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Protein

Enolase

Gene

eno

Organism
Streptococcus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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+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

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)
  4. Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (AMD33_04615), Pyruvate kinase (pyk), Pyruvate kinase (ADU38_1005)
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 sitei154 – 1541SubstrateUniRule annotation
Binding sitei163 – 1631SubstrateUniRule annotation
Active sitei204 – 2041Proton donorUniRule annotation
Metal bindingi241 – 2411MagnesiumUniRule annotation
Metal bindingi285 – 2851MagnesiumUniRule annotation
Binding sitei285 – 2851SubstrateUniRule annotation
Metal bindingi312 – 3121MagnesiumUniRule annotation
Binding sitei312 – 3121SubstrateUniRule annotation
Active sitei337 – 3371Proton acceptorUniRule annotation
Binding sitei337 – 3371Substrate (covalent); in inhibited formUniRule annotation
Binding sitei388 – 3881SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, 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
Encoded oniPlasmid pCI65st0 Publication
OrganismiStreptococcus thermophilus
Taxonomic identifieri1308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422EnolasePRO_0000133988Add
BLAST

Proteomic databases

PRIDEiO52191.

Structurei

3D structure databases

ProteinModelPortaliO52191.
SMRiO52191. Positions 4-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3674Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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.

O52191-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTIENIHA REIFDSRGNP TVEVDVRLTD GTLGRAAVPS GASTGDREAV
60 70 80 90 100
ELRDGGARLQ GKGVSKAVAN VNGEIYEALK GQSPFNQAKL DHLMIELDGT
110 120 130 140 150
ENKSCLGANA ILGVSMAIFR AAANSEKIPL YRYFGGVDLE LPQPFFNVIN
160 170 180 190 200
GGVHADSGID VQEFLITPVK RDSFRDGLKK IANIYHTLKK ILSDKGLKTP
210 220 230 240 250
VGDEGGFAPK LGTTENAIAI LYQPIDSAGY FPGEKIAIAI DSSSIEFYDD
260 270 280 290 300
KKKFYRFEGK NLTSKELLTY YDNLVEKYPA LISIEDGFSE HDWEGFAAQT
310 320 330 340 350
KARGQKIQLV GDDIFVTNPT IFKEGIKKNV ANAILIKLNQ IGTVTETIET
360 370 380 390 400
ISLARKAGYK TMISHRSGET VDSYIADFSV AMHAGQIKSG SMARSERVEK
410 420
YNQLLRIEED LGKDVALAQF PG
Length:422
Mass (Da):46,081
Last modified:June 1, 1998 - v1
Checksum:iB68528A677560B16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027167 Genomic DNA. Translation: AAC64907.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF027167 Genomic DNA. Translation: AAC64907.1.

3D structure databases

ProteinModelPortaliO52191.
SMRiO52191. Positions 4-416.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO52191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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...

Publicationsi

  1. "pCI65st, a 6.5 kb plasmid from Streptococcus thermophilus NDI-6, harbours genes encoding two small heat shock proteins, enolase and a putative specificity subunit protein from a type I R/M system."
    O'Sullivan T.F., Fitzgerald G.F.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NDI-6.

Entry informationi

Entry nameiENO_STRTR
AccessioniPrimary (citable) accession number: O52191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.