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P14604

- ECHM_RAT

UniProt

P14604 - ECHM_RAT

Protein

Enoyl-CoA hydratase, mitochondrial

Gene

Echs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.

    Catalytic activityi

    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei141 – 1411Substrate; via amide nitrogen
    Sitei164 – 1641Important for catalytic activity

    GO - Molecular functioni

    1. enoyl-CoA hydratase activity Source: RGD

    GO - Biological processi

    1. fatty acid beta-oxidation Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Enoyl-CoA hydratase, mitochondrial (EC:4.2.1.17)
    Alternative name(s):
    Enoyl-CoA hydratase 1
    Short-chain enoyl-CoA hydratase
    Short name:
    SCEH
    Gene namesi
    Name:Echs1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi69330. Echs1.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi144 – 1441E → D: Reduces activity 50-fold. 1 Publication
    Mutagenesisi144 – 1441E → Q: Reduces activity 3300-fold. 1 Publication
    Mutagenesisi164 – 1641E → D: Reduces activity 1250-fold. 1 Publication
    Mutagenesisi164 – 1641E → Q: Reduces activity 330000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929Mitochondrion1 PublicationAdd
    BLAST
    Chaini30 – 290261Enoyl-CoA hydratase, mitochondrialPRO_0000007414Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011N6-acetyllysine; alternateBy similarity
    Modified residuei101 – 1011N6-succinyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
    Modified residuei204 – 2041N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP14604.
    PRIDEiP14604.

    PTM databases

    PhosphoSiteiP14604.

    Expressioni

    Tissue specificityi

    Detected in liver (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP14604.

    Interactioni

    Subunit structurei

    Homohexamer; dimer of trimers.4 Publications

    Protein-protein interaction databases

    IntActiP14604. 1 interaction.
    STRINGi10116.ENSRNOP00000025446.

    Structurei

    Secondary structure

    1
    290
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 429
    Helixi43 – 453
    Beta strandi47 – 526
    Helixi55 – 573
    Helixi63 – 7816
    Beta strandi84 – 885
    Beta strandi91 – 955
    Helixi100 – 1034
    Helixi108 – 1136
    Helixi119 – 1257
    Beta strandi130 – 1345
    Beta strandi136 – 1394
    Helixi141 – 1488
    Beta strandi149 – 1557
    Beta strandi159 – 1613
    Helixi163 – 1675
    Turni175 – 1773
    Helixi178 – 1836
    Helixi185 – 19410
    Beta strandi197 – 1993
    Helixi200 – 2056
    Beta strandi210 – 2134
    Turni215 – 2173
    Helixi218 – 23114
    Helixi234 – 24512
    Helixi246 – 2483
    Helixi252 – 26514
    Helixi266 – 2683
    Helixi270 – 28011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DUBX-ray2.50A/B/C/D/E/F30-290[»]
    1EY3X-ray2.30A/B/C/D/E/F33-290[»]
    1MJ3X-ray2.10A/B/C/D/E/F31-290[»]
    2DUBX-ray2.40A/B/C/D/E/F30-290[»]
    ProteinModelPortaliP14604.
    SMRiP14604. Positions 31-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14604.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1014Substrate binding

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1024.
    GeneTreeiENSGT00720000108577.
    HOGENOMiHOG000027939.
    HOVERGENiHBG010157.
    InParanoidiP14604.
    KOiK07511.
    OMAiHWDQLTR.
    OrthoDBiEOG7N63NC.
    PhylomeDBiP14604.
    TreeFamiTF314497.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    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.

    P14604-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI    50
    QLNRPKALNA LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI 100
    KEMQNRTFQD CYSGKFLSHW DHITRIKKPV IAAVNGYALG GGCELAMMCD 150
    IIYAGEKAQF GQPEILLGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA 200
    QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA KESVNAAFEM 250
    TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH 290
    Length:290
    Mass (Da):31,516
    Last modified:April 1, 1990 - v1
    Checksum:i1E528590961D0CC0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15958 mRNA. Translation: CAA34080.1.
    BC064655 mRNA. Translation: AAH64655.1.
    PIRiS06477.
    RefSeqiNP_511178.1. NM_078623.2.
    XP_003748934.1. XM_003748886.2.
    UniGeneiRn.6847.

