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Protein

Enolase 1

Gene

ENO1

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

Miscellaneous

Present with 76700 molecules/cell in log phase SD medium.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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 PublicationNote: Mg2+ is required for catalysis and for stabilizing the dimer.1 Publication

<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: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 1 (TDH1), Glyceraldehyde-3-phosphate dehydrogenase 2 (TDH2), Glyceraldehyde-3-phosphate dehydrogenase 3 (TDH3)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase 2 (GPM2), Phosphoglycerate mutase 3 (GPM3), Phosphoglycerate mutase 1 (GPM1)
  4. Enolase 1 (ENO1), Enolase-related protein 3 (ERR3), Enolase 2 (ENO2), Enolase-related protein 1 (ERR1), Enolase-related protein 2 (ERR2)
  5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (CDC19)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

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 sitei160Substrate2 Publications1
Binding sitei169Substrate2 Publications1
<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 sitei212Proton donorCurated1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi247Magnesium1 Publication1
Metal bindingi296Magnesium1 Publication1
Binding sitei296Substrate2 Publications1
Metal bindingi321Magnesium1 Publication1
Binding sitei321Substrate2 Publications1
Active sitei346Proton acceptor1
Binding sitei397Substrate2 Publications1

<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

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: SGD

GO - Biological processi

  • gluconeogenesis Source: SGD
  • glycolytic process Source: SGD
  • regulation of vacuole fusion, non-autophagic Source: SGD

<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 functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YGR254W-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.11 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-70171 Glycolysis
R-SCE-70263 Gluconeogenesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00924

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

More...
UniPathwayi
UPA00109;UER00187

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
P00924 Curated

MoonProt database of moonlighting proteins

More...
MoonProti
P00924

<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:
Enolase 1 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
<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:ENO1
Synonyms:ENOA, HSP48
Ordered Locus Names:YGR254W
ORF Names:G9160
<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 VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003486 ENO1

<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

Cytoplasm

<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>Mutagenesisi40S → A: Reduces activity by 99.9%. 1
Mutagenesisi160H → A, F or N: Reduces activity by 99%. 2 Publications1
Mutagenesisi169E → Q: Reduces Kcat over 100000-fold. 1
Mutagenesisi208N → A: Reduces activity by 44%. 1 Publication1
Mutagenesisi212E → Q: Reduces Kcat over 100000-fold. 1
Mutagenesisi346K → A: Reduces Kcat over 100000-fold. Abolishes of the proton exchange reaction that initiates the enzymatic reaction. 1 Publication1

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
786 Sac c Enolase

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00001340622 – 437Enolase 1Add BLAST436

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki60Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei119PhosphoserineCombined sources1
Modified residuei138PhosphoserineBy similarity1
Modified residuei188PhosphoserineBy similarity1
Cross-linki243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei313PhosphothreonineBy similarity1
Modified residuei324PhosphothreonineBy similarity1
Cross-linki358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P00924

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

More...
PaxDbi
P00924

PRoteomics IDEntifications database

More...
PRIDEi
P00924

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P00924

2D gel databases

2-DE database at Universidad Complutense de Madrid

More...
COMPLUYEAST-2DPAGEi
P00924

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P00924

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P00924

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P00924

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00924

<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

Homodimer.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33505, 136 interactors

Database of interacting proteins

More...
DIPi
DIP-5561N

Protein interaction database and analysis system

More...
IntActi
P00924, 82 interactors

Molecular INTeraction database

More...
MINTi
P00924

STRING: functional protein association networks

More...
STRINGi
4932.YGR254W

<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

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1EBGX-ray2.10A/B2-437[»]
1EBHX-ray1.90A/B2-437[»]
1ELSX-ray2.40A2-437[»]
1L8PX-ray2.10A/B/C/D2-437[»]
1NELX-ray2.60A2-437[»]
1ONEX-ray1.80A/B2-437[»]
1P43X-ray1.80A/B2-437[»]
1P48X-ray2.00A/B2-437[»]
2AL1X-ray1.50A/B2-437[»]
2AL2X-ray1.85A/B2-437[»]
2ONEX-ray2.00A/B2-437[»]
2XGZX-ray1.80A/B2-437[»]
2XH0X-ray1.70A/B/C/D2-437[»]
2XH2X-ray1.80A/B/C/D2-437[»]
2XH4X-ray1.70A/B/C/D2-437[»]
2XH7X-ray1.80A/B2-437[»]
3ENLX-ray2.25A2-437[»]
4ENLX-ray1.90A2-437[»]
5ENLX-ray2.20A2-437[»]
6ENLX-ray2.20A2-437[»]
7ENLX-ray2.20A2-437[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00924

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

More...
SMRi
P00924

Database of comparative protein structure models

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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
P00924

<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>Regioni373 – 376Substrate binding4

<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

Belongs to the enolase family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155260

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000072174

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00924

KEGG Orthology (KO)

