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Protein

Enoyl-CoA hydratase, mitochondrial

Gene

Echs1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi4.2.1.17. 5301.
ReactomeiREACT_275090. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_289411. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_292108. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_299914. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_350057. Beta oxidation of butanoyl-CoA to acetyl-CoA.
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 Componenti: 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
Complete GO annotation...

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 – 429Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 526Combined sources
Helixi55 – 573Combined sources
Helixi63 – 7816Combined sources
Beta strandi84 – 885Combined sources
Beta strandi91 – 955Combined sources
Helixi100 – 1034Combined sources
Helixi108 – 1136Combined sources
Helixi119 – 1257Combined sources
Beta strandi130 – 1345Combined sources
Beta strandi136 – 1394Combined sources
Helixi141 – 1488Combined sources
Beta strandi149 – 1557Combined sources
Beta strandi159 – 1613Combined sources
Helixi163 – 1675Combined sources
Turni175 – 1773Combined sources
Helixi178 – 1836Combined sources
Helixi185 – 19410Combined sources
Beta strandi197 – 1993Combined sources
Helixi200 – 2056Combined sources
Beta strandi210 – 2134Combined sources
Turni215 – 2173Combined sources
Helixi218 – 23114Combined sources
Helixi234 – 24512Combined sources
Helixi246 – 2483Combined sources
Helixi252 – 26514Combined sources
Helixi266 – 2683Combined sources
Helixi270 – 28011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP14604.
KOiK07511.
OMAiMMADFII.
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

        10         20         30         40         50
MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI
60 70 80 90 100
QLNRPKALNA LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI
110 120 130 140 150
KEMQNRTFQD CYSGKFLSHW DHITRIKKPV IAAVNGYALG GGCELAMMCD
160 170 180 190 200
IIYAGEKAQF GQPEILLGTI PGAGGTQRLT RAVGKSLAME MVLTGDRISA
210 220 230 240 250
QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA KESVNAAFEM
260 270 280 290
TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH
Length:290
Mass (Da):31,516
Last modified:April 1, 1990 - v1
Checksum:i1E528590961D0CC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiP14604. 1 interaction.
STRINGi10116.ENSRNOP00000025446.

Chemistry

ChEMBLiCHEMBL3153.

PTM databases

PhosphoSiteiP14604.

Proteomic databases

PaxDbiP14604.
PRIDEiP14604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1892.
RGDi69330. Echs1.

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027939.
HOVERGENiHBG010157.
InParanoidiP14604.
KOiK07511.
OMAiMMADFII.
OrthoDBiEOG7N63NC.
PhylomeDBiP14604.
TreeFamiTF314497.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi4.2.1.17. 5301.
ReactomeiREACT_275090. Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
REACT_289411. Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
REACT_292108. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_299914. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_350057. Beta oxidation of butanoyl-CoA to acetyl-CoA.

Miscellaneous databases

EvolutionaryTraceiP14604.
NextBioi620493.
PROiP14604.

Gene expression databases

GenevestigatoriP14604.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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(2003) [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(1994) [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(1995) [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(1997) [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(2001) [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(2001) [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: April 1, 2015
This is version 136 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.