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Protein

Alpha-enolase

Gene

ENO1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds two Mg2+ per subunit. 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. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
  2. Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase (PGK2)
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1)
  5. Pyruvate kinase (PKM), Pyruvate kinase PKM (PKM), Pyruvate kinase (PKLR)
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
Metal bindingi40Magnesium 1By similarity1
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245Magnesium 2By similarity1
Metal bindingi293Magnesium 2By similarity1
Binding sitei293SubstrateBy similarity1
Metal bindingi318Magnesium 2By similarity1
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy 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:
Alpha-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 1
Non-neural enolase
Short name:
NNE
Gene namesi
Name:ENO1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002900002 – 434Alpha-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei5N6-acetyllysineBy similarity1
Modified residuei27PhosphoserineBy similarity1
Modified residuei44PhosphotyrosineBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei64N6-acetyllysineBy similarity1
Modified residuei71N6-acetyllysineBy similarity1
Modified residuei89N6-acetyllysine; alternateBy similarity1
Modified residuei89N6-succinyllysine; alternateBy similarity1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei126N6-acetyllysineBy similarity1
Modified residuei193N6-acetyllysineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei202N6-acetyllysine; alternateBy similarity1
Cross-linki202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei228N6-acetyllysine; alternateBy similarity1
Modified residuei228N6-succinyllysine; alternateBy similarity1
Modified residuei233N6-acetyllysine; alternateBy similarity1
Modified residuei233N6-malonyllysine; alternateBy similarity1
Modified residuei254PhosphoserineBy similarity1
Modified residuei256N6-acetyllysineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei272PhosphoserineBy similarity1
Modified residuei281N6-acetyllysineBy similarity1
Modified residuei285N6-acetyllysineBy similarity1
Modified residuei287PhosphotyrosineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1
Modified residuei343N6-acetyllysineBy similarity1
Modified residuei406N6-acetyllysineBy similarity1
Modified residuei420N6-acetyllysine; alternateBy similarity1
Modified residuei420N6-malonyllysine; alternateBy similarity1
Modified residuei420N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ5R6Y1.

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding. Interacts with ENO4 and PGAM2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000002227.

Structurei

3D structure databases

ProteinModelPortaliQ5R6Y1.
SMRiQ5R6Y1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingBy similarity4
Regioni405 – 434Required for interaction with PLGAdd BLAST30

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
HOVERGENiHBG000067.
InParanoidiQ5R6Y1.
KOiK01689.

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.
IPR036849. Enolase_C-like_sf.
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.

Sequencei

Sequence statusi: Complete.

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

Q5R6Y1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE
260 270 280 290 300
FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD
310 320 330 340 350
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNRIGSV
360 370 380 390 400
TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK
Length:434
Mass (Da):47,197
Last modified:December 21, 2004 - v1
Checksum:iA3DE650FFF169EA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860345 mRNA. Translation: CAH92479.1.
RefSeqiNP_001126461.1. NM_001132989.1.

Genome annotation databases

GeneIDi100173448.
KEGGipon:100173448.

Similar proteinsi

Entry informationi

Entry nameiENOA_PONAB
AccessioniPrimary (citable) accession number: Q5R6Y1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: December 21, 2004
Last modified: October 25, 2017
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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