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Protein

Enolase

Gene

eno

Organism
Rhodopseudomonas palustris (strain BisB5)
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-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (RPD_2327), Pyruvate kinase (RPD_1402)
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:RPD_2816
OrganismiRhodopseudomonas palustris (strain BisB5)
Taxonomic identifieri316057 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
Proteomesi
  • UP000001818 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_00002670921 – 427EnolaseAdd BLAST427

Proteomic databases

PRIDEiQ136E5.

Interactioni

Protein-protein interaction databases

STRINGi316057.RPD_2816.

Structurei

3D structure databases

ProteinModelPortaliQ136E5.
SMRiQ136E5.
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.
HOGENOMiHOG000072173.
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.
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.
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.

Q136E5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAIVDIIGR EILDSRGNPT VEVDVVLEDG SVGRAAVPSG ASTGAHEAVE
60 70 80 90 100
LRDGDKARYL GKGVLKAVEA VNGELFDALG GMDAEQQVQI DQTMIELDGT
110 120 130 140 150
PNKGRLGANA ILGVSLAVAK AAASSYDLPL YRYVGGTSAR TLPVPMMNII
160 170 180 190 200
NGGAHADNPI DFQEFMIMPV GAASFSEALR CGSEIFHTLK GELKKAGHNT
210 220 230 240 250
NVGDEGGFAP NLPSADAALD FVMAAIGKAG YKAGEDVMIA LDPASTEFFK
260 270 280 290 300
NGKYVYEAEG RSLGPQEQAK YLADLVARYP IVSIEDGMAE DDIEGWKAIT
310 320 330 340 350
DLIGDKCQLV GDDLFVTNVT RLADGIKNGY ANSILIKVNQ IGTLTETLAA
360 370 380 390 400
VEMAHKAGYT AVMSHRSGET EDSTIADLAV ATNCGQIKTG SLARADRTAK
410 420
YNQLLRIEQE LGAQAHYAGK AALKAFR
Length:427
Mass (Da):45,044
Last modified:October 31, 2006 - v1
Checksum:i664E946B528C7674
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000283 Genomic DNA. Translation: ABE40044.1.
RefSeqiWP_011503221.1. NC_007958.1.

Genome annotation databases

EnsemblBacteriaiABE40044; ABE40044; RPD_2816.
KEGGirpd:RPD_2816.
PATRICi23280675. VBIRhoPal120395_2903.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000283 Genomic DNA. Translation: ABE40044.1.
RefSeqiWP_011503221.1. NC_007958.1.

3D structure databases

ProteinModelPortaliQ136E5.
SMRiQ136E5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316057.RPD_2816.

Proteomic databases

PRIDEiQ136E5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE40044; ABE40044; RPD_2816.
KEGGirpd:RPD_2816.
PATRICi23280675. VBIRhoPal120395_2903.

Phylogenomic databases

eggNOGiENOG4105C70. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072173.
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.
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.
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_RHOPS
AccessioniPrimary (citable) accession number: Q136E5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 31, 2006
Last modified: March 15, 2017
This is version 76 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

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.