Q62651 (ECH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
EC=5.3.3.-

Gene names

Name:

Ech1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	327 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	Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homohexamer. Ref.5
Subcellular location	Mitochondrion. Peroxisome.
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion Peroxisome
Domain	Transit peptide Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Isomerase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay Ref.4. Source: UniProtKB peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

33

Mitochondrion Potential

Chain

34 – 327

294

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

PRO_0000007419

Regions

Motif

325 – 327

3

Microbody targeting signal Potential

Sites

Binding site

173

1

Substrate; via amide nitrogen By similarity

Site

196

1

Important for catalytic activity Probable

Site

204

1

Important for catalytic activity Potential

Amino acid modifications

Modified residue

94

1

N6-acetyllysine By similarity

Modified residue

326

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

164

1

A → T in AAA82008. Ref.1

Secondary structure

1

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327

Helix Strand Turn

Details...

Beta strand

55 – 63

9

Beta strand

66 – 71

6

Helix

74 – 76

3

Helix

82 – 96

15

Beta strand

103 – 109

7

Helix

119 – 126

8

Helix

134 – 157

24

Beta strand

158 – 160

3

Beta strand

162 – 166

5

Beta strand

168 – 171

4

Helix

173 – 178

6

Beta strand

181 – 187

7

Beta strand

191 – 193

3

Helix

196 – 199

4

Helix

207 – 210

4

Helix

211 – 213

3

Helix

218 – 227

10

Beta strand

230 – 232

3

Helix

233 – 238

6

Beta strand

241 – 248

8

Helix

249 – 265

17

Helix

268 – 283

16

Helix

286 – 300

15

Helix

304 – 314

11

Helix

319 – 321

3

Sequences

	Sequence		Length	Mass (Da)
	Q62651 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 6FAE35D7D5F66BC2	FASTA	327	36,172
	10 20 30 40 50 60 MATAMTVSSK LLGLLMQQLR GTRQLYFNVS LRSLSSSAQE ASKRIPEEVS DHNYESIQVT 70 80 90 100 110 120 SAQKHVLHVQ LNRPEKRNAM NRAFWRELVE CFQKISKDSD CRAVVVSGAG KMFTSGIDLM 130 140 150 160 170 180 DMASDILQPP GDDVARIAWY LRDLISRYQK TFTVIEKCPK PVIAAIHGGC IGGGVDLISA 190 200 210 220 230 240 CDIRYCTQDA FFQVKEVDVG LAADVGTLQR LPKVIGNRSL VNELTFTARK MMADEALDSG 250 260 270 280 290 300 LVSRVFPDKD VMLNAAFALA ADISSKSPVA VQGSKINLIY SRDHSVDESL DYMATWNMSM 310 320 LQTQDIIKSV QAAMEKKDSK SITFSKL

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U08976 mRNA. Translation: AAA82008.1.
BC062226 mRNA. Translation: AAH62226.1.

IPI

IPI00326561.

PIR

A57626.

RefSeq

NP_072116.1. NM_022594.1.

UniGene

Rn.6148.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DCI	X-ray	1.50	A/B/C	54-327	[»]

ProteinModelPortal

Q62651.

SMR

Q62651. Positions 54-327.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4597589.

STRING

10116.ENSRNOP00000027537.

Proteomic databases

PaxDb

Q62651.

PRIDE

Q62651.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000027537; ENSRNOP00000027537; ENSRNOG00000020308.

GeneID

64526.

KEGG

rno:64526.

UCSC

RGD:69353. rat.

Organism-specific databases

CTD

1891.

RGD

69353. Ech1.

Phylogenomic databases

eggNOG

COG1024.

GeneTree

ENSGT00700000104254.

HOGENOM

HOG000027939.

HOVERGEN

HBG005556.

InParanoid

Q62651.

KO

K12663.

OMA

EIDMGMA.

OrthoDB

EOG4VQ9PW.

Enzyme and pathway databases

UniPathway

UPA00659.

Gene expression databases

Genevestigator

Q62651.

GermOnline

ENSRNOG00000020308. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.12.10. 1 hit.

InterPro

IPR014748. Crontonase_C.
IPR001753. Crotonase_core_superfam.
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

EvolutionaryTrace

Q62651.

NextBio

613350.

Entry information

Entry name

ECH1_RAT

Accession

Primary (citable) accession number: Q62651

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1999
Last modified:	April 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program