Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enolase

Gene

eno

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
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)
  5. Pyruvate kinase (pykA)
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 sitei154SubstrateUniRule annotation1
Binding sitei163SubstrateUniRule annotation1
Active sitei204Proton donorUniRule annotation1
Metal bindingi241MagnesiumUniRule annotation1
Metal bindingi284MagnesiumUniRule annotation1
Binding sitei284SubstrateUniRule annotation1
Metal bindingi311MagnesiumUniRule annotation1
Binding sitei311SubstrateUniRule annotation1
Active sitei336Proton acceptorUniRule annotation1
Binding sitei336Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei387SubstrateUniRule 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:R01443
ORF Names:SMc01028
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
Proteomesi
  • UP000001976 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_00001339551 – 424EnolaseAdd BLAST424

Proteomic databases

PRIDEiQ92Q98.

Interactioni

Protein-protein interaction databases

STRINGi266834.SMc01028.

Structurei

3D structure databases

ProteinModelPortaliQ92Q98.
SMRiQ92Q98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni363 – 366Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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

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.

Q92Q98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAIIDIIGR EILDSRGNPT VEVDVHLEDG SFGRAAVPSG ASTGAHEAVE
60 70 80 90 100
LRDGGTRYLG KGVERAVDAV NGEIFEAIGG LDAENQIQID RTMIELDGTP
110 120 130 140 150
NKSRLGANAI LGVSLAVAKA AAEASGLPLY RYVGGPNAHL LPVPMMNIIN
160 170 180 190 200
GGAHADNPID FQEFMIMPVG AETLKDAVRM GSEVFHTLKK QLAADGHNTN
210 220 230 240 250
VGDEGGFAPG LASAPAALDF IMKSIEKAGY KPGEDMYVAL DCASTEFFKD
260 270 280 290 300
GKYVLEGEGR TLEPGAMAEY LAELAGKYPI ISIEDGMAED DWDGWKSLTD
310 320 330 340 350
LVGNKCQLVG DDLFVTNSAR LRDGIKMGVA NSILVKVNQI GSLSETLDAV
360 370 380 390 400
ETAHKARYTA VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRLAKY
410 420
NQLIRIEEQL GPQAQYAGRS VLRG
Length:424
Mass (Da):44,996
Last modified:December 1, 2001 - v1
Checksum:iD698D8E07DCA0F14
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591688 Genomic DNA. Translation: CAC46022.1.
RefSeqiNP_385549.1. NC_003047.1.
WP_010969226.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC46022; CAC46022; SMc01028.
GeneIDi1233096.
KEGGisme:SMc01028.
PATRICifig|266834.11.peg.2863.

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.

Entry informationi

Entry nameiENO_RHIME
AccessioniPrimary (citable) accession number: Q92Q98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: December 1, 2001
Last modified: June 7, 2017
This is version 102 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