Q05871 (ECI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3,2-trans-enoyl-CoA isomerase
EC=5.3.3.8

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

Gene names

Name:	ECI1
Ordered Locus Names:	YLR284C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for the beta oxidation of unsaturated fatty acids. Ref.1
Catalytic activity	(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Homohexamer, dimer of trimers. Interacts with DCI1. Ref.4 Ref.5 Ref.7 Ref.8
Subcellular location	Peroxisome. Note: This location is DCI1 dependent. Ref.1 Ref.4 Ref.6
Induction	By oleate. Ref.1
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Inferred from direct assay PubMed 9813046Ref.1. Source: SGD
Cellular_component	peroxisome Inferred from direct assay PubMed 9813046Ref.1. Source: SGD
Molecular_function	dodecenoyl-CoA delta-isomerase activity Inferred from mutant phenotype PubMed 9813046Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 280

280

3,2-trans-enoyl-CoA isomerase

PRO_0000109263

Regions

Region

68 – 72

5

Substrate binding

Motif

278 – 280

3

Microbody targeting signal Potential

Sites

Binding site

126

1

Substrate; via amide nitrogen

Site

158

1

Important for catalytic activity

Experimental info

Mutagenesis

158

1

E → A: Loss of activity. Ref.7

Secondary structure

1

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280

Helix Strand Turn

Details...

Beta strand

11 – 16

6

Beta strand

19 – 24

6

Helix

27 – 29

3

Helix

35 – 50

16

Beta strand

56 – 60

5

Beta strand

65 – 67

3

Helix

72 – 76

5

Turn

77 – 81

5

Helix

89 – 96

8

Helix

98 – 110

13

Beta strand

113 – 119

7

Helix

125 – 133

9

Beta strand

134 – 141

8

Beta strand

145 – 147

3

Helix

150 – 153

4

Helix

161 – 169

9

Helix

171 – 179

9

Helix

186 – 191

6

Beta strand

196 – 198

3

Helix

206 – 221

16

Beta strand

222 – 224

3

Helix

226 – 237

12

Turn

238 – 240

3

Helix

241 – 261

21

Helix

263 – 268

6

Sequences

	Sequence		Length	Mass (Da)
	Q05871 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: CDB72D157ABB845C	FASTA	280	31,698
	10 20 30 40 50 60 MSQEIRQNEK ISYRIEGPFF IIHLMNPDNL NALEGEDYIY LGELLELADR NRDVYFTIIQ 70 80 90 100 110 120 SSGRFFSSGA DFKGIAKAQG DDTNKYPSET SKWVSNFVAR NVYVTDAFIK HSKVLICCLN 130 140 150 160 170 180 GPAIGLSAAL VALCDIVYSI NDKVYLLYPF ANLGLITEGG TTVSLPLKFG TNTTYECLMF 190 200 210 220 230 240 NKPFKYDIMC ENGFISKNFN MPSSNAEAFN AKVLEELREK VKGLYLPSCL GMKKLLKSNH 250 260 270 280 IDAFNKANSV EVNESLKYWV DGEPLKRFRQ LGSKQRKHRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase." Geisbrecht B.V., Zhu D., Schulz K., Nau K., Morrell J.C., Geraghty M.T., Schulz H., Erdmann R., Gould S.J. J. Biol. Chem. 273:33184-33191(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Preliminary characterization of Yor180Cp: identification of a novel peroxisomal protein of Saccharomyces cerevisiae involved in fatty acid metabolism." Geisbrecht B.V., Schulz K., Nau K., Geraghty M.T., Schulz H., Erdmann R., Gould S.J. Biochem. Biophys. Res. Commun. 260:28-34(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCI1.
[5]	"Crystallization and X-ray diffraction analysis of peroxisomal Delta3-Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae." Mursula A.M., van Aalten D.M., Modis Y., Hiltunen J.K., Wierenga R.K. Acta Crystallogr. D 56:1020-1023(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION, SUBUNIT.
[6]	"Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a partner, Dci1p." Yang X., Purdue P.E., Lazarow P.B. Eur. J. Cell Biol. 80:126-138(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN.
[7]	"The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase." Mursula A.M., van Aalten D.M., Hiltunen J.K., Wierenga R.K. J. Mol. Biol. 309:845-853(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH OCTANOYL COENZYME A, MUTAGENESIS OF GLU-158, SUBUNIT.
[8]	"Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily." Mursula A.M., Hiltunen J.K., Wierenga R.K. FEBS Lett. 557:81-87(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF090442 Genomic DNA. Translation: AAC83700.1.
U17243 Genomic DNA. Translation: AAB67329.1.
BK006945 Genomic DNA. Translation: DAA09594.1.

PIR

S50369.

RefSeq

NP_013386.1. NM_001182171.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HNO	X-ray	2.50	A	1-280	[»]
1HNU	X-ray	2.15	A	1-280	[»]
1K39	X-ray	3.29	A/B/C	1-280	[»]
1PJH	X-ray	2.10	A/B/C	1-280	[»]

ProteinModelPortal

Q05871.

SMR

Q05871. Positions 4-274.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1692N.

IntAct

Q05871. 4 interactions.

MINT

MINT-386405.

STRING

4932.YLR284C.

Proteomic databases

PaxDb

Q05871.

PeptideAtlas

Q05871.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR284C; YLR284C; YLR284C.

GeneID

850990.

KEGG

sce:YLR284C.

Organism-specific databases

CYGD

YLR284c.

SGD

S000004274. ECI1.

Phylogenomic databases

eggNOG

COG1024.

GeneTree

ENSGT00670000097595.

HOGENOM

HOG000027948.

OMA

ICCLNGP.

OrthoDB

EOG4NPBCC.

Enzyme and pathway databases

UniPathway

UPA00659.

Gene expression databases

Genevestigator

Q05871.

GermOnline

YLR284C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001753. Crotonase_core_superfam.
[Graphical view]

Pfam

PF00378. ECH. 1 hit.
[Graphical view]

PROSITE

PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q05871.

NextBio

967513.

Entry information

Entry name

ECI1_YEAST

Accession

Primary (citable) accession number: Q05871
Secondary accession number(s): D6VYS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program