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Protein

3,2-trans-enoyl-CoA isomerase

Gene

ECI1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the beta oxidation of unsaturated fatty acids.1 Publication

Catalytic activityi

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

Pathway:ifatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate; via amide nitrogen
Sitei158 – 1581Important for catalytic activity

GO - Molecular functioni

  • dodecenoyl-CoA delta-isomerase activity Source: SGD

GO - Biological processi

  • fatty acid beta-oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:YLR284C-MONOMER.
YEAST:YLR284C-MONOMER.
BRENDAi5.3.3.8. 984.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ECI1
Ordered Locus Names:YLR284C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR284c.
EuPathDBiFungiDB:YLR284C.
SGDiS000004274. ECI1.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581E → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2802803,2-trans-enoyl-CoA isomerasePRO_0000109263Add
BLAST

Proteomic databases

MaxQBiQ05871.
PaxDbiQ05871.
PeptideAtlasiQ05871.

Expressioni

Inductioni

By oleate.1 Publication

Interactioni

Subunit structurei

Homohexamer, dimer of trimers. Interacts with DCI1.4 Publications

Protein-protein interaction databases

BioGridi31549. 11 interactions.
DIPiDIP-1692N.
IntActiQ05871. 4 interactions.
MINTiMINT-386405.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 166Combined sources
Beta strandi19 – 246Combined sources
Helixi27 – 293Combined sources
Helixi35 – 5016Combined sources
Beta strandi56 – 605Combined sources
Beta strandi65 – 673Combined sources
Helixi72 – 765Combined sources
Turni77 – 815Combined sources
Helixi89 – 968Combined sources
Helixi98 – 11013Combined sources
Beta strandi113 – 1197Combined sources
Helixi125 – 1339Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 1534Combined sources
Helixi161 – 1699Combined sources
Helixi171 – 1799Combined sources
Helixi186 – 1916Combined sources
Beta strandi196 – 1983Combined sources
Helixi206 – 22116Combined sources
Beta strandi222 – 2243Combined sources
Helixi226 – 23712Combined sources
Turni238 – 2403Combined sources
Helixi241 – 26121Combined sources
Helixi263 – 2686Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNOX-ray2.50A1-280[»]
1HNUX-ray2.15A1-280[»]
1K39X-ray3.29A/B/C1-280[»]
1PJHX-ray2.10A/B/C1-280[»]
ProteinModelPortaliQ05871.
SMRiQ05871. Positions 4-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05871.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 725Substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi278 – 2803Microbody targeting signalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027948.
InParanoidiQ05871.
KOiK13239.
OMAiLGTHLNQ.
OrthoDBiEOG70PC7K.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQEIRQNEK ISYRIEGPFF IIHLMNPDNL NALEGEDYIY LGELLELADR
60 70 80 90 100
NRDVYFTIIQ SSGRFFSSGA DFKGIAKAQG DDTNKYPSET SKWVSNFVAR
110 120 130 140 150
NVYVTDAFIK HSKVLICCLN GPAIGLSAAL VALCDIVYSI NDKVYLLYPF
160 170 180 190 200
ANLGLITEGG TTVSLPLKFG TNTTYECLMF NKPFKYDIMC ENGFISKNFN
210 220 230 240 250
MPSSNAEAFN AKVLEELREK VKGLYLPSCL GMKKLLKSNH IDAFNKANSV
260 270 280
EVNESLKYWV DGEPLKRFRQ LGSKQRKHRL
Length:280
Mass (Da):31,698
Last modified:November 1, 1996 - v1
Checksum:iCDB72D157ABB845C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090442 Genomic DNA. Translation: AAC83700.1.
U17243 Genomic DNA. Translation: AAB67329.1.
BK006945 Genomic DNA. Translation: DAA09594.1.
PIRiS50369.
RefSeqiNP_013386.1. NM_001182171.1.

Genome annotation databases

EnsemblFungiiYLR284C; YLR284C; YLR284C.
GeneIDi850990.
KEGGisce:YLR284C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090442 Genomic DNA. Translation: AAC83700.1.
U17243 Genomic DNA. Translation: AAB67329.1.
BK006945 Genomic DNA. Translation: DAA09594.1.
PIRiS50369.
RefSeqiNP_013386.1. NM_001182171.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HNOX-ray2.50A1-280[»]
1HNUX-ray2.15A1-280[»]
1K39X-ray3.29A/B/C1-280[»]
1PJHX-ray2.10A/B/C1-280[»]
ProteinModelPortaliQ05871.
SMRiQ05871. Positions 4-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31549. 11 interactions.
DIPiDIP-1692N.
IntActiQ05871. 4 interactions.
MINTiMINT-386405.

Proteomic databases

MaxQBiQ05871.
PaxDbiQ05871.
PeptideAtlasiQ05871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR284C; YLR284C; YLR284C.
GeneIDi850990.
KEGGisce:YLR284C.

Organism-specific databases

CYGDiYLR284c.
EuPathDBiFungiDB:YLR284C.
SGDiS000004274. ECI1.

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00760000119100.
HOGENOMiHOG000027948.
InParanoidiQ05871.
KOiK13239.
OMAiLGTHLNQ.
OrthoDBiEOG70PC7K.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:YLR284C-MONOMER.
YEAST:YLR284C-MONOMER.
BRENDAi5.3.3.8. 984.

Miscellaneous databases

EvolutionaryTraceiQ05871.
NextBioi967513.
PROiQ05871.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  3. 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.

Entry informationi

Entry nameiECI1_YEAST
AccessioniPrimary (citable) accession number: Q05871
Secondary accession number(s): D6VYS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.