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Protein

Enolase

Gene

eno

Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
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), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (Cbei_0485), Pyruvate kinase (Cbei_1412), Pyruvate kinase (Cbei_4851)
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 sitei158SubstrateUniRule annotation1
Binding sitei167SubstrateUniRule annotation1
Active sitei208Proton donorUniRule annotation1
Metal bindingi245MagnesiumUniRule annotation1
Metal bindingi288MagnesiumUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Metal bindingi315MagnesiumUniRule annotation1
Binding sitei315SubstrateUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei391SubstrateUniRule 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:Cbei_0602
OrganismiClostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
Taxonomic identifieri290402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000565 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_10000791281 – 430EnolaseAdd BLAST430

Proteomic databases

PRIDEiA6LR09.

Interactioni

Protein-protein interaction databases

STRINGi290402.Cbei_0602.

Structurei

3D structure databases

ProteinModelPortaliA6LR09.
SMRiA6LR09.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 370Substrate 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.

A6LR09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKDYLEIVDV VARQILDSRC FPTVEVEIYL EDGTIGRAAV PSGASTGMYE
60 70 80 90 100
AVELRDGDKD KFLGKGVLNA IRNVNEIIAE ELIGCNVFEQ TYIDKMLIEL
110 120 130 140 150
DGTNNKSKLG ANAILGVSLA VANAAANSLD MPLYRYIGGV NSKVLPVPMM
160 170 180 190 200
NILNGGSHAD NSVDLQEFMI MPAGAPTFSE ALRMCAEVYH TLKKILNDKG
210 220 230 240 250
YSTGIGDEGG FAPNLKSNQE ALDVIIEAIG KAGYKAGEEI FIAIDAASSE
260 270 280 290 300
YYKDGKYVLE HEGRTLTSAE MVDFFEDWVN KYPIISIEDG MAEEDWEGWK
310 320 330 340 350
LITERLGKKV QLVGDDLFVT NTERLEKGID LGVANSILIK LNQIGTLTET
360 370 380 390 400
LNAIEMANRA GYTAVVSHRS GETEDTTIAD LVVAVNAGQI KTGAPARSER
410 420 430
VAKYNQLLRI EEELNDVAEY RGRKAFFNIK
Length:430
Mass (Da):47,059
Last modified:July 24, 2007 - v1
Checksum:iFD5F5E3883AA7A17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000721 Genomic DNA. Translation: ABR32789.1.
RefSeqiWP_011967950.1. NC_009617.1.

Genome annotation databases

EnsemblBacteriaiABR32789; ABR32789; Cbei_0602.
KEGGicbe:Cbei_0602.

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_CLOB8
AccessioniPrimary (citable) accession number: A6LR09
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: June 7, 2017
This is version 69 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