3,2-trans-enoyl-CoA isomerase - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot Q05871 (ECI1_YEAST)

Last modified November 3, 2009. Version 64. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    3,2-trans-enoyl-CoA isomerase
    EC=5.3.3.8
Alternative name(s):
    Dodecenoyl-CoA isomerase
    Delta(3),Delta(2)-enoyl-CoA isomerase
      Short name=D3,D2-enoyl-CoA isomerase

Gene names

Name:	ECI1
Ordered Locus Names:	YLR284C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.3 Ref.4 Ref.6 Ref.7
Subcellular location	Peroxisome. Note: This location is DCI1 dependent. Ref.1 Ref.3 Ref.5
Induction	By oleate. Ref.1
Sequence similarities	Belongs to the enoyl-CoA hydratase/isomerase family.

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Ontologies

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

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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

Substrate binding

Motif

278 – 280

Microbody targeting signal Potential

Sites

Binding site

126

Substrate; via amide nitrogen

Site

158

Important for catalytic activity

Experimental info

Mutagenesis

158

E → A: Loss of activity. Ref.6

Secondary structure

280

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q05871-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CDB72D157ABB845C
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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

« Hide

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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: 9837886] [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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 10381339] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DCI1.
[4]	"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: 10944342] [Abstract] Cited for: CRYSTALLIZATION, SUBUNIT.
[5]	"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: 11302517] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN.
[6]	"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: 11399063] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH OCTANOYL COENZYME A, MUTAGENESIS OF GLU-158, SUBUNIT.
[7]	"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: 14741345] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

PIR

S50369.

RefSeq

NP_013386.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1692N.

IntAct

Q05871. 11 interactions.

STRING

Q05871.

Proteomic databases

PeptideAtlas

Q05871.

Genome annotation databases

Ensembl

YLR284C; YLR284C; YLR284C; Saccharomyces cerevisiae. [Genome view]

GeneID

850990.

GenomeReviews

Gene locus YLR284C in contig Y13138_GR.

KEGG

sce:YLR284C.

NMPDR

fig|4932.3.peg.4401.

Organism-specific databases

CYGD

YLR284c.

SGD

S000004274. ECI1.

Phylogenomic databases

HOGENOM

Q05871.

OMA

DSTEGVQ.

Enzyme and pathway databases

BRENDA

5.3.3.8. 250.

Gene expression databases

ArrayExpress

Q05871.

Genevestigator

Q05871.

GermOnline

YLR284C. Saccharomyces cerevisiae.

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. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

967513.

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Entry information

Entry name

ECI1_YEAST

Accession

Primary (citable) accession number: Q05871

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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