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Protein

Enolase

Gene

eno

Organism
Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637)
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 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=136 µM for 2-phosphoglycerate (at 25 degrees Celsius and pH 8)1 Publication
  2. KM=674 µM for phosphoenolpyruvate (at 25 degrees Celsius and pH 8)1 Publication

    pH dependencei

    Optimum pH is 7.8-8.1.1 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. no protein annotated in this organism
    2. Phosphoglycerate kinase (pgk)
    3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
    4. Enolase (eno)
    5. Pyruvate kinase (DvMF_0965)
    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 bindingi285MagnesiumUniRule annotation1
    Binding sitei285SubstrateUniRule annotation1
    Metal bindingi312MagnesiumUniRule annotation1
    Binding sitei312SubstrateUniRule annotation1
    Active sitei337Proton acceptorUniRule annotation1
    Binding sitei337Substrate (covalent); in inhibited formUniRule annotation1
    Binding sitei388SubstrateUniRule 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:DvMF_1810
    OrganismiDesulfovibrio vulgaris (strain Miyazaki F / DSM 19637)
    Taxonomic identifieri883 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
    Proteomesi
    • UP000001361 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_00001338811 – 434EnolaseAdd BLAST434

    Proteomic databases

    PRIDEiO32513.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Protein-protein interaction databases

    STRINGi883.DvMF_1810.

    Structurei

    3D structure databases

    ProteinModelPortaliO32513.
    SMRiO32513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni364 – 367Substrate bindingUniRule annotation4

    Sequence similaritiesi

    Belongs to the enolase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C70. Bacteria.
    COG0148. LUCA.
    HOGENOMiHOG000072174.
    KOiK01689.
    OMAiEFMIIPV.
    OrthoDBiPOG091H02DK.

    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.

    O32513-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTIVSVWAR EILDSRGNPT VEVEVSLESG HTGRAAVPSG ASTGSREALE
    60 70 80 90 100
    MRDGDKGRYK GKGVEKAVDN VMGEIAEAIV GLDSLRQVQV DNTLLDLDGT
    110 120 130 140 150
    DNKSRLGANA MLGVSLATAR AASSFLGLPL YQYLGGVNAK VLPVPLMNII
    160 170 180 190 200
    NGGAHAPNNL DIQEFMIMPI GAATFRDALR MGAETFHTLK ALLAADGHVT
    210 220 230 240 250
    SVGDEGGFAP NLKNHDEAFR YIMKAIEEAG YIPGAEIALA IDAAASEFHK
    260 270 280 290 300
    DGKYVLAGEG KNLSNSEMVE WLGEFTTRYP LISIEDGLAE ADWDGWRELT
    310 320 330 340 350
    YKLGDTIQLV GDDIFVTNPD ILAEGIDEGV ANSILIKLNQ IGTLTETLDT
    360 370 380 390 400
    IEMAKQAAYT TVISHRSGET EDHFISDLAV GLNAGQIKTG SLCRSDRLAK
    410 420 430
    YNQLLRIEED LDDTGIYFGP MMSSHFGFEE EGEE
    Length:434
    Mass (Da):46,689
    Last modified:February 21, 2001 - v2
    Checksum:iF4C0AB4AE4AEBC33
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti34R → G in BAA21475 (Ref. 3) Curated1
    Sequence conflicti83D → N in BAA21475 (Ref. 3) Curated1
    Sequence conflicti113G → A in BAA21475 (Ref. 3) Curated1
    Sequence conflicti118 – 120TAR → HRA in BAA21475 (Ref. 3) Curated3

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB046715 Genomic DNA. Translation: BAB07786.1.
    CP001197 Genomic DNA. Translation: ACL08754.1.
    AB005550 Genomic DNA. Translation: BAA21475.1.
    RefSeqiWP_012612929.1. NC_011769.1.

    Genome annotation databases

    EnsemblBacteriaiACL08754; ACL08754; DvMF_1810.
    KEGGidvm:DvMF_1810.

    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.

    Entry informationi

    Entry nameiENO_DESVM
    AccessioniPrimary (citable) accession number: O32513
    Secondary accession number(s): B8DMB0, Q9KVZ6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 21, 2001
    Last modified: June 7, 2017
    This is version 116 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