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Protein

Enolase

Gene

eno

Organism
Enterococcus hirae
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 annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation1 PublicationNote: Mg2+ is required for catalysis and for stabilizing the dimer.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.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. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase (eno)
  5. no protein annotated in this organism
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 – 2421Magnesium
Metal bindingi288 – 2881Magnesium
Binding sitei288 – 2881SubstrateUniRule annotation
Metal bindingi315 – 3151Magnesium
Binding sitei315 – 3151SubstrateUniRule annotation
Active sitei340 – 3401Proton acceptorUniRule annotation
Binding sitei340 – 3401Substrate (covalent); in inhibited formUniRule annotation
Binding sitei391 – 3911SubstrateUniRule 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

BRENDAi4.2.1.11. 2097.
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
OrganismiEnterococcus hirae
Taxonomic identifieri1354 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

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 – 432432EnolasePRO_0000133886Add
BLAST

Proteomic databases

PRIDEiQ8GR70.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Beta strandi19 – 279Combined sources
Beta strandi32 – 365Combined sources
Beta strandi45 – 473Combined 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 strandi156 – 1594Combined sources
Beta strandi162 – 1687Combined sources
Helixi175 – 19622Combined sources
Beta strandi204 – 2063Combined sources
Beta strandi213 – 2153Combined sources
Helixi216 – 22914Combined sources
Turni233 – 2364Combined sources
Beta strandi238 – 2425Combined sources
Turni245 – 2484Combined sources
Turni251 – 2533Combined sources
Beta strandi255 – 2573Combined sources
Turni259 – 2624Combined sources
Helixi268 – 28114Combined sources
Beta strandi284 – 2896Combined sources
Helixi296 – 30611Combined sources
Turni307 – 3093Combined sources
Beta strandi310 – 3156Combined sources
Turni316 – 3205Combined sources
Helixi322 – 33110Combined sources
Beta strandi337 – 3393Combined sources
Helixi341 – 3444Combined sources
Helixi347 – 35913Combined sources
Beta strandi364 – 3674Combined sources
Helixi377 – 3848Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi395 – 3973Combined sources
Helixi398 – 41417Combined sources
Helixi415 – 4173Combined sources
Helixi422 – 4254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYXX-ray2.80A/B1-432[»]
ProteinModelPortaliQ8GR70.
SMRiQ8GR70. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GR70.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 3704Substrate 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.

Q8GR70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIITDVYAR EILDSRGNPT IEVEVYTESG AFGRGMVPSG ASTGEYEAVE
60 70 80 90 100
LRDGDKARYG GKGVTKAVDN VNNIIAEAII GYDVRDQMAI DKAMIALDGT
110 120 130 140 150
PNKGKLGANA ILGVSIAVAR AAADYLEVPL YHYLGGFNTK VLPTPMMNII
160 170 180 190 200
NGGSHADNSI DFQEFMIMPV GAPTFKEALR MGAEVFHALA AILKSRGLAT
210 220 230 240 250
SVGDEGGFAP NLGSNEEGFE VIIEAIEKAG YVPGKDVVLA MDAASSEFYD
260 270 280 290 300
KEKGVYVLAD SGEGEKTTDE MIKFYEELVS KYPIISIEDG LDENDWDGFK
310 320 330 340 350
KLTDVLGDKV QLVGDDLFVT NTQKLSEGIE KGIANSILIK VNQIGTLTET
360 370 380 390 400
FEAIEMAKEA GYTAVVSHRS GETEDSTISD IAVATNAGQI KTGSLSRTDR
410 420 430
IAKYNQLLRI EDQLGEVAEY KGLKSFYNLK AA
Length:432
Mass (Da):46,411
Last modified:March 1, 2003 - v1
Checksum:i45F203F55685F1C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091345 Genomic DNA. Translation: BAC16223.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091345 Genomic DNA. Translation: BAC16223.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYXX-ray2.80A/B1-432[»]
ProteinModelPortaliQ8GR70.
SMRiQ8GR70. Positions 2-432.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ8GR70.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BRENDAi4.2.1.11. 2097.

Miscellaneous databases

EvolutionaryTraceiQ8GR70.

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. "Crystal structure of Enterococcus hirae enolase at 2.8 A resolution."
    Hosaka T., Meguro T., Yamato I., Shirakihara Y.
    J. Biochem. 133:817-823(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiENO_ENTHR
AccessioniPrimary (citable) accession number: Q8GR70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 79 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.