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KOi
K01689

Identification of Orthologs from Complete Genome Data

More...
OMAi
EFMIIPV

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03313 enolase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.120, 1 hit
3.30.390.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00318 Enolase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N

The PANTHER Classification System

More...
PANTHERi
PTHR11902 PTHR11902, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001400 Enolase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00148 ENOLASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51604 SSF51604, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01060 eno, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00164 ENOLASE, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00924-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR
60 70 80 90 100
DGDKSKWMGK GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT
110 120 130 140 150
ANKSKLGANA ILGVSLAASR AAAAEKNVPL YKHLADLSKS KTSPYVLPVP
160 170 180 190 200
FLNVLNGGSH AGGALALQEF MIAPTGAKTF AEALRIGSEV YHNLKSLTKK
210 220 230 240 250
RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG KIKIGLDCAS
260 270 280 290 300
SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI
360 370 380 390 400
GTLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA
410 420 430
PARSERLAKL NQLLRIEEEL GDNAVFAGEN FHHGDKL
Length:437
Mass (Da):46,816
Last modified:October 5, 2010 - v3
<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:i69F45214DBD375BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti242I → V in AAA88712 (PubMed:6256394).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J01322 Genomic DNA Translation: AAA88712.1
X99228 Genomic DNA Translation: CAA67616.1
Z73039 Genomic DNA Translation: CAA97283.1
BK006941 Genomic DNA Translation: DAA08345.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64586 NOBY

NCBI Reference Sequences

More...
RefSeqi
NP_011770.3, NM_001181383.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGR254W_mRNA; YGR254W_mRNA; YGR254W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853169

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGR254W

<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
J01322 Genomic DNA Translation: AAA88712.1
X99228 Genomic DNA Translation: CAA67616.1
Z73039 Genomic DNA Translation: CAA97283.1
BK006941 Genomic DNA Translation: DAA08345.1
PIRiS64586 NOBY
RefSeqiNP_011770.3, NM_001181383.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBGX-ray2.10A/B2-437[»]
1EBHX-ray1.90A/B2-437[»]
1ELSX-ray2.40A2-437[»]
1L8PX-ray2.10A/B/C/D2-437[»]
1NELX-ray2.60A2-437[»]
1ONEX-ray1.80A/B2-437[»]
1P43X-ray1.80A/B2-437[»]
1P48X-ray2.00A/B2-437[»]
2AL1X-ray1.50A/B2-437[»]
2AL2X-ray1.85A/B2-437[»]
2ONEX-ray2.00A/B2-437[»]
2XGZX-ray1.80A/B2-437[»]
2XH0X-ray1.70A/B/C/D2-437[»]
2XH2X-ray1.80A/B/C/D2-437[»]
2XH4X-ray1.70A/B/C/D2-437[»]
2XH7X-ray1.80A/B2-437[»]
3ENLX-ray2.25A2-437[»]
4ENLX-ray1.90A2-437[»]
5ENLX-ray2.20A2-437[»]
6ENLX-ray2.20A2-437[»]
7ENLX-ray2.20A2-437[»]
ProteinModelPortaliP00924
SMRiP00924
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33505, 136 interactors
DIPiDIP-5561N
IntActiP00924, 82 interactors
MINTiP00924
STRINGi4932.YGR254W

Protein family/group databases

Allergomei786 Sac c Enolase
MoonDBiP00924 Curated
MoonProtiP00924

PTM databases

CarbonylDBiP00924
iPTMnetiP00924

2D gel databases

COMPLUYEAST-2DPAGEiP00924
SWISS-2DPAGEiP00924
UCD-2DPAGEiP00924

Proteomic databases

MaxQBiP00924
PaxDbiP00924
PRIDEiP00924
TopDownProteomicsiP00924

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR254W_mRNA; YGR254W_mRNA; YGR254W
GeneIDi853169
KEGGisce:YGR254W

Organism-specific databases

SGDiS000003486 ENO1

Phylogenomic databases

GeneTreeiENSGT00940000155260
HOGENOMiHOG000072174
InParanoidiP00924
KOiK01689
OMAiEFMIIPV

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00187

BioCyciYEAST:YGR254W-MONOMER
BRENDAi4.2.1.11 984
ReactomeiR-SCE-70171 Glycolysis
R-SCE-70263 Gluconeogenesis
SABIO-RKiP00924

Miscellaneous databases

EvolutionaryTraceiP00924

Protein Ontology

More...
PROi
PR:P00924

Family and domain databases

CDDicd03313 enolase, 1 hit
Gene3Di3.20.20.120, 1 hit
3.30.390.10, 1 hit
HAMAPiMF_00318 Enolase, 1 hit
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 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 nameiENO1_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: P00924
Secondary accession number(s): D6VV34, P99013
<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: July 21, 1986
Last sequence update: October 5, 2010
Last modified: January 16, 2019
This is version 211 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

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