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UniProtKB - P37869 (ENO_BACSU)
Protein
Enolase
Gene
eno
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
UniRule annotationCatalytic activityi
- EC:4.2.1.11UniRule annotation
Cofactori
Mg2+Curated
Activity regulationi
The covalent binding to the substrate at Lys-339 of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (PubMed:15003462). Citrate acts as a non-competitive inhibitor for both forward and reverse reactions, probably by chelating Mg2+ (PubMed:22198292).2 Publications
Kineticsi
- KM=0.44 µM for 2-phospho-D-glycerate1 Publication
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation 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 |
---|---|---|---|---|
Binding sitei | 155 | SubstrateUniRule annotation | 1 | |
Binding sitei | 164 | SubstrateUniRule annotation | 1 | |
Active sitei | 205 | Proton donorUniRule annotation | 1 | |
Metal bindingi | 242 | MagnesiumCurated | 1 | |
Metal bindingi | 287 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 287 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 314 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 314 | SubstrateUniRule annotation | 1 | |
Active sitei | 339 | Proton acceptorUniRule annotation | 1 | |
Binding sitei | 339 | Substrate; covalent; in inhibited form | 1 | |
Binding sitei | 390 | SubstrateUniRule annotation | 1 |
GO - Molecular functioni
- magnesium ion binding Source: UniProtKB-UniRule
- phosphopyruvate hydratase activity Source: GO_Central
GO - Biological processi
- glycolytic process Source: GO_Central
- sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Keywordsi
Molecular function | Lyase |
Biological process | Glycolysis, Sporulation |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | BSUB:BSU33900-MONOMER |
BRENDAi | 4.2.1.11, 658 |
SABIO-RKi | P37869 |
UniPathwayi | UPA00109;UER00187 |
Names & Taxonomyi
Protein namesi | Recommended name: EnolaseUniRule annotation (EC:4.2.1.11UniRule annotation)Alternative name(s): 2-phospho-D-glycerate hydro-lyaseUniRule annotation 2-phosphoglycerate dehydrataseUniRule annotation |
Gene namesi | Name:enoUniRule annotation Ordered Locus Names:BSU33900 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted UniRule annotation1 Publication
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation1 Publication
Other locations
- Cell surface UniRule annotation1 Publication
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 at Lys-339; once secreted, it remains attached to the cell surface.
Cytosol
- phosphopyruvate hydratase complex Source: GO_Central
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- cell surface Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasm, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000133841 | 2 – 430 | EnolaseAdd BLAST | 429 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 141 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 259 | Phosphoserine1 Publication | 1 | |
Modified residuei | 281 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 325 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
Phosphorylated during sporulation.2 Publications
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P37869 |
PaxDbi | P37869 |
PRIDEi | P37869 |
PTM databases
iPTMneti | P37869 |
Interactioni
Subunit structurei
Homooctamer.
Component of a possible RNA degradosome complex composed of rny, rnjA, rnjB, pnp, pfkA and eno (PubMed:19193632) (although rnjA and rnjB's presence is unclear).
4 PublicationsBinary interactionsi
P37869
With | #Exp. | IntAct |
---|---|---|
rny [O31774] | 2 | EBI-6415666,EBI-6415578 |
Protein-protein interaction databases
IntActi | P37869, 2 interactors |
MINTi | P37869 |
STRINGi | 224308.BSU33900 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P37869 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 366 – 369 | Substrate bindingUniRule annotation | 4 |
Sequence similaritiesi
Belongs to the enolase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0148, Bacteria |
InParanoidi | P37869 |
OMAi | EFMIIPV |
PhylomeDBi | P37869 |
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
P37869-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE
60 70 80 90 100
LRDGDKDRYL GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT
110 120 130 140 150
ENKGKLGANA ILGVSMACAR AAADFLQIPL YQYLGGFNSK TLPVPMMNIV
160 170 180 190 200
NGGEHADNNV DIQEFMIMPV GAPNFREALR MGAQIFHSLK SVLSAKGLNT
210 220 230 240 250
AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA MDAASSEFYN
260 270 280 290 300
KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL
310 320 330 340 350
LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF
360 370 380 390 400
DAIEMAKRAG YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV
410 420 430
AKYNQLLRIE DQLAETAQYH GINSFYNLNK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 45 | E → Q in AAA21681 (PubMed:8021172).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L29475 Genomic DNA Translation: AAA21681.1 AL009126 Genomic DNA Translation: CAB15395.1 |
PIRi | B69620 |
RefSeqi | NP_391270.1, NC_000964.3 WP_003228333.1, NZ_JNCM01000033.1 |
Genome annotation databases
EnsemblBacteriai | CAB15395; CAB15395; BSU_33900 |
GeneIDi | 938641 |
KEGGi | bsu:BSU33900 |
PATRICi | fig|224308.179.peg.3675 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L29475 Genomic DNA Translation: AAA21681.1 AL009126 Genomic DNA Translation: CAB15395.1 |
PIRi | B69620 |
RefSeqi | NP_391270.1, NC_000964.3 WP_003228333.1, NZ_JNCM01000033.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4A3R | X-ray | 2.20 | A/B/C/D | 1-430 | [»] | |
SMRi | P37869 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P37869, 2 interactors |
MINTi | P37869 |
STRINGi | 224308.BSU33900 |
PTM databases
iPTMneti | P37869 |
Proteomic databases
jPOSTi | P37869 |
PaxDbi | P37869 |
PRIDEi | P37869 |
Genome annotation databases
EnsemblBacteriai | CAB15395; CAB15395; BSU_33900 |
GeneIDi | 938641 |
KEGGi | bsu:BSU33900 |
PATRICi | fig|224308.179.peg.3675 |
Phylogenomic databases
eggNOGi | COG0148, Bacteria |
InParanoidi | P37869 |
OMAi | EFMIIPV |
PhylomeDBi | P37869 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00187 |
BioCyci | BSUB:BSU33900-MONOMER |
BRENDAi | 4.2.1.11, 658 |
SABIO-RKi | P37869 |
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 | ENO_BACSU | |
Accessioni | P37869Primary (citable) accession number: P37869 Secondary accession number(s): O32249 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 174 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families