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Protein

Enolase

Gene

eno

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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 (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (pykA), Pyruvate kinase (pyk)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581SubstrateUniRule annotation
Binding sitei167 – 1671SubstrateUniRule annotation
Active sitei208 – 2081Proton donorUniRule annotation
Metal bindingi245 – 2451MagnesiumUniRule annotation
Metal bindingi288 – 2881MagnesiumUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Metal bindingi315 – 3151MagnesiumUniRule annotation
Binding sitei315 – 3151SubstrateUniRule annotation
Active sitei340 – 3401Proton acceptorUniRule annotation
Binding sitei340 – 3401Substrate (covalent); in inhibited formUniRule annotation
Binding sitei391 – 3911SubstrateUniRule annotation

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

BioCyciCACE272562:GJIH-756-MONOMER.
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:CA_C0713
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431EnolasePRO_0000133871Add
BLAST

Proteomic databases

PRIDEiQ97L52.

Interactioni

Protein-protein interaction databases

STRINGi272562.CA_C0713.

Structurei

3D structure databases

ProteinModelPortaliQ97L52.
SMRiQ97L52. Positions 7-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 3704Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

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.

Q97L52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSYVEIVDV MARQILDSRA NPTVEVEVVL EDGTVGRASV PSGASTGQFE
60 70 80 90 100
AVELRDNDKA QYLGKSVLNA VDNVNETIAT ELIGMNVFDQ TLIDQTMLEI
110 120 130 140 150
DGTENKSKLG ANAMLGVSLA VARAAAEYLG ISLYQYLGGV NAKVLPVPMM
160 170 180 190 200
NIVNGGKHAD NNVDFQEFMI MPAGAPSFSE ALRSCAEVYH TLKSLLQSKG
210 220 230 240 250
LETAVGDEGG FAPNLNSNEE AIQIILEAVT KAGYEPGKDM FIAMDPASTE
260 270 280 290 300
FYENGKYNLK GEGKVYTSEE MVEVYANLVE KYPIISLEDG MAEEDWDGWK
310 320 330 340 350
LLTDRIGDKV QLVGDDLFVT NTKRLSKGIQ LGVANSILIK LNQIGTLTET
360 370 380 390 400
LNAIEMAQRA GYTAVVSHRS GETEDTTISD LVVAVNAGQI KTGAPARTER
410 420 430
VAKYNQLLRI EEELGEVAEF RGLNAFYNIK K
Length:431
Mass (Da):46,802
Last modified:October 1, 2001 - v1
Checksum:i298E9CA31C733FF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78690.1.
PIRiG96987.
RefSeqiNP_347350.1. NC_003030.1.
WP_010964032.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK78690; AAK78690; CA_C0713.
GeneIDi1116896.
KEGGicac:CA_C0713.
PATRICi32035793. VBICloAce74127_0916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78690.1.
PIRiG96987.
RefSeqiNP_347350.1. NC_003030.1.
WP_010964032.1. NC_003030.1.

3D structure databases

ProteinModelPortaliQ97L52.
SMRiQ97L52. Positions 7-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C0713.

Proteomic databases

PRIDEiQ97L52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK78690; AAK78690; CA_C0713.
GeneIDi1116896.
KEGGicac:CA_C0713.
PATRICi32035793. VBICloAce74127_0916.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciCACE272562:GJIH-756-MONOMER.

Family and domain databases

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_CLOAB
AccessioniPrimary (citable) accession number: Q97L52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2001
Last modified: September 7, 2016
This is version 102 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

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.