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Protein

Enolase

Gene
N/A
Organism
Homarus gammarus (European lobster) (Homarus vulgaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

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 sitei36Substrate1
Binding sitei157Substrate1
Binding sitei166Substrate1
Active sitei209Proton donorBy similarity1
Metal bindingi244Magnesium1
Metal bindingi294Magnesium1
Binding sitei294Substrate1
Metal bindingi319Magnesium1
Binding sitei319Substrate1
Active sitei344Proton acceptorBy similarity1
Binding sitei344Substrate1
Binding sitei374Substrate1
Binding sitei395Substrate1

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
OrganismiHomarus gammarus (European lobster) (Homarus vulgaris)
Taxonomic identifieri6707 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaNephropoideaNephropidaeHomarus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001340851 – 433EnolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylserine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP56252.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi17 – 25Combined sources9
Beta strandi28 – 33Combined sources6
Beta strandi38 – 40Combined sources3
Beta strandi42 – 44Combined sources3
Helixi56 – 58Combined sources3
Helixi62 – 70Combined sources9
Helixi72 – 79Combined sources8
Helixi86 – 97Combined sources12
Beta strandi99 – 102Combined sources4
Turni103 – 105Combined sources3
Helixi107 – 124Combined sources18
Helixi129 – 136Combined sources8
Beta strandi149 – 153Combined sources5
Beta strandi155 – 158Combined sources4
Beta strandi166 – 170Combined sources5
Helixi177 – 199Combined sources23
Helixi201 – 204Combined sources4
Helixi219 – 233Combined sources15
Beta strandi239 – 244Combined sources6
Turni247 – 250Combined sources4
Helixi259 – 261Combined sources3
Beta strandi263 – 265Combined sources3
Turni267 – 270Combined sources4
Helixi274 – 287Combined sources14
Beta strandi290 – 294Combined sources5
Helixi302 – 311Combined sources10
Beta strandi313 – 319Combined sources7
Turni320 – 324Combined sources5
Helixi326 – 334Combined sources9
Beta strandi339 – 343Combined sources5
Helixi345 – 348Combined sources4
Helixi351 – 363Combined sources13
Beta strandi367 – 371Combined sources5
Helixi381 – 388Combined sources8
Beta strandi393 – 395Combined sources3
Helixi402 – 418Combined sources17
Helixi419 – 421Combined sources3
Helixi426 – 428Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PDYX-ray2.40A1-433[»]
1PDZX-ray2.20A1-433[»]
ProteinModelPortaliP56252.
SMRiP56252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56252.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 374Substrate binding4

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: Complete.

P56252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SITKVFARTI FDSRGNPTVE VDLYTSKGLF RAAVPSGAST GVHEALEMRD
60 70 80 90 100
GDKSKYHGKS VFNAVKNVND VIVPEIIKSG LKVTQQKECD EFMCKLDGTE
110 120 130 140 150
NKSSLGANAI LGVSLAICKA GAAELGIPLY RHIANLANYD EVILPVPAFN
160 170 180 190 200
VINGGSHAGN KLAMQEFMIL PTGATSFTEA MRMGTEVYHH LKAVIKARFG
210 220 230 240 250
LDATAVGDEG GFAPNILNNK DALDLIQEAI KKAGYTGKIE IGMDVAASEF
260 270 280 290 300
YKQNNIYDLD FKTANNDGSQ KISGDQLRDM YMEFCKDFPI VSIEDPFDQD
310 320 330 340 350
DWETWSKMTS GTTIQIVGDD LTVTNPKRIT TAVEKKACKC LLLKVNQIGS
360 370 380 390 400
VTESIDAHLL AKKNGWGTMV SHRSGETEDC FIADLVVGLC TGQIKTGAPC
410 420 430
RSERLAKYNQ ILRIEEELGS GAKFAGKNFR APS
Length:433
Mass (Da):47,042
Last modified:July 15, 1998 - v1
Checksum:iCC7DA44B67E9DE3D
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PDYX-ray2.40A1-433[»]
1PDZX-ray2.20A1-433[»]
ProteinModelPortaliP56252.
SMRiP56252.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP56252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

Miscellaneous databases

EvolutionaryTraceiP56252.

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_HOMGA
AccessioniPrimary (citable) accession number: P56252
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 12, 2017
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.