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Protein

Enolase

Gene

eno

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 annotation1 Publication

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

Enzyme regulationi

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (By similarity). Inhibited by fluoride and phosphate.UniRule annotation1 Publication

Kineticsi

  1. KM=0.07 mM for 2-phospho-D-glycerate (at 75 degrees Celsius)1 Publication
  2. KM=0.03 mM for magnesium (at 75 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius.1 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 (gap)
    2. Bifunctional PGK/TIM (pgk/tpi), Multifunctional fusion protein (pgk)
    3. Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM)
    4. Enolase (eno), Enolase (eno)
    5. Pyruvate kinase (pyk), Pyruvate kinase (Tmari_0206)
    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
    Binding sitei156SubstrateUniRule annotation1
    Binding sitei165SubstrateUniRule annotation1
    Active sitei206Proton donorUniRule annotation1
    Metal bindingi243MagnesiumUniRule annotation1
    Metal bindingi286MagnesiumUniRule annotation1
    Binding sitei286SubstrateUniRule annotation1
    Metal bindingi313MagnesiumUniRule annotation1
    Binding sitei313SubstrateUniRule annotation1
    Active sitei338Proton acceptorUniRule annotation1
    Binding sitei338Substrate (covalent); in inhibited formUniRule annotation1
    Binding sitei389SubstrateUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    Biological processGlycolysis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    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:TM_0877
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    Proteomesi
    • UP000008183 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation
    • Secreted UniRule annotation
    • Cell surface UniRule annotation

    • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001339941 – 429EnolaseAdd BLAST429

    Proteomic databases

    PRIDEiP42848.

    Interactioni

    Subunit structurei

    Homooctamer. Forms a ring-shaped particle.1 Publication

    Protein-protein interaction databases

    STRINGi243274.TM0877.

    Structurei

    3D structure databases

    ProteinModelPortaliP42848.
    SMRiP42848.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni365 – 368Substrate bindingUniRule annotation4

    Sequence similaritiesi

    Belongs to the enolase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C70. Bacteria.
    COG0148. LUCA.
    InParanoidiP42848.
    KOiK01689.
    OMAiEFMIIPV.

    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.
    IPR034390. Enolase-like_superfamily.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N-like.
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiView protein in Pfam
    PF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SFLDiSFLDG00178. enolase. 1 hit.
    SFLDS00001. 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.

    Sequencei

    Sequence statusi: Complete.

    P42848-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MYVEIVDVRA REVLDSRGNP TVEAEVVLED GTMGRAIVPS GASTGKFEAL
    60 70 80 90 100
    EIRDKDKKRY LGKGVLKAVE NVNETIAPAL IGMNAFDQPL VDKTLIELDG
    110 120 130 140 150
    TENKSKLGAN AILAVSMAVA RAAANYLGLP LYKYLGGVNA KVLPVPLMNV
    160 170 180 190 200
    INGGQHADNN LDLQEFMIVP AGFDSFREAL RAGAEIFHTL KKILHEAGHV
    210 220 230 240 250
    TAVGDEGGFA PNLSSNEEAI KVLIEAIEKA GYKPGEEVFI ALDCAASSFY
    260 270 280 290 300
    DEEKGVYYVD GEEKSSEVLM GYYEELVAKY PIISIEDPFA EEDWDAFVEF
    310 320 330 340 350
    TKRVGNKVQI VGDDLYVTNV KRLSKGIELK ATNSILIKLN QIGTVTETLD
    360 370 380 390 400
    AVEMAQKNNM TAIISHRSGE SEDTFIADLA VATNAGFIKT GSLSRSERIA
    410 420
    KYNQLLRIEE ELGKVAEFRG LKSFYSIKR
    Length:429
    Mass (Da):46,870
    Last modified:May 30, 2000 - v2
    Checksum:i35D65899D3AE56CB
    GO

    Sequence cautioni

    The sequence AAD35958 differs from that shown. Reason: Erroneous initiation.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35958.1. Different initiation.
    PIRiG72323.
    RefSeqiNP_228685.1. NC_000853.1.
    WP_010865214.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35958; AAD35958; TM_0877.
    GeneIDi898551.
    KEGGitma:TM0877.
    tmi:THEMA_00250.
    tmw:THMA_0899.
    PATRICifig|243274.18.peg.50.

    Similar proteinsi

    Entry informationi

    Entry nameiENO_THEMA
    AccessioniPrimary (citable) accession number: P42848
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: May 30, 2000
    Last modified: August 30, 2017
    This is version 135 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families