UniProtKB - Q9XSJ4 (ENOA_BOVIN)
Alpha-enolase
ENO1
Functioni
Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (By similarity).
In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:7499243).
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 (By similarity).
Stimulates immunoglobulin production (By similarity).
By similarity1 PublicationCatalytic activityi
- EC:4.2.1.11By similarity
Cofactori
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate. 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 40 | Magnesium 1By similarity | 1 | |
Binding sitei | 158 | SubstrateBy similarity | 1 | |
Binding sitei | 167 | SubstrateBy similarity | 1 | |
Active sitei | 210 | Proton donorBy similarity | 1 | |
Metal bindingi | 245 | Magnesium 2By similarity | 1 | |
Metal bindingi | 293 | Magnesium 2By similarity | 1 | |
Binding sitei | 293 | SubstrateBy similarity | 1 | |
Metal bindingi | 318 | Magnesium 2By similarity | 1 | |
Binding sitei | 318 | SubstrateBy similarity | 1 | |
Active sitei | 343 | Proton acceptorBy similarity | 1 | |
Binding sitei | 394 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- magnesium ion binding Source: InterPro
- phosphopyruvate hydratase activity Source: UniProtKB
GO - Biological processi
- canonical glycolysis Source: UniProtKB
- glycolytic process Source: GO_Central
Keywordsi
Molecular function | Lyase |
Biological process | Glycolysis, Plasminogen activation |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
SABIO-RKi | Q9XSJ4 |
UniPathwayi | UPA00109;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 HAP47 Non-neural enolase Short name: NNE Phosphopyruvate hydratase |
Gene namesi | Name:ENO1 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Plasma membrane
- Cell membrane By similarity
Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band.By similarity
Cytosol
- phosphopyruvate hydratase complex Source: GO_Central
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: AgBase
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000134096 | 2 – 434 | Alpha-enolaseAdd BLAST | 433 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 5 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 44 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 60 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 60 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 64 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 71 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 89 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 89 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 92 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 126 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 193 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 199 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 202 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 202 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 228 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 228 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 228 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 233 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 233 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 254 | PhosphoserineBy similarity | 1 | |
Modified residuei | 256 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 263 | PhosphoserineBy similarity | 1 | |
Modified residuei | 281 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 281 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 287 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 291 | PhosphoserineBy similarity | 1 | |
Modified residuei | 335 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 343 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 406 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 420 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 420 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 420 | N6-succinyllysine; alternateBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q9XSJ4 |
PeptideAtlasi | Q9XSJ4 |
PRIDEi | Q9XSJ4 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
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).
Interacts with CMTM6 (By similarity).
By similarityProtein-protein interaction databases
STRINGi | 9913.ENSBTAP00000017839 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 370 – 373 | Substrate bindingBy similarity | 4 | |
Regioni | 405 – 434 | Required for interaction with PLGBy similarityAdd BLAST | 30 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2670, Eukaryota |
InParanoidi | Q9XSJ4 |
OMAi | EFMIIPV |
OrthoDBi | 773373at2759 |
Family and domain databases
CDDi | cd03313, enolase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
HAMAPi | MF_00318, Enolase, 1 hit |
InterProi | View protein in InterPro IPR000941, Enolase IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR020810, Enolase_C IPR020809, Enolase_CS IPR020811, Enolase_N |
PANTHERi | PTHR11902, PTHR11902, 1 hit |
Pfami | View protein in Pfam PF00113, Enolase_C, 1 hit PF03952, Enolase_N, 1 hit |
PIRSFi | PIRSF001400, Enolase, 1 hit |
PRINTSi | PR00148, ENOLASE |
SFLDi | SFLDF00002, enolase, 1 hit |
SMARTi | View protein in SMART SM01192, Enolase_C, 1 hit SM01193, Enolase_N, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01060, eno, 1 hit |
PROSITEi | View protein in PROSITE PS00164, ENOLASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MSILKVHARE IFDSRGNPTV EVDLFTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVVEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN AEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAENFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEALELLKNA IGKAGYSDKV VIGMDVAASE
260 270 280 290 300
FYRSGKYDLD FKSPDDPSRY ITPDELANLY KSFIRDYPVV SIEDPFDQDD
310 320 330 340 350
WEAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVSEKSCNCL LLKVNQIGSV
360 370 380 390 400
TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTVAPCR
410 420 430
SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 82 | L → S in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 102 | N → K in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 324 | N → T in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 327 | R → T in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 331 – 333 | AVS → GVN in AAD33073 (Ref. 1) Curated | 3 | |
Sequence conflicti | 347 | I → N in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 356 | A → G in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 361 – 362 | QS → HA in AAD33073 (Ref. 1) Curated | 2 | |
Sequence conflicti | 377 | E → D in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 383 | D → E in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 395 – 397 | TVA → NGP in AAD33073 (Ref. 1) Curated | 3 | |
Sequence conflicti | 401 | S → T in AAD33073 (Ref. 1) Curated | 1 | |
Sequence conflicti | 427 | S → N in AAD33073 (Ref. 1) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF149256 mRNA Translation: AAD33073.1 BC103354 mRNA Translation: AAI03355.1 |
RefSeqi | NP_776474.2, NM_174049.2 |
Genome annotation databases
GeneIDi | 281141 |
KEGGi | bta:281141 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF149256 mRNA Translation: AAD33073.1 BC103354 mRNA Translation: AAI03355.1 |
RefSeqi | NP_776474.2, NM_174049.2 |
3D structure databases
SMRi | Q9XSJ4 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9913.ENSBTAP00000017839 |
Protein family/group databases
Allergomei | 11909, Bos d Enolase |
Proteomic databases
PaxDbi | Q9XSJ4 |
PeptideAtlasi | Q9XSJ4 |
PRIDEi | Q9XSJ4 |
Genome annotation databases
GeneIDi | 281141 |
KEGGi | bta:281141 |
Organism-specific databases
CTDi | 2023 |
Phylogenomic databases
eggNOGi | KOG2670, Eukaryota |
InParanoidi | Q9XSJ4 |
OMAi | EFMIIPV |
OrthoDBi | 773373at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00187 |
SABIO-RKi | Q9XSJ4 |
Family and domain databases
CDDi | cd03313, enolase, 1 hit |
Gene3Di | 3.20.20.120, 1 hit 3.30.390.10, 1 hit |
HAMAPi | MF_00318, Enolase, 1 hit |
InterProi | View protein in InterPro IPR000941, Enolase IPR036849, Enolase-like_C_sf IPR029017, Enolase-like_N IPR020810, Enolase_C IPR020809, Enolase_CS IPR020811, Enolase_N |
PANTHERi | PTHR11902, PTHR11902, 1 hit |
Pfami | View protein in Pfam PF00113, Enolase_C, 1 hit PF03952, Enolase_N, 1 hit |
PIRSFi | PIRSF001400, Enolase, 1 hit |
PRINTSi | PR00148, ENOLASE |
SFLDi | SFLDF00002, enolase, 1 hit |
SMARTi | View protein in SMART SM01192, Enolase_C, 1 hit SM01193, Enolase_N, 1 hit |
SUPFAMi | SSF51604, SSF51604, 1 hit SSF54826, SSF54826, 1 hit |
TIGRFAMsi | TIGR01060, eno, 1 hit |
PROSITEi | View protein in PROSITE PS00164, ENOLASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ENOA_BOVIN | |
Accessioni | Q9XSJ4Primary (citable) accession number: Q9XSJ4 Secondary accession number(s): Q3SYW4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 21, 2001 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 147 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families