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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. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (A6P53_04110)
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 bindingi242Magnesium1
Metal bindingi288Magnesium1
Binding sitei288SubstrateUniRule annotation1
Metal bindingi315Magnesium1
Binding sitei315SubstrateUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei391SubstrateUniRule annotation1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001338861 – 432EnolaseAdd BLAST432

Proteomic databases

PRIDEiQ8GR70.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 13Combined sources11
Beta strandi19 – 27Combined sources9
Beta strandi32 – 36Combined sources5
Beta strandi45 – 47Combined sources3
Helixi59 – 61Combined sources3
Helixi65 – 73Combined sources9
Helixi75 – 79Combined sources5
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 126Combined sources19
Helixi130 – 135Combined sources6
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Beta strandi156 – 159Combined sources4
Beta strandi162 – 168Combined sources7
Helixi175 – 196Combined sources22
Beta strandi204 – 206Combined sources3
Beta strandi213 – 215Combined sources3
Helixi216 – 229Combined sources14
Turni233 – 236Combined sources4
Beta strandi238 – 242Combined sources5
Turni245 – 248Combined sources4
Turni251 – 253Combined sources3
Beta strandi255 – 257Combined sources3
Turni259 – 262Combined sources4
Helixi268 – 281Combined sources14
Beta strandi284 – 289Combined sources6
Helixi296 – 306Combined sources11
Turni307 – 309Combined sources3
Beta strandi310 – 315Combined sources6
Turni316 – 320Combined sources5
Helixi322 – 331Combined sources10
Beta strandi337 – 339Combined sources3
Helixi341 – 344Combined sources4
Helixi347 – 359Combined sources13
Beta strandi364 – 367Combined sources4
Helixi377 – 384Combined sources8
Beta strandi388 – 391Combined sources4
Beta strandi395 – 397Combined sources3
Helixi398 – 414Combined sources17
Helixi415 – 417Combined sources3
Helixi422 – 425Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8GR70.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 370Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

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.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IYXX-ray2.80A/B1-432[»]
ProteinModelPortaliQ8GR70.
SMRiQ8GR70.
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

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
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...

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: November 2, 2016
This is version 81 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.