Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q62651 (ECH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. 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:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

EC=5.3.3.-
Gene names
Name:Ech1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homohexamer. Ref.5

Subcellular location

Mitochondrion. Peroxisome.

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
Peroxisome
   DomainTransit peptide
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from direct assay Ref.4. Source: UniProtKB

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion Potential
Chain34 – 327294Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
PRO_0000007419

Regions

Motif325 – 3273Microbody targeting signal Potential

Sites

Binding site1731Substrate; via amide nitrogen By similarity
Site1961Important for catalytic activity Probable
Site2041Important for catalytic activity Potential

Amino acid modifications

Modified residue2301N6-succinyllysine By similarity
Modified residue3161N6-succinyllysine By similarity
Modified residue3261N6-acetyllysine By similarity

Experimental info

Sequence conflict1641A → T in AAA82008. Ref.1

Secondary structure

............................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62651 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 6FAE35D7D5F66BC2

FASTA32736,172
        10         20         30         40         50         60 
MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS DHNYESIQVT 

        70         80         90        100        110        120 
SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM 

       130        140        150        160        170        180 
DMASDILQPP GDDVARIAWY LRDLISRYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLISA 

       190        200        210        220        230        240 
CDIRYCTQDA FFQVKEVDVG LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG 

       250        260        270        280        290        300 
LVSRVFPDKD VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM 

       310        320 
LQTQDIIKSV QAAMEKKDSK SITFSKL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase."
Fitzpatrick D.R., Germain-Lee E., Valle D.
Genomics 27:457-466(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[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: Pituitary.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 185-210 AND 219-229, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[4]"Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization."
Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D., Fitzpatrick D.R., Vihinen M., Valle D., Hiltunen J.K.
J. Biol. Chem. 273:349-355(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.
[5]"The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis."
Modis Y., Filppula S.A., Novikov D.K., Norledge B., Hiltunen J.K., Wierenga R.K.
Structure 6:957-970(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SEQUENCE REVISION TO 164, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08976 mRNA. Translation: AAA82008.1.
BC062226 mRNA. Translation: AAH62226.1.
PIRA57626.
RefSeqNP_072116.1. NM_022594.1.
UniGeneRn.6148.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DCIX-ray1.50A/B/C54-327[»]
ProteinModelPortalQ62651.
SMRQ62651. Positions 54-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ62651. 1 interaction.
MINTMINT-4597589.
STRING10116.ENSRNOP00000027537.

Proteomic databases

PaxDbQ62651.
PRIDEQ62651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027537; ENSRNOP00000027537; ENSRNOG00000020308.
GeneID64526.
KEGGrno:64526.
UCSCRGD:69353. rat.

Organism-specific databases

CTD1891.
RGD69353. Ech1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00720000108577.
HOGENOMHOG000027939.
HOVERGENHBG005556.
InParanoidQ62651.
KOK12663.
OMASWVKDVC.
OrthoDBEOG7JHM64.
PhylomeDBQ62651.
TreeFamTF314317.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ62651.

Family and domain databases

Gene3D1.10.12.10. 1 hit.
3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ62651.
NextBio613350.
PROQ62651.

Entry information

Entry nameECH1_RAT
AccessionPrimary (citable) accession number: Q62651
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: June 11, 2014
This is version 114 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