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Protein

Beta-enolase

Gene

ENO3

Organism
Salmo salar (Atlantic salmon)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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.By similarity
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gapdh), Glyceraldehyde-3-phosphate dehydrogenase (G3P), Glyceraldehyde-3-phosphate dehydrogenase (G3P), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (G3P), Glyceraldehyde-3-phosphate dehydrogenase (G3P)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Beta-enolase (ENO3)
  5. Pyruvate kinase (KPYK), Pyruvate kinase (KPYK), Pyruvate kinase (KPYK), Pyruvate kinase (pk), Pyruvate kinase (KPYK)
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 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181MagnesiumBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

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

UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase1 Publication (EC:4.2.1.11By similarity)
Alternative name(s):
2-phospho-D-glycerate hydro-lyaseBy similarity
Enolase 3By similarity
Muscle-specific enolaseBy similarity
Short name:
MSEBy similarity
Skeletal muscle enolaseBy similarity
Allergen: Sal s 2.01011 Publication
Gene namesi
Name:ENO3By similarity
OrganismiSalmo salar (Atlantic salmon)
Taxonomic identifieri8030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei9699. Sal s 2.
9700. Sal s 2.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 434433Beta-enolase1 PublicationPRO_0000425076Add
BLAST

Interactioni

Subunit structurei

Dimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliB5DGQ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Sequence analysis

Phylogenomic databases

HOVERGENiHBG000067.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

B5DGQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSITKIHARE ILDSRGNPTV EVDLYTAKGR FRAAVPSGAS TGVHEALELR
60 70 80 90 100
DGDKSRYLGK GTVKAVDHVN KDIAAKLIEK KFSVVDQEKI DHFMLELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGH KDVILPCPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPIGASNFHE AMRIGAEVYH NLKNVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IEKAGYPDKI IIGMDVAASE
260 270 280 290 300
FYKAGKYDLD FKSPDDPARY ITGDQLGDLY KSFIKGYPVQ SIEDPFDQDD
310 320 330 340 350
WAAWTKFTAA VDIQVVGDDL TVTNPKRIQQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIKACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEELGAK AKFAGKDYRH PKIN
Length:434
Mass (Da):47,287
Last modified:October 14, 2008 - v1
Checksum:i802A7956054679B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → I in ACH70930 (PubMed:19878547).Curated
Sequence conflicti43 – 431V → I in ACH70930 (PubMed:19878547).Curated
Sequence conflicti63 – 631V → L in ACH70930 (PubMed:19878547).Curated
Sequence conflicti92 – 921H → K in ACH70930 (PubMed:19878547).Curated
Sequence conflicti131 – 1311Y → F in ACH70930 (PubMed:19878547).Curated
Sequence conflicti229 – 2291T → S in ACH70930 (PubMed:19878547).Curated
Sequence conflicti305 – 3051T → S in ACH70930 (PubMed:19878547).Curated
Sequence conflicti416 – 4161E → A in ACH70930 (PubMed:19878547).Curated
Sequence conflicti419 – 4191A → D in ACH70930 (PubMed:19878547).Curated
Sequence conflicti433 – 4331I → V in ACH70930 (PubMed:19878547).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT043815 mRNA. Translation: ACH70930.1.
BT043816 mRNA. Translation: ACH70931.1.
BT043817 mRNA. Translation: ACH70932.1.
RefSeqiNP_001133193.1. NM_001139721.1.
NP_001135172.1. NM_001141700.1.
UniGeneiSsa.4786.
Ssa.5704.

Genome annotation databases

GeneIDi100194636.
100196671.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT043815 mRNA. Translation: ACH70930.1.
BT043816 mRNA. Translation: ACH70931.1.
BT043817 mRNA. Translation: ACH70932.1.
RefSeqiNP_001133193.1. NM_001139721.1.
NP_001135172.1. NM_001141700.1.
UniGeneiSsa.4786.
Ssa.5704.

3D structure databases

ProteinModelPortaliB5DGQ7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9699. Sal s 2.
9700. Sal s 2.0101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100194636.
100196671.

Phylogenomic databases

HOVERGENiHBG000067.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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 nameiENOB_SALSA
AccessioniPrimary (citable) accession number: B5DGQ7
Secondary accession number(s): B5DGQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: October 14, 2008
Last modified: May 11, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.