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P14604 (ECHM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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:
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 names
Name:Echs1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homohexamer; dimer of trimers. Ref.4 Ref.5 Ref.6

Subcellular location

Mitochondrion matrix Ref.5.

Tissue specificity

Detected in liver (at protein level). Ref.5

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Ref.1
Chain30 – 290261Enoyl-CoA hydratase, mitochondrial
PRO_0000007414

Regions

Region98 – 1014Substrate binding

Sites

Binding site1411Substrate; via amide nitrogen
Site1641Important for catalytic activity

Amino acid modifications

Modified residue1011N6-acetyllysine; alternate By similarity
Modified residue1011N6-succinyllysine; alternate By similarity
Modified residue1151N6-acetyllysine; alternate By similarity
Modified residue1151N6-succinyllysine; alternate By similarity
Modified residue2041N6-succinyllysine By similarity
Modified residue2111N6-acetyllysine By similarity

Experimental info

Mutagenesis1441E → D: Reduces activity 50-fold. Ref.7
Mutagenesis1441E → Q: Reduces activity 3300-fold. Ref.7
Mutagenesis1641E → D: Reduces activity 1250-fold. Ref.3
Mutagenesis1641E → Q: Reduces activity 330000-fold. Ref.3

Secondary structure

.................................................... 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14604 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1E528590961D0CC0

FASTA29031,516
        10         20         30         40         50         60 
MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA 

        70         80         90        100        110        120 
LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI KEMQNRTFQD CYSGKFLSHW 

       130        140        150        160        170        180 
DHITRIKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT 

       190        200        210        220        230        240 
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA 

       250        260        270        280        290 
KESVNAAFEM TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15958 mRNA. Translation: CAA34080.1.
BC064655 mRNA. Translation: AAH64655.1.
PIRS06477.
RefSeqNP_511178.1. NM_078623.2.
XP_003748934.1. XM_003748886.2.
UniGeneRn.6847.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP14604.
SMRP14604. Positions 31-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP14604. 1 interaction.
STRING10116.ENSRNOP00000025446.

Chemistry

ChEMBLCHEMBL3153.

PTM databases

PhosphoSiteP14604.

Proteomic databases

PaxDbP14604.
PRIDEP14604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025446; ENSRNOP00000025446; ENSRNOG00000018522.
ENSRNOT00000071574; ENSRNOP00000066388; ENSRNOG00000047565.
GeneID100911186.
140547.
KEGGrno:100911186.
rno:140547.
UCSCRGD:69330. rat.

Organism-specific databases

CTD1892.
RGD69330. Echs1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00720000108577.
HOGENOMHOG000027939.
HOVERGENHBG010157.
InParanoidP14604.
KOK07511.
OMANVGFIQL.
OrthoDBEOG7N63NC.
PhylomeDBP14604.
TreeFamTF314497.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

GenevestigatorP14604.

Family and domain databases

InterProIPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14604.
NextBio620493.
PROP14604.

Entry information

Entry nameECHM_RAT
AccessionPrimary (citable) accession number: P14604
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 128 of the entry and version 1 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