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Q05871

- ECI1_YEAST

UniProt

Q05871 - ECI1_YEAST

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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: 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. dodecenoyl-CoA delta-isomerase activity Source: SGD

GO - Biological processi

  1. 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.
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: Chromosome XII

Organism-specific databases

CYGDiYLR284c.
SGDiS000004274. ECI1.

Subcellular locationi

Peroxisome 3 Publications
Note: This location is DCI1 dependent.

GO - Cellular componenti

  1. 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

Gene expression databases

GenevestigatoriQ05871.

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.
STRINGi4932.YLR284C.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF090442 Genomic DNA. Translation: AAC83700.1 .
U17243 Genomic DNA. Translation: AAB67329.1 .
BK006945 Genomic DNA. Translation: DAA09594.1 .
PIRi S50369.
RefSeqi NP_013386.1. NM_001182171.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q05871.
SMRi Q05871. Positions 4-274.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31549. 11 interactions.
DIPi DIP-1692N.
IntActi Q05871. 4 interactions.
MINTi MINT-386405.
STRINGi 4932.YLR284C.

Proteomic databases

MaxQBi Q05871.
PaxDbi Q05871.
PeptideAtlasi Q05871.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR284C ; YLR284C ; YLR284C .
GeneIDi 850990.
KEGGi sce:YLR284C.

Organism-specific databases

CYGDi YLR284c.
SGDi S000004274. ECI1.

Phylogenomic databases

eggNOGi COG1024.
GeneTreei ENSGT00760000119100.
HOGENOMi HOG000027948.
InParanoidi Q05871.
OMAi LGTHLNQ.
OrthoDBi EOG70PC7K.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:YLR284C-MONOMER.
YEAST:YLR284C-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q05871.
NextBioi 967513.

Gene expression databases

Genevestigatori Q05871.

Family and domain databases

Gene3Di 3.90.226.10. 1 hit.
InterProi IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
[Graphical view ]
Pfami PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF52096. SSF52096. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 104 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