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Protein

Enolase

Gene

eno

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Mg2+Curated

Enzyme 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

Kineticsi

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

    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 1 (gapA)
    2. Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
    4. Enolase (eno)
    5. Pyruvate kinase (pyk)
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551SubstrateUniRule annotation
    Binding sitei164 – 1641SubstrateUniRule annotation
    Active sitei205 – 2051Proton donorUniRule annotation
    Metal bindingi242 – 2421MagnesiumCurated
    Metal bindingi287 – 2871MagnesiumUniRule annotation
    Binding sitei287 – 2871SubstrateUniRule annotation
    Metal bindingi314 – 3141MagnesiumUniRule annotation
    Binding sitei314 – 3141SubstrateUniRule annotation
    Active sitei339 – 3391Proton acceptorUniRule annotation
    Binding sitei339 – 3391Substrate (covalent); in inhibited form
    Binding sitei390 – 3901SubstrateUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis, Sporulation

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU33900-MONOMER.
    BRENDAi4.2.1.11. 658.
    SABIO-RKP37869.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    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
    Gene namesi
    Name:enoUniRule annotation
    Ordered Locus Names:BSU33900
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 430429EnolasePRO_0000133841Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei141 – 1411Phosphothreonine1 Publication
    Modified residuei259 – 2591Phosphoserine1 Publication
    Modified residuei281 – 2811Phosphotyrosine1 Publication
    Modified residuei325 – 3251Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated during sporulation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP37869.
    PRIDEiP37869.

    PTM databases

    iPTMnetiP37869.

    Interactioni

    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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rnyO317742EBI-6415666,EBI-6415578

    Protein-protein interaction databases

    IntActiP37869. 2 interactions.
    MINTiMINT-8364947.
    STRINGi224308.Bsubs1_010100018386.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1311Combined sources
    Beta strandi19 – 279Combined sources
    Beta strandi32 – 365Combined sources
    Helixi59 – 613Combined sources
    Helixi65 – 739Combined sources
    Helixi75 – 795Combined sources
    Helixi87 – 9812Combined sources
    Turni104 – 1063Combined sources
    Helixi108 – 12619Combined sources
    Helixi130 – 1356Combined sources
    Beta strandi147 – 1515Combined sources
    Helixi153 – 1553Combined sources
    Beta strandi157 – 1593Combined sources
    Beta strandi162 – 1687Combined sources
    Helixi175 – 19521Combined sources
    Helixi215 – 22915Combined sources
    Turni234 – 2363Combined sources
    Beta strandi237 – 2426Combined sources
    Helixi245 – 2473Combined sources
    Turni251 – 2544Combined sources
    Beta strandi255 – 2584Combined sources
    Turni259 – 2624Combined sources
    Beta strandi263 – 2653Combined sources
    Helixi267 – 28014Combined sources
    Beta strandi283 – 2886Combined sources
    Helixi295 – 30511Combined sources
    Turni306 – 3083Combined sources
    Beta strandi309 – 3146Combined sources
    Turni315 – 3195Combined sources
    Helixi321 – 3299Combined sources
    Beta strandi334 – 3385Combined sources
    Helixi340 – 3434Combined sources
    Helixi346 – 35813Combined sources
    Beta strandi362 – 3665Combined sources
    Helixi376 – 3838Combined sources
    Beta strandi388 – 3903Combined sources
    Helixi397 – 41317Combined sources
    Helixi414 – 4163Combined sources
    Helixi421 – 4244Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A3RX-ray2.20A/B/C/D1-430[»]
    ProteinModelPortaliP37869.
    SMRiP37869. Positions 4-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni366 – 3694Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the enolase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C70. Bacteria.
    COG0148. LUCA.
    HOGENOMiHOG000072174.
    InParanoidiP37869.
    KOiK01689.
    OMAiEFMIIPV.
    PhylomeDBiP37869.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPiMF_00318. Enolase. 1 hit.
    InterProiIPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N-like.
    [Graphical view]
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiPF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SMARTiSM01192. Enolase_C. 1 hit.
    SM01193. Enolase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR01060. eno. 1 hit.
    PROSITEiPS00164. ENOLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:iC82B60F49D11AE68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451E → Q in AAA21681 (PubMed:8021172).Curated

    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.

    Genome annotation databases

    EnsemblBacteriaiCAB15395; CAB15395; BSU33900.
    GeneIDi938641.
    KEGGibsu:BSU33900.
    PATRICi18978780. VBIBacSub10457_3553.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A3RX-ray2.20A/B/C/D1-430[»]
    ProteinModelPortaliP37869.
    SMRiP37869. Positions 4-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP37869. 2 interactions.
    MINTiMINT-8364947.
    STRINGi224308.Bsubs1_010100018386.

    PTM databases

    iPTMnetiP37869.

    Proteomic databases

    PaxDbiP37869.
    PRIDEiP37869.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB15395; CAB15395; BSU33900.
    GeneIDi938641.
    KEGGibsu:BSU33900.
    PATRICi18978780. VBIBacSub10457_3553.

    Phylogenomic databases

    eggNOGiENOG4105C70. Bacteria.
    COG0148. LUCA.
    HOGENOMiHOG000072174.
    InParanoidiP37869.
    KOiK01689.
    OMAiEFMIIPV.
    PhylomeDBiP37869.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00187.
    BioCyciBSUB:BSU33900-MONOMER.
    BRENDAi4.2.1.11. 658.
    SABIO-RKP37869.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPiMF_00318. Enolase. 1 hit.
    InterProiIPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N-like.
    [Graphical view]
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiPF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SMARTiSM01192. Enolase_C. 1 hit.
    SM01193. Enolase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR01060. eno. 1 hit.
    PROSITEiPS00164. ENOLASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiENO_BACSU
    AccessioniPrimary (citable) accession number: P37869
    Secondary accession number(s): O32249
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.