P23965 (ECI1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enoyl-CoA delta isomerase 1, mitochondrial
EC=5.3.3.8

Alternative name(s):
3,2-trans-enoyl-CoA isomerase
Delta(3),Delta(2)-enoyl-CoA isomerase
Short name=D3,D2-enoyl-CoA isomerase
Dodecenoyl-CoA isomerase

Gene names

Name:	Eci1
Synonyms:	Dci

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	289 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	Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.
Catalytic activity	(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homotrimer. Ref.4
Subcellular location	Mitochondrion matrix.
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	Isomerase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Traceable author statement Ref.1. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dodecenoyl-CoA delta-isomerase activity Inferred from direct assay Ref.1. Source: RGD identical protein binding Inferred from direct assay Ref.4. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

28

Mitochondrion

Chain

29 – 289

261

Enoyl-CoA delta isomerase 1, mitochondrial

PRO_0000007422

Regions

Region

93 – 97

5

Substrate binding By similarity

Sites

Binding site

140

1

Substrate; via amide nitrogen By similarity

Binding site

164

1

Substrate By similarity

Site

165

1

Important for catalytic activity

Amino acid modifications

Modified residue

76

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

165

1

E → Q: Loss of activity. Ref.3

Sequence conflict

1 – 8

8

MALAAARR → AGCCAC AA sequence Ref.2

Sequence conflict

260

1

D → N in AAA41073. Ref.2

Secondary structure

1

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289

Helix Strand Turn

Details...

Beta strand

32 – 37

6

Beta strand

44 – 49

6

Turn

52 – 55

4

Helix

59 – 74

16

Beta strand

80 – 87

8

Beta strand

89 – 91

3

Helix

97 – 100

4

Helix

105 – 123

19

Beta strand

126 – 133

8

Beta strand

135 – 138

4

Helix

139 – 147

9

Beta strand

148 – 154

7

Helix

165 – 168

4

Helix

174 – 184

11

Helix

186 – 195

10

Helix

201 – 206

6

Beta strand

209 – 214

6

Helix

216 – 218

3

Helix

219 – 230

12

Helix

235 – 254

20

Helix

257 – 269

13

Helix

271 – 282

12

Sequences

	Sequence		Length	Mass (Da)
	P23965 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 79D2CED09DD8FDC6	FASTA	289	32,254
	10 20 30 40 50 60 MALAAARRVL LQAGSRLGRR GAVDGARRFS NKRVLVEKEG EAGIAVMKFK NPPVNSLSLE 70 80 90 100 110 120 FLTEFVISLE KLENDKSIRG VILTSERPGI FSAGLDLMEM YGRNPAHYAE YWKAVQELWL 130 140 150 160 170 180 RLYLSNLTLI SAINGASPAG GCLMALTCDY RIMADNSKYT IGLNESLLGI VAPFWLKDNY 190 200 210 220 230 240 VNTIGHRAAE RALQLGTLFP PAEALKVGLV DEVVPEDQVH SKARSVMAKW FTIPDHSRQL 250 260 270 280 TKSMMRKATA DNLIKQREAD IQNFTSFISR DSIQKSLHVY LEKLKQKKG

References

[1]	"Mitochondrial 3-2trans-Enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid beta-oxidation." Mueller-Newen G., Stoffel W. Biol. Chem. Hoppe-Seyler 372:613-624(1991) [PubMed: 1958319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[2]	"Amino acid sequence similarities of the mitochondrial short chain delta 3, delta 2-enoyl-CoA isomerase and peroxisomal multifunctional delta 3, delta 2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase enzyme in rat liver. The proposed occurrence of isomerization and hydration in the same catalytic domain of the multifunctional enzyme." Palosaari P.M., Vihinen M., Maentsaelae P.I., Alexson S.E., Pihlajaniemi T., Hiltunen J.K. J. Biol. Chem. 266:10750-10753(1991) [PubMed: 2040594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[3]	"Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family." Mueller-Newen G., Stoffel W. Biochemistry 32:11405-11412(1993) [PubMed: 8218206] [Abstract] Cited for: MUTAGENESIS OF GLU-165.
[4]	"Domain swapping in the low-similarity isomerase/hydratase superfamily: the crystal structure of rat mitochondrial delta3, delta2-enoyl-CoA isomerase." Hubbard P.A., Yu W., Schulz H., Kim J.-J.P. Protein Sci. 14:1545-1555(2005) [PubMed: 15883186] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 29-289, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61184 mRNA. Translation: CAA43488.1.
M61112 mRNA. Translation: AAA41073.1.

IPI

IPI00215574.

PIR

S17161.

UniGene

Rn.80835.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XX4	X-ray	2.20	A	29-289	[»]

ProteinModelPortal

P23965.

SMR

P23965. Positions 29-285.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23965. 1 interaction.

STRING

P23965.

PTM databases

PhosphoSite

P23965.

Proteomic databases

PRIDE

P23965.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

UCSC

NM_017306. rat.

Organism-specific databases

RGD

61892. Eci1.

Phylogenomic databases

eggNOG

roNOG07688.

HOVERGEN

HBG001112.

InParanoid

P23965.

OrthoDB

EOG4R23VQ.

Enzyme and pathway databases

BRENDA

5.3.3.8. 5301.

Gene expression databases

ArrayExpress

P23965.

Genevestigator

P23965.

GermOnline

ENSRNOG00000008843. 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...

Entry information

Entry name

ECI1_RAT

Accession

Primary (citable) accession number: P23965

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	September 21, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program