Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase

Gene

eno

Organism
Escherichia coli (strain K12)
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

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.UniRule annotation3 Publications

<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+UniRule annotation2 PublicationsNote: Mg2+ is required for catalysis and for stabilizing the dimer.UniRule annotation2 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Inhibited by fluoride ion.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 8.1.1 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.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase II (pykA), Pyruvate kinase I (pykF)
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 sitei159SubstrateUniRule annotation1
Binding sitei168SubstrateUniRule annotation1
<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 sitei209Proton donorUniRule annotation1
<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 bindingi246Magnesium1
Metal bindingi290Magnesium1
Binding sitei290SubstrateUniRule annotation1
Metal bindingi317Magnesium1
Binding sitei317SubstrateUniRule annotation1
Active sitei342Proton acceptorUniRule annotation1
Binding sitei342Substrate (covalent); in inhibited form1
Binding sitei393SubstrateUniRule annotation1

<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

  • identical protein binding Source: IntAct
  • magnesium ion binding Source: EcoliWiki
  • phosphopyruvate hydratase activity Source: CAFA

GO - Biological processi

  • glycolytic process Source: EcoliWiki

<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
EcoCyc:ENOLASE-MONOMER
MetaCyc:ENOLASE-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.11 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A6P9

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

More...
UniPathwayi
UPA00109;UER00187

<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:
EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseUniRule annotation
2-phosphoglycerate dehydrataseUniRule annotation
<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:enoUniRule annotation
Ordered Locus Names:b2779, JW2750
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10258 eno

<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

  • cytoskeleton
  • Secreted
  • Cell surface
  • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the cell surface.

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

<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>Mutagenesisi168E → Q: 5% activity; not secreted. 1 Publication1
Mutagenesisi209E → Q: 1% activity; not secreted. 1 Publication1
Mutagenesisi342K → A, Q or R: 1% activity; not secreted. 1 Publication1
Mutagenesisi342K → E: 94% activity; not secreted. 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 <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 methionineiRemoved3 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_00001338822 – 432EnolaseAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei257N6-acetyllysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on serine residue(s).1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A6P9

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

More...
PaxDbi
P0A6P9

PRoteomics IDEntifications database

More...
PRIDEi
P0A6P9

2D gel databases

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

More...
SWISS-2DPAGEi
P0A6P9

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0A6P9

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0A6P9

<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

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with the C-terminal region of the endoribonuclease RNase E. Homodimer.UniRule annotation7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei120Interaction with RNase E1
Sitei376Interaction with RNase E1
Sitei408Interaction with RNase E1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262297, 354 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-403 Degradosome

Database of interacting proteins

More...
DIPi
DIP-31847N

Protein interaction database and analysis system

More...
IntActi
P0A6P9, 38 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_2946

<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

1432
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
P0A6P9

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

More...
SMRi
P0A6P9

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
P0A6P9

<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>Regioni5 – 34Interaction with RNase EAdd BLAST30
Regioni369 – 372Substrate bindingUniRule annotation4

<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.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C70 Bacteria
COG0148 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000072173

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6P9

KEGG Orthology (KO)

More...
KOi
K01689

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6P9

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.

P0A6P9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE
60 70 80 90 100
LRDGDKSRFL GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT
110 120 130 140 150
ENKSKFGANA ILAVSLANAK AAAAAKGMPL YEHIAELNGT PGKYSMPVPM
160 170 180 190 200
MNIINGGEHA DNNVDIQEFM IQPVGAKTVK EAIRMGSEVF HHLAKVLKAK
210 220 230 240 250
GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD ITLAMDCAAS
260 270 280 290 300
EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG
310 320 330 340 350
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT
360 370 380 390 400
ETLAAIKMAK DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS
410 420 430
DRVAKYNQLI RIEEALGEKA PYNGRKEIKG QA
Length:432
Mass (Da):45,655
Last modified:January 23, 2007 - v2
<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:i0569036E87471B91
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 conflicti102N → K in CAA57795 (Ref. 1) Curated1
Sequence conflicti102N → K in AAA24486 (Ref. 1) Curated1
Sequence conflicti220A → D in CAA57795 (Ref. 1) Curated1
Sequence conflicti339I → Y in CAA57795 (Ref. 1) Curated1
Sequence conflicti421 – 432PYNGR…IKGQA → RTTVVKRSKARHKTDFI in CAA57795 (Ref. 1) CuratedAdd BLAST12

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
X82400 Genomic DNA Translation: CAA57795.1
U29580 Genomic DNA Translation: AAA69289.1
U00096 Genomic DNA Translation: AAC75821.1
AP009048 Genomic DNA Translation: BAE76853.1
M12843 mRNA Translation: AAA24486.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65059 NOEC

NCBI Reference Sequences

More...
RefSeqi
NP_417259.1, NC_000913.3
WP_000036723.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75821; AAC75821; b2779
BAE76853; BAE76853; BAE76853

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945032

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2750
eco:b2779

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3956

<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
X82400 Genomic DNA Translation: CAA57795.1
U29580 Genomic DNA Translation: AAA69289.1
U00096 Genomic DNA Translation: AAC75821.1
AP009048 Genomic DNA Translation: BAE76853.1
M12843 mRNA Translation: AAA24486.1
PIRiG65059 NOEC
RefSeqiNP_417259.1, NC_000913.3
WP_000036723.1, NZ_LN832404.1

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
1E9IX-ray2.48A/B/C/D2-432[»]
2FYMX-ray1.60A/C/D/F2-432[»]
3H8AX-ray1.90A/B/C/D1-432[»]
5OHGX-ray2.00A/B/H/I1-432[»]
ProteinModelPortaliP0A6P9
SMRiP0A6P9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262297, 354 interactors
ComplexPortaliCPX-403 Degradosome
DIPiDIP-31847N
IntActiP0A6P9, 38 interactors
STRINGi316385.ECDH10B_2946

PTM databases

CarbonylDBiP0A6P9
iPTMnetiP0A6P9

2D gel databases

SWISS-2DPAGEiP0A6P9

Proteomic databases

EPDiP0A6P9
PaxDbiP0A6P9
PRIDEiP0A6P9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75821; AAC75821; b2779
BAE76853; BAE76853; BAE76853
GeneIDi945032
KEGGiecj:JW2750
eco:b2779
PATRICifig|1411691.4.peg.3956

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0254
EcoGeneiEG10258 eno

Phylogenomic databases

eggNOGiENOG4105C70 Bacteria
COG0148 LUCA
HOGENOMiHOG000072173
InParanoidiP0A6P9
KOiK01689
PhylomeDBiP0A6P9

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00187

BioCyciEcoCyc:ENOLASE-MONOMER
MetaCyc:ENOLASE-MONOMER
BRENDAi4.2.1.11 2026
SABIO-RKiP0A6P9

Miscellaneous databases

EvolutionaryTraceiP0A6P9

Protein Ontology

More...
PROi
PR:P0A6P9

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 nameiENO_ECOLI
<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: P0A6P9
Secondary accession number(s): P08324, Q2MA53
<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: August 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 129 of the entry and version 2 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 programProkaryotic 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again