Reviewed, UniProtKB/Swiss-Prot P14604 (ECHM_RAT)

Names and origin

Protein names

Recommended name:
    Enoyl-CoA hydratase, mitochondrial
    EC=4.2.1.17
Alternative name(s):
    Short chain enoyl-CoA hydratase
      Short name=SCEH
    Enoyl-CoA hydratase 1

Gene names

Name:

Echs1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	290 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Ref.1 Traceable author statement. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enoyl-CoA hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

29

Mitochondrion Ref.1

Chain

30 – 290

261

Enoyl-CoA hydratase, mitochondrial

PRO_0000007414

Regions

Region

98 – 101

4

Substrate binding

Sites

Binding site

141

1

Substrate; via amide nitrogen

Site

164

1

Important for catalysis

Amino acid modifications

Modified residue

101

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

144

1

E → D: Reduces activity 50-fold. Ref.7

Mutagenesis

144

1

E → Q: Reduces activity 3300-fold. Ref.7

Mutagenesis

164

1

E → D: Reduces activity 1250-fold. Ref.3

Mutagenesis

164

1

E → Q: Reduces activity 330000-fold. Ref.3

Secondary structure

1

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290

Helix Strand Turn

Details...

Beta strand

35 – 40

6

Beta strand

42 – 45

4

Beta strand

47 – 52

6

Helix

55 – 57

3

Helix

63 – 78

16

Beta strand

84 – 88

5

Beta strand

91 – 95

5

Helix

100 – 103

4

Helix

108 – 111

4

Helix

122 – 125

4

Beta strand

130 – 134

5

Beta strand

136 – 139

4

Helix

141 – 148

8

Beta strand

149 – 155

7

Beta strand

159 – 161

3

Helix

163 – 167

5

Turn

175 – 177

3

Helix

178 – 183

6

Helix

185 – 194

10

Helix

200 – 205

6

Beta strand

210 – 213

4

Turn

215 – 217

3

Helix

218 – 230

13

Helix

234 – 245

12

Helix

246 – 248

3

Helix

252 – 265

14

Helix

266 – 268

3

Helix

270 – 280

11

Sequences

	Sequence		Length	Mass (Da)
	P14604-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 1E528590961D0CC0	FASTA	290	31,516
	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

References

	« Hide 'large scale' referencesShow '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: 2806264] [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: 15489334] [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: 7883013] [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: 8895557] [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: 9480773] [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: 11851409] [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: 12445775] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-290 IN COMPLEX WITH HEXADIENOL COENZYME A, MUTAGENESIS OF GLU-144.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X15958 mRNA. Translation: CAA34080.1.
BC064655 mRNA. Translation: AAH64655.1.

IPI

IPI00207217.

PIR

S06477.

RefSeq

NP_511178.1.

UniGene

Rn.6847

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

PTM databases

PhosphoSite

P14604.

2-D gel databases

Rat-heart-2DPAGE

P14604.

Proteomic databases

PRIDE

P14604.

Genome annotation databases

Ensembl

ENSRNOG00000018522. Rattus norvegicus. [Contig view]

GeneID

140547.

KEGG

rno:140547.

NMPDR

fig|10116.3.peg.3204.

Organism-specific databases

RGD

69330. Echs1.

Phylogenomic databases

HOVERGEN

P14604.

OMA

P14604. GVEYERR.

Enzyme and pathway databases

BRENDA

4.2.1.17. 248.

Gene expression databases

ArrayExpress

P14604.

GermOnline

ENSRNOG00000018522. Rattus norvegicus.

Family and domain databases

InterPro

IPR001753. Crotonase_core.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

620493.

Entry information

Entry name

ECHM_RAT

Accession

Primary (citable) accession number: P14604

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)