Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q05871 (ECI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from direct assay PubMed 9813046Ref.1. Source: SGD

   Cellular_componentperoxisome

Inferred from direct assay PubMed 9813046Ref.1. Source: SGD

   Molecular_functiondodecenoyl-CoA delta-isomerase activity

Inferred from direct assay PubMed 9813046Ref.1. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2802803,2-trans-enoyl-CoA isomerase
PRO_0000109263

Regions

Region68 – 725Substrate binding
Motif278 – 2803Microbody targeting signal Potential

Sites

Binding site1261Substrate; via amide nitrogen
Site1581Important for catalytic activity

Experimental info

Mutagenesis1581E → A: Loss of activity. Ref.7

Secondary structure

.............................................. 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05871 [UniParc].

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

FASTA28031,698
        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

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
PIRS50369.
RefSeqNP_013386.1. NM_001182171.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNOX-ray2.50A1-280[»]
1HNUX-ray2.15A1-280[»]
1K39X-ray3.29A/B/C1-280[»]
1PJHX-ray2.10A/B/C1-280[»]
ProteinModelPortalQ05871.
SMRQ05871. Positions 4-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31549. 11 interactions.
DIPDIP-1692N.
IntActQ05871. 4 interactions.
MINTMINT-386405.
STRING4932.YLR284C.

Proteomic databases

MaxQBQ05871.
PaxDbQ05871.
PeptideAtlasQ05871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR284C; YLR284C; YLR284C.
GeneID850990.
KEGGsce:YLR284C.

Organism-specific databases

CYGDYLR284c.
SGDS000004274. ECI1.

Phylogenomic databases

eggNOGCOG1024.
GeneTreeENSGT00670000097595.
HOGENOMHOG000027948.
OMALGTHLNQ.
OrthoDBEOG70PC7K.

Enzyme and pathway databases

BioCycMetaCyc:YLR284C-MONOMER.
YEAST:YLR284C-MONOMER.
UniPathwayUPA00659.

Gene expression databases

GenevestigatorQ05871.

Family and domain databases

Gene3D3.90.226.10. 1 hit.
InterProIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF52096. SSF52096. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ05871.
NextBio967513.

Entry information

Entry nameECI1_YEAST
AccessionPrimary (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: June 11, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways