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Protein

Enolase

Gene
N/A
Organism
Cunninghamella elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

Cofactori

Mg2+By similarityNote: Mg2+ is required for catalysis and for stabilizing the dimer.By similarity

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase
  5. no protein annotated in this organism
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 sitei159SubstrateBy similarity1
Binding sitei168SubstrateBy similarity1
Active sitei211Proton donorBy similarity1
Metal bindingi246MagnesiumBy similarity1
Metal bindingi295MagnesiumBy similarity1
Binding sitei295SubstrateBy similarity1
Metal bindingi320MagnesiumBy similarity1
Binding sitei320SubstrateBy similarity1
Active sitei345Proton acceptorBy similarity1
Binding sitei396SubstrateBy similarity1

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 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
OrganismiCunninghamella elegans
Taxonomic identifieri4853 [NCBI]
Taxonomic lineageiEukaryotaFungiMucoromycotaMucoromycotinaMucoralesCunninghamellaceaeCunninghamella

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000134048‹1 – 436EnolaseAdd BLAST›436

Proteomic databases

PRIDEiO74286.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO74286.
SMRiO74286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni372 – 375Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

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: Fragment.

O74286-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
STITKVHARQ IFDSRGNPTV EVEVTTDKGV FRAGVPSGAS TGVHEALELR
60 70 80 90 100
DGVKSDYLGK GVLKAVGNVN TIINEELVKA NLSVVDQKAV DDFLIQLDGT
110 120 130 140 150
ENKEKLGANA ILGVSLAVAK AGAAEKGVPF YVHIADLAGS KKPFVLPVPA
160 170 180 190 200
FNVINGGSHA GNKLAMQEFM IMPTGAKSFS EAMKLGSEVY HTLKKVINEK
210 220 230 240 250
YGQDATNVGD EGGFAPNIQD NQEGLELLVT AIEKAGYTGK IKVAMDCAAS
260 270 280 290 300
DFYKDGKYDL DFKNPNSDPS TYLTGQDLTD LYNSYAGKYP IVSIEDAFDQ
310 320 330 340 350
DDWENWAHMN ASADYQLVGD DLTVTNPKRI ATAVEKKACN ALLLKVNQIG
360 370 380 390 400
TLTESIQAAL DSQKAGWGVM VSHRSGETED TSIASIVVGL RTGQIKTGAP
410 420 430
CRSERLAKYN ELLRIEEELG DAAIYAGEHF RKAHDL
Length:436
Mass (Da):46,878
Last modified:November 1, 1998 - v1
Checksum:i32BA0B8E5C801738
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17298 mRNA. Translation: CAA76735.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17298 mRNA. Translation: CAA76735.1.

3D structure databases

ProteinModelPortaliO74286.
SMRiO74286.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO74286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiENO_CUNEL
AccessioniPrimary (citable) accession number: O74286
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: April 12, 2017
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.