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Protein

Enolase 1

Gene

eno1

Organism
Desulfitobacterium hafniense (strain Y51)
Status
Reviewed-Annotation score: Annotation score: 4 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 1 (eno1), Enolase 2 (eno2)
  5. 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)DescriptionActionsGraphical viewLength
Binding sitei156SubstrateUniRule annotation1
Binding sitei165SubstrateUniRule annotation1
Active sitei206Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi289MagnesiumUniRule annotation1
Binding sitei289SubstrateUniRule annotation1
Metal bindingi316MagnesiumUniRule annotation1
Binding sitei316SubstrateUniRule annotation1
Active sitei341Proton acceptorUniRule annotation1
Binding sitei341Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei392SubstrateUniRule 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:
Enolase 1UniRule annotation (EC:4.2.1.11UniRule annotation)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1UniRule annotation
2-phosphoglycerate dehydratase 1UniRule annotation
Gene namesi
Name:eno1UniRule annotation
Ordered Locus Names:DSY0989
OrganismiDesulfitobacterium hafniense (strain Y51)
Taxonomic identifieri138119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
Proteomesi
  • UP000001946 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_00002808441 – 437Enolase 1Add BLAST437

Interactioni

Protein-protein interaction databases

STRINGi138119.DSY0989.

Structurei

3D structure databases

ProteinModelPortaliQ24YW4.
SMRiQ24YW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108N3Q. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OMAiKWNEVLR.
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.

Q24YW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGFKIKSVK ARQVFDSRAN PTVEVDITLK DGTVGRGIVP SGASTGLFEA
60 70 80 90 100
VELRDGEETF DGKGVSKAIH HVNEQLAPLL LDMDVRDQKA IDSRLIEIDG
110 120 130 140 150
TPNKSRLGAN AILGCSMAAC WAGANYYKVP LYRYLGGSAA NKLPVPMVQI
160 170 180 190 200
IGGGAHADNV IDIQDFLVIP TSAPTFSEGY EMVVNVYNAA KMIFKGAGKP
210 220 230 240 250
VSIADEGGLW PTGFQSNEEG LKLLCESIEL AGYTPGQDLG IALDIASSEF
260 270 280 290 300
YDPERGTYRL ELEKKTLTKE EMVGMLSDWV DNYPIISIED GMSELDWEGN
310 320 330 340 350
LLLTQKLGKK IQLIGDDLFT TNIERIRKGV EMKVDNAVLI KMNQIGTITE
360 370 380 390 400
TIETIEFTQN HGYLPVVSAR SGETEDCTIV HLAIATNAGQ LKVGSAARSE
410 420 430
RTAKWNEVLR IEEALGSSAR YPSKGVFAAA GIQFNQY
Length:437
Mass (Da):47,492
Last modified:April 18, 2006 - v1
Checksum:iE8BCC5D462347988
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008230 Genomic DNA. Translation: BAE82778.1.
RefSeqiWP_011459461.1. NC_007907.1.

Genome annotation databases

EnsemblBacteriaiBAE82778; BAE82778; DSY0989.
KEGGidsy:DSY0989.
PATRICi21670280. VBIDesHaf65307_1107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008230 Genomic DNA. Translation: BAE82778.1.
RefSeqiWP_011459461.1. NC_007907.1.

3D structure databases

ProteinModelPortaliQ24YW4.
SMRiQ24YW4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi138119.DSY0989.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE82778; BAE82778; DSY0989.
KEGGidsy:DSY0989.
PATRICi21670280. VBIDesHaf65307_1107.

Phylogenomic databases

eggNOGiENOG4108N3Q. Bacteria.
COG0148. LUCA.
HOGENOMiHOG000072174.
KOiK01689.
OMAiKWNEVLR.
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 nameiENO1_DESHY
AccessioniPrimary (citable) accession number: Q24YW4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: April 18, 2006
Last modified: March 15, 2017
This is version 78 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Asp-165 is present instead of the conserved Glu which is expected to be a substrate-binding residue.Curated
Ala-369 is present instead of the conserved His which is expected to be part of the substrate-binding region.Curated

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.