    Genome annotation databases

    EnsembliENSRNOT00000025446; ENSRNOP00000025446; ENSRNOG00000018522.
    ENSRNOT00000071574; ENSRNOP00000066388; ENSRNOG00000047565.
    GeneIDi100911186.
    140547.
    KEGGirno:100911186.
    rno:140547.
    UCSCiRGD:69330. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15958 mRNA. Translation: CAA34080.1 .
    BC064655 mRNA. Translation: AAH64655.1 .
    PIRi S06477.
    RefSeqi NP_511178.1. NM_078623.2.
    XP_003748934.1. XM_003748886.2.
    UniGenei Rn.6847.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUB X-ray 2.50 A/B/C/D/E/F 30-290 [» ]
    1EY3 X-ray 2.30 A/B/C/D/E/F 33-290 [» ]
    1MJ3 X-ray 2.10 A/B/C/D/E/F 31-290 [» ]
    2DUB X-ray 2.40 A/B/C/D/E/F 30-290 [» ]
    ProteinModelPortali P14604.
    SMRi P14604. Positions 31-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14604. 1 interaction.
    STRINGi 10116.ENSRNOP00000025446.

    Chemistry

    ChEMBLi CHEMBL3153.

    PTM databases

    PhosphoSitei P14604.

    Proteomic databases

    PaxDbi P14604.
    PRIDEi P14604.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000025446 ; ENSRNOP00000025446 ; ENSRNOG00000018522 .
    ENSRNOT00000071574 ; ENSRNOP00000066388 ; ENSRNOG00000047565 .
    GeneIDi 100911186.
    140547.
    KEGGi rno:100911186.
    rno:140547.
    UCSCi RGD:69330. rat.

    Organism-specific databases

    CTDi 1892.
    RGDi 69330. Echs1.

    Phylogenomic databases

    eggNOGi COG1024.
    GeneTreei ENSGT00720000108577.
    HOGENOMi HOG000027939.
    HOVERGENi HBG010157.
    InParanoidi P14604.
    KOi K07511.
    OMAi HWDQLTR.
    OrthoDBi EOG7N63NC.
    PhylomeDBi P14604.
    TreeFami TF314497.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .

    Miscellaneous databases

    EvolutionaryTracei P14604.
    NextBioi 620493.
    PROi P14604.

    Gene expression databases

    Genevestigatori P14604.

    Family and domain databases

    Gene3Di 3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    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. "Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system."
      Minami-Ishii N., Taketani S., Osumi T., Hashimoto T.
      Eur. J. Biochem. 185:73-78(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-39 AND 80-94.
      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: Prostate.
    3. "Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue."
      Mueller-Newen G., Janssen U., Stoffel W.
      Eur. J. Biochem. 228:68-73(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-164.
    4. "Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5-A resolution: a spiral fold defines the CoA-binding pocket."
      Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., Wierenga R.K.
      EMBO J. 15:5135-5145(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH OCTANOYL COENZYME A, SUBUNIT.
      Tissue: Liver.
    5. "The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule."
      Engel C.K., Kiema T.R., Hiltunen J.K., Wierenga R.K.
      J. Mol. Biol. 275:847-859(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ACETOACETYL COENZYME A, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion."
      Bahnson B.J., Anderson V.E., Petsko G.A.
      Biochemistry 41:2621-2629(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-290 IN COMPLEX WITH 4-N,N-DIMETHYLAMINOCINNAMOYL COENZYME A, ENZYME MECHANISM, SUBUNIT.
    7. "Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers."
      Bell A.F., Feng Y., Hofstein H.A., Parikh S., Wu J., Rudolph M.J., Kisker C., Whitty A., Tonge P.J.
      Chem. Biol. 9:1247-1255(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-290 IN COMPLEX WITH HEXADIENOL COENZYME A, MUTAGENESIS OF GLU-144.

    Entry informationi

    Entry nameiECHM_RAT
    AccessioniPrimary (citable) accession number: P14604
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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