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Protein

Enolase

Gene

eno

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: Annotation score: 4 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 annotation

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.UniRule annotation

Kineticsi

  1. KM=0.08 mM 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 (gap)
    2. Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
    4. Enolase (eno)
    5. Pyruvate kinase (ZMO0152)
    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 sitei155SubstrateUniRule annotation1
    Binding sitei164SubstrateUniRule annotation1
    Active sitei205Proton donorUniRule annotation1
    Metal bindingi242MagnesiumUniRule annotation1
    Metal bindingi287MagnesiumUniRule annotation1
    Binding sitei287SubstrateUniRule annotation1
    Metal bindingi314MagnesiumUniRule annotation1
    Binding sitei314SubstrateUniRule annotation1
    Active sitei339Proton acceptorUniRule annotation1
    Binding sitei339Substrate (covalent); in inhibited formUniRule annotation1
    Binding sitei390SubstrateUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    Biological processGlycolysis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    SABIO-RKiP33675.
    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:ZMO1608
    OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
    Taxonomic identifieri264203 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
    Proteomesi
    • UP000001173 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_00001340181 – 429EnolaseAdd BLAST429

    Proteomic databases

    PRIDEiP33675.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP33675.
    SMRiP33675.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni366 – 369Substrate bindingUniRule annotation4

    Sequence similaritiesi

    Belongs to the enolase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000072174.
    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.

    P33675-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTAIVSIHGR QVVDSRGNPT VEVDVTLEDG SFGRAAVPSG ASTGVHEAVE
    60 70 80 90 100
    LRDGDKTRWG GKGVTKAVHA VNNEIANAII GLEAEDQELI DQTMIKLDGT
    110 120 130 140 150
    PNKGKFGANA ILGVSLAVAK AAAEARGLPL YRYVGGTAAH VLPVPMMNIV
    160 170 180 190 200
    NGGMHADNPI DFQEFMIAPV GASSINEAVR IGTEVFHTLK KELSAKGMNT
    210 220 230 240 250
    NVGDEGGFAP SLDSASSALD FIVDSISKAG YKPGEDVFIA LDAASSEFYN
    260 270 280 290 300
    KDQNIYDLKG EGRKLTSAQL VDYYVELCGK YPIYSIEDGL AEDDFEGWKI
    310 320 330 340 350
    LTEKLGDKVQ LVGDDLFVTN VKRLSDGIER GIANSLLVKF NQIGSLSETL
    360 370 380 390 400
    AAVNMANDAS YTAVMSHRSG ETEDTTIADL AVATNCGQIK TGSLCRSERI
    410 420
    AKYNQLMRIE EELGSVAKYA GRSVLRKAK
    Length:429
    Mass (Da):45,743
    Last modified:February 15, 2005 - v2
    Checksum:i557E9E258FD9F93E
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti186F → S in AAC70360 (Ref. 2) Curated1
    Sequence conflicti288Missing (PubMed:1400207).Curated1
    Sequence conflicti288Missing (Ref. 2) Curated1
    Sequence conflicti297G → F (PubMed:1400207).Curated1
    Sequence conflicti297G → F (Ref. 2) Curated1
    Sequence conflicti363A → P (PubMed:1400207).Curated1
    Sequence conflicti363A → P (Ref. 2) Curated1
    Sequence conflicti370G → V in AAA27686 (PubMed:1400207).Curated1
    Sequence conflicti371 – 429ETEDT…LRKAK → GNRRHHDC (Ref. 2) CuratedAdd BLAST59

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M99380 Genomic DNA. Translation: AAA27686.1.
    AF086791 Genomic DNA. Translation: AAC70360.1.
    AE008692 Genomic DNA. Translation: AAV90232.1.
    PIRiA45732.
    T33721.
    RefSeqiWP_011241362.1. NC_006526.2.

    Genome annotation databases

    EnsemblBacteriaiAAV90232; AAV90232; ZMO1608.
    GeneIDi33073272.
    KEGGizmo:ZMO1608.

    Similar proteinsi

    Entry informationi

    Entry nameiENO_ZYMMO
    AccessioniPrimary (citable) accession number: P33675
    Secondary accession number(s): O69010, Q5NM28
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 15, 2005
    Last modified: September 27, 2017
    This is version 124 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, Reference proteome

    Documents

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