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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei126Substrate; via amide nitrogenCombined sources1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei158Proton donor/acceptor1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • dodecenoyl-CoA delta-isomerase activity Source: SGD

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YLR284C-MONOMER
YEAST:YLR284C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.3.3.8 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-390247 Beta-oxidation of very long chain fatty acids
R-SCE-70895 Branched-chain amino acid catabolism
R-SCE-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-SCE-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-SCE-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-SCE-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-SCE-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
R-SCE-9033241 Peroxisomal protein import

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00659

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ECI1
Ordered Locus Names:YLR284C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004274 ECI1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi158E → A: Loss of activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001092631 – 2803,2-trans-enoyl-CoA isomeraseAdd BLAST280

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q05871

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q05871

PRoteomics IDEntifications database

More...
PRIDEi
Q05871

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By oleate.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31549, 22 interactors

Database of interacting proteins

More...
DIPi
DIP-1692N

Protein interaction database and analysis system

More...
IntActi
Q05871, 4 interactors

Molecular INTeraction database

More...
MINTi
Q05871

STRING: functional protein association networks

More...
STRINGi
4932.YLR284C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1280
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q05871

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q05871

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q05871

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni68 – 72Substrate bindingCombined sources1 Publication5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi278 – 280Microbody targeting signalSequence analysis3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000173631

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000027948

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05871

KEGG Orthology (KO)

More...
KOi
K13239

Identification of Orthologs from Complete Genome Data

More...
OMAi
AHADFIY

Database of Orthologous Groups

More...
OrthoDBi
EOG092C431D

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR001753 Enoyl-CoA_hydra/iso

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00378 ECH_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52096 SSF52096, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCDB72D157ABB845C
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF090442 Genomic DNA Translation: AAC83700.1
U17243 Genomic DNA Translation: AAB67329.1
BK006945 Genomic DNA Translation: DAA09594.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50369

NCBI Reference Sequences

More...
RefSeqi
NP_013386.1, NM_001182171.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR284C_mRNA; YLR284C_mRNA; YLR284C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850990

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR284C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HNOX-ray2.50A1-280[»]
1HNUX-ray2.15A1-280[»]
1K39X-ray3.29A/B/C1-280[»]
1PJHX-ray2.10A/B/C1-280[»]
4ZDBX-ray2.14A/B/C1-280[»]
4ZDCX-ray2.13A/B/C1-280[»]
4ZDDX-ray3.00A1-280[»]
4ZDEX-ray2.10A/B/C1-280[»]
4ZDFX-ray1.81A/B1-268[»]
ProteinModelPortaliQ05871
SMRiQ05871
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31549, 22 interactors
DIPiDIP-1692N
IntActiQ05871, 4 interactors
MINTiQ05871
STRINGi4932.YLR284C

Proteomic databases

MaxQBiQ05871
PaxDbiQ05871
PRIDEiQ05871

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR284C_mRNA; YLR284C_mRNA; YLR284C
GeneIDi850990
KEGGisce:YLR284C

Organism-specific databases

SGDiS000004274 ECI1

Phylogenomic databases

GeneTreeiENSGT00940000173631
HOGENOMiHOG000027948
InParanoidiQ05871
KOiK13239
OMAiAHADFIY
OrthoDBiEOG092C431D

Enzyme and pathway databases

UniPathwayi
UPA00659

BioCyciMetaCyc:YLR284C-MONOMER
YEAST:YLR284C-MONOMER
BRENDAi5.3.3.8 984
ReactomeiR-SCE-390247 Beta-oxidation of very long chain fatty acids
R-SCE-70895 Branched-chain amino acid catabolism
R-SCE-77310 Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA
R-SCE-77346 Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA
R-SCE-77348 Beta oxidation of octanoyl-CoA to hexanoyl-CoA
R-SCE-77350 Beta oxidation of hexanoyl-CoA to butanoyl-CoA
R-SCE-77352 Beta oxidation of butanoyl-CoA to acetyl-CoA
R-SCE-9033241 Peroxisomal protein import

Miscellaneous databases

EvolutionaryTraceiQ05871

Protein Ontology

More...
PROi
PR:Q05871

Family and domain databases

InterProiView protein in InterPro
IPR029045 ClpP/crotonase-like_dom_sf
IPR001753 Enoyl-CoA_hydra/iso
PfamiView protein in Pfam
PF00378 ECH_1, 1 hit
SUPFAMiSSF52096 SSF52096, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiECI1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q05871
Secondary accession number(s): D6VYS8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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