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Q62651

- ECH1_RAT

UniProt

Q62651 - ECH1_RAT

Protein

Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial

Gene

Ech1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei173 – 1731Substrate; via amide nitrogenBy similarity
    Sitei196 – 1961Important for catalytic activityCurated
    Sitei204 – 2041Important for catalytic activitySequence Analysis

    GO - Molecular functioni

    1. isomerase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial (EC:5.3.3.-)
    Gene namesi
    Name:Ech1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi69353. Ech1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB
    2. peroxisome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
    BLAST
    Chaini34 – 327294Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrialPRO_0000007419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei230 – 2301N6-succinyllysineBy similarity
    Modified residuei316 – 3161N6-succinyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ62651.
    PRIDEiQ62651.

    Expressioni

    Gene expression databases

    GenevestigatoriQ62651.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    IntActiQ62651. 1 interaction.
    MINTiMINT-4597589.
    STRINGi10116.ENSRNOP00000027537.

    Structurei

    Secondary structure

    1
    327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 639
    Beta strandi66 – 716
    Helixi74 – 763
    Helixi82 – 9615
    Beta strandi103 – 1097
    Helixi119 – 1268
    Helixi134 – 15724
    Beta strandi158 – 1603
    Beta strandi162 – 1665
    Beta strandi168 – 1714
    Helixi173 – 1786
    Beta strandi181 – 1877
    Beta strandi191 – 1933
    Helixi196 – 1994
    Helixi207 – 2104
    Helixi211 – 2133
    Helixi218 – 22710
    Beta strandi230 – 2323
    Helixi233 – 2386
    Beta strandi241 – 2488
    Helixi249 – 26517
    Helixi268 – 28316
    Helixi286 – 30015
    Helixi304 – 31411
    Helixi319 – 3213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DCIX-ray1.50A/B/C54-327[»]
    ProteinModelPortaliQ62651.
    SMRiQ62651. Positions 54-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62651.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi325 – 3273Microbody targeting signalSequence Analysis

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00720000108577.
    HOGENOMiHOG000027939.
    HOVERGENiHBG005556.
    InParanoidiQ62651.
    KOiK12663.
    OMAiSWVKDVC.
    OrthoDBiEOG7JHM64.
    PhylomeDBiQ62651.
    TreeFamiTF314317.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q62651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS    50
    DHNYESIQVT SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD 100
    CRAVVVSGAG KMFTSGIDLM DMASDILQPP GDDVARIAWY LRDLISRYQK 150
    TFTVIEKCPK PVIAAIHGGC IGGGVDLISA CDIRYCTQDA FFQVKEVDVG 200
    LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG LVSRVFPDKD 250
    VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM 300
    LQTQDIIKSV QAAMEKKDSK SITFSKL 327
    Length:327
    Mass (Da):36,172
    Last modified:July 15, 1999 - v2
    Checksum:i6FAE35D7D5F66BC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti164 – 1641A → T in AAA82008. (PubMed:7558027)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08976 mRNA. Translation: AAA82008.1.
    BC062226 mRNA. Translation: AAH62226.1.
    PIRiA57626.
    RefSeqiNP_072116.1. NM_022594.1.
    UniGeneiRn.6148.

    Genome annotation databases

    EnsembliENSRNOT00000027537; ENSRNOP00000027537; ENSRNOG00000020308.
    GeneIDi64526.
    KEGGirno:64526.
    UCSCiRGD:69353. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08976 mRNA. Translation: AAA82008.1 .
    BC062226 mRNA. Translation: AAH62226.1 .
    PIRi A57626.
    RefSeqi NP_072116.1. NM_022594.1.
    UniGenei Rn.6148.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DCI X-ray 1.50 A/B/C 54-327 [» ]
    ProteinModelPortali Q62651.
    SMRi Q62651. Positions 54-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q62651. 1 interaction.
    MINTi MINT-4597589.
    STRINGi 10116.ENSRNOP00000027537.

    Proteomic databases

    PaxDbi Q62651.
    PRIDEi Q62651.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000027537 ; ENSRNOP00000027537 ; ENSRNOG00000020308 .
    GeneIDi 64526.
    KEGGi rno:64526.
    UCSCi RGD:69353. rat.

    Organism-specific databases

    CTDi 1891.
    RGDi 69353. Ech1.

    Phylogenomic databases

    eggNOGi COG1024.
    GeneTreei ENSGT00720000108577.
    HOGENOMi HOG000027939.
    HOVERGENi HBG005556.
    InParanoidi Q62651.
    KOi K12663.
    OMAi SWVKDVC.
    OrthoDBi EOG7JHM64.
    PhylomeDBi Q62651.
    TreeFami TF314317.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Miscellaneous databases

    EvolutionaryTracei Q62651.
    NextBioi 613350.
    PROi Q62651.

    Gene expression databases

    Genevestigatori Q62651.

    Family and domain databases

    Gene3Di 1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view ]
    Pfami PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 1 hit.
    PROSITEi PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiECH1_RAT
    AccessioniPrimary (citable) accession number: Q62651
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3