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Entry version 172 (02 Jun 2021)
Sequence version 4 (23 Jan 2007)
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Protein

Enolase

Gene

eno

Organism
Bacillus subtilis (strain 168)
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.

UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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-339 of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (PubMed:15003462). Citrate acts as a non-competitive inhibitor for both forward and reverse reactions, probably by chelating Mg2+ (PubMed:22198292).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>Kineticsi

  1. KM=0.44 µM for 2-phospho-D-glycerate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei155SubstrateUniRule annotation1
    Binding sitei164SubstrateUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei205Proton donorUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi242MagnesiumCurated1
    Metal bindingi287MagnesiumUniRule annotation1
    Binding sitei287SubstrateUniRule annotation1
    Metal bindingi314MagnesiumUniRule annotation1
    Binding sitei314SubstrateUniRule annotation1
    Active sitei339Proton acceptorUniRule annotation1
    Binding sitei339Substrate; covalent; in inhibited form1
    Binding sitei390SubstrateUniRule 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

    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 functionLyase
    Biological processGlycolysis, Sporulation
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU33900-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.1.11, 658

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P37869

    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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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:BSU33900
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBacillus subtilis (strain 168)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri224308 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

    <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

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    <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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001338412 – 430EnolaseAdd BLAST429

    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 residuei141Phosphothreonine1 Publication1
    Modified residuei259Phosphoserine1 Publication1
    Modified residuei281Phosphotyrosine1 Publication1
    Modified residuei325Phosphoserine1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 during sporulation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P37869

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

    More...
    PaxDbi
    P37869

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P37869

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P37869

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homooctamer.

    Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear).

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P37869, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P37869

    STRING: functional protein association networks

    More...
    STRINGi
    224308.BSU33900

    <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

    1430
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P37869

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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>Regioni366 – 369Substrate 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
    COG0148, Bacteria

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P37869

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    GPELVGY

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P37869

    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

    Structure-Function Linkage Database

    More...
    SFLDi
    SFLDF00002, enolase, 1 hit

    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
    SSF54826, SSF54826, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P37869-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE
    60 70 80 90 100
    LRDGDKDRYL GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT
    110 120 130 140 150
    ENKGKLGANA ILGVSMACAR AAADFLQIPL YQYLGGFNSK TLPVPMMNIV
    160 170 180 190 200
    NGGEHADNNV DIQEFMIMPV GAPNFREALR MGAQIFHSLK SVLSAKGLNT
    210 220 230 240 250
    AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA MDAASSEFYN
    260 270 280 290 300
    KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL
    310 320 330 340 350
    LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF
    360 370 380 390 400
    DAIEMAKRAG YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV
    410 420 430
    AKYNQLLRIE DQLAETAQYH GINSFYNLNK
    Length:430
    Mass (Da):46,581
    Last modified:January 23, 2007 - v4
    <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:iC82B60F49D11AE68
    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 conflicti45E → Q in AAA21681 (PubMed:8021172).Curated1

    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
    L29475 Genomic DNA Translation: AAA21681.1
    AL009126 Genomic DNA Translation: CAB15395.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    B69620

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_391270.1, NC_000964.3
    WP_003228333.1, NZ_JNCM01000033.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB15395; CAB15395; BSU_33900

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    938641

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU33900

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.179.peg.3675

    <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
    L29475 Genomic DNA Translation: AAA21681.1
    AL009126 Genomic DNA Translation: CAB15395.1
    PIRiB69620
    RefSeqiNP_391270.1, NC_000964.3
    WP_003228333.1, NZ_JNCM01000033.1

    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
    4A3RX-ray2.20A/B/C/D1-430[»]
    SMRiP37869
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP37869, 2 interactors
    MINTiP37869
    STRINGi224308.BSU33900

    PTM databases

    iPTMnetiP37869

    Proteomic databases

    jPOSTiP37869
    PaxDbiP37869
    PRIDEiP37869

    Genome annotation databases

    EnsemblBacteriaiCAB15395; CAB15395; BSU_33900
    GeneIDi938641
    KEGGibsu:BSU33900
    PATRICifig|224308.179.peg.3675

    Phylogenomic databases

    eggNOGiCOG0148, Bacteria
    InParanoidiP37869
    OMAiGPELVGY
    PhylomeDBiP37869

    Enzyme and pathway databases

    UniPathwayiUPA00109;UER00187
    BioCyciBSUB:BSU33900-MONOMER
    BRENDAi4.2.1.11, 658
    SABIO-RKiP37869

    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
    SFLDiSFLDF00002, enolase, 1 hit
    SMARTiView protein in SMART
    SM01192, Enolase_C, 1 hit
    SM01193, Enolase_N, 1 hit
    SUPFAMiSSF51604, SSF51604, 1 hit
    SSF54826, SSF54826, 1 hit
    TIGRFAMsiTIGR01060, eno, 1 hit
    PROSITEiView protein in PROSITE
    PS00164, ENOLASE, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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_BACSU
    <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: P37869
    Secondary accession number(s): O32249
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: June 2, 2021
    This is version 172 of the entry and version 4 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, Direct protein sequencing, 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
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