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Protein

Enolase

Gene

eno

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
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. Glyceraldehyde-3-phosphate dehydrogenase 1 (gap1), Glyceraldehyde-3-phosphate dehydrogenase 2 (gap2)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (pykA2), Pyruvate kinase (pykA1)
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 bindingi283MagnesiumUniRule annotation1
Binding sitei283SubstrateUniRule annotation1
Metal bindingi310MagnesiumUniRule annotation1
Binding sitei310SubstrateUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Binding sitei335Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei386SubstrateUniRule 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:SAV_3533
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000000428 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_00001339751 – 428EnolaseAdd BLAST428

Proteomic databases

PRIDEiQ82HH5.

Interactioni

Protein-protein interaction databases

STRINGi227882.SAV_3533.

Structurei

3D structure databases

ProteinModelPortaliQ82HH5.
SMRiQ82HH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni362 – 365Substrate 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.

Q82HH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSIDVVVAR EILDSRGNPT VEVEVGLDDG STGRAAVPSG ASTGAFEAIE
60 70 80 90 100
LRDGDPNRYQ GKGVEKAVLA VIEQIGPELV GYDATEQRLI DQAMFDLDAT
110 120 130 140 150
DNKGSLGANA ILGVSLAVAH AASEASDLPL FRYLGGPNAH LLPVPMMNIL
160 170 180 190 200
NGGSHADSNV DIQEFMIAPI GAESFSEALR WGAEVYHTLK KVLKTKGLST
210 220 230 240 250
GLGDEGGFAP NLESNRAALD LIIEAIKQAG YIPGEQIALA LDVAASEFYK
260 270 280 290 300
DGKYEFEGKS RSAAEMTEYY EELVSAYPLV SIEDPLYEDD WAGWKVITDK
310 320 330 340 350
LGDKVQIVGD DLFVTNPERL ARGIEEGSAN ALLVKVNQIG SLTETLDAVE
360 370 380 390 400
LAQRNGFKCM MSHRSGETED VTIADLAVAV NCGQIKTGAP ARSDRVAKYN
410 420
QLLRIEEILD DAAEYAGRSA FPRFRSAN
Length:428
Mass (Da):45,869
Last modified:June 1, 2003 - v1
Checksum:i095A3976F6C5F70D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC71245.1.

Genome annotation databases

EnsemblBacteriaiBAC71245; BAC71245; SAVERM_3533.
KEGGisma:SAV_3533.
PATRICi23720739. VBIStrAve112782_3775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC71245.1.

3D structure databases

ProteinModelPortaliQ82HH5.
SMRiQ82HH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_3533.

Proteomic databases

PRIDEiQ82HH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC71245; BAC71245; SAVERM_3533.
KEGGisma:SAV_3533.
PATRICi23720739. VBIStrAve112782_3775.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiENO_STRAW
AccessioniPrimary (citable) accession number: Q82HH5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2003
Last modified: April 12, 2017
This is version 101 of the entry and version 1 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

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.