyllysine By similarity
Modified residue3591N6-acetyllysine By similarity
Modified residue4631N6-acetyllysine By similarity
Modified residue5311N6-succinyllysine By similarity
Modified residue5761N6-succinyllysine By similarity
Modified residue5831N6-acetyllysine; alternate By similarity
Modified residue5831N6-succinyllysine; alternate By similarity
Modified residue5901N6-acetyllysine; alternate By similarity
Modified residue5901N6-succinyllysine; alternate By similarity
Modified residue7091N6-acetyllysine; alternate By similarity
Modified residue7091N6-succinyllysine; alternate By similarity
Modified residue7211N6-succinyllysine By similarity

Secondary structure

...................................................................................................................................... 722
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07896 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 76ACC709C5F23E86

FASTA72278,658
        10         20         30         40         50         60 
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI CGANGNFCAG 

        70         80         90        100        110        120 
ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG GLELALGCHY RIANAKARVG 

       130        140        150        160        170        180 
LPEVTLGILP GARGTQLLPR VVGVPVALDL ITSGKYLSAD EALRLGILDA VVKSDPVEEA 

       190        200        210        220        230        240 
IKFAQKIIDK PIEPRRIFNK PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV 

       250        260        270        280        290        300 
KHPYEVGIKE EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG 

       310        320        330        340        350        360 
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA HQNGQASAKP 

       370        380        390        400        410        420 
KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK PGAFLCTNTS ALNVDDIASS 

       430        440        450        460        470        480 
TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS SPTTIATVMS LSKKIGKIGV VVGNCYGFVG 

       490        500        510        520        530        540 
NRMLAPYYNQ GFFLLEEGSK PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG 

       550        560        570        580        590        600 
PSLPPGTPVR KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS 

       610        620        630        640        650        660 
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL HGYGWPRHKG 

       670        680        690        700        710        720 
GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL VAQGSPPLKE WQSLAGPHGS 


KL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.
J. Biol. Chem. 260:8905-8910(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]"Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
Ishii N., Hijikata M., Osumi T., Hashimoto T.
J. Biol. Chem. 262:8144-8150(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
[4]"Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins."
Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P.
Eur. J. Biochem. 240:660-666(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719.
[5]"Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities."
Palosaari P.M., Hiltunen J.K.
J. Biol. Chem. 265:2446-2449(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ISOMERASE.
[6]"Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1."
Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K.
J. Mol. Biol. 355:734-746(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03249 mRNA. Translation: AAA41825.1.
BC089777 mRNA. Translation: AAH89777.1.
J02748 Genomic DNA. Translation: AAA41826.1.
PIRDWRTEP. A23575.
RefSeqNP_598290.1. NM_133606.1.
UniGeneRn.3671.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCJX-ray1.90A260-722[»]
2X58X-ray2.80A/B1-722[»]
3ZW8X-ray2.50A/B1-722[»]
3ZW9X-ray2.90A/B1-722[»]
3ZWAX-ray2.47A/B1-722[»]
3ZWBX-ray3.10A/B1-722[»]
3ZWCX-ray2.30A/B1-722[»]
ProteinModelPortalP07896.
SMRP07896. Positions 261-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07896. 6 interactions.
STRING10116.ENSRNOP00000002410.

Chemistry

ChEMBLCHEMBL3232.

PTM databases

PhosphoSiteP07896.

Proteomic databases

PaxDbP07896.
PRIDEP07896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770.
GeneID171142.
KEGGrno:171142.
UCSCRGD:621441. rat.

Organism-specific databases

CTD1962.
RGD621441. Ehhadh.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00720000108673.
HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidP07896.
KOK07514.
OMAKGWYQYD.
OrthoDBEOG725DH0.
PhylomeDBP07896.
TreeFamTF316708.

Enzyme and pathway databases

SABIO-RKP07896.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorP07896.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 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. SSF48179. 2 hits.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07896.
NextBio621936.
PROP07896.

Entry information

Entry nameECHP_RAT
AccessionPrimary (citable) accession number: P07896
Secondary accession number(s): Q5EBD2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways