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Protein

Enolase

Gene

eno

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.UniRule annotation

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2 (apgM2), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1 (apgM1)
  4. Enolase (eno)
  5. Pyruvate kinase (MJ0108)
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 sitei157SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei209Proton donorUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi285MagnesiumUniRule annotation1
Binding sitei285SubstrateUniRule annotation1
Metal bindingi310MagnesiumUniRule annotation1
Binding sitei310SubstrateUniRule annotation1
Active sitei335Proton acceptorUniRule annotation1
Binding sitei335Substrate (covalent); in inhibited formUniRule annotation1
Binding sitei386SubstrateUniRule annotation1

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:
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:MJ0232
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Secreted UniRule annotation
  • Cell surface UniRule annotation

  • 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; once secreted, it remains attached to the cell surface.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001340241 – 423EnolaseAdd BLAST423

Proteomic databases

PRIDEiQ60173.

Interactioni

Protein-protein interaction databases

STRINGi243232.MJ_0232.

Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Beta strandi6 – 16Combined sources11
Beta strandi22 – 30Combined sources9
Beta strandi35 – 39Combined sources5
Beta strandi48 – 50Combined sources3
Helixi60 – 63Combined sources4
Helixi67 – 75Combined sources9
Helixi77 – 81Combined sources5
Helixi89 – 100Combined sources12
Turni106 – 108Combined sources3
Helixi110 – 128Combined sources19
Helixi132 – 137Combined sources6
Beta strandi149 – 153Combined sources5
Turni156 – 158Combined sources3
Beta strandi159 – 161Combined sources3
Beta strandi163 – 170Combined sources8
Helixi177 – 199Combined sources23
Helixi219 – 233Combined sources15
Turni236 – 238Combined sources3
Beta strandi240 – 244Combined sources5
Helixi247 – 250Combined sources4
Beta strandi255 – 258Combined sources4
Beta strandi261 – 263Combined sources3
Helixi265 – 278Combined sources14
Beta strandi281 – 285Combined sources5
Helixi293 – 302Combined sources10
Beta strandi303 – 310Combined sources8
Turni311 – 315Combined sources5
Helixi317 – 326Combined sources10
Beta strandi330 – 334Combined sources5
Helixi336 – 339Combined sources4
Helixi342 – 353Combined sources12
Turni354 – 356Combined sources3
Beta strandi358 – 362Combined sources5
Helixi372 – 379Combined sources8
Beta strandi383 – 386Combined sources4
Helixi393 – 408Combined sources16
Beta strandi409 – 411Combined sources3
Helixi416 – 418Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA6X-ray1.85A/B1-423[»]
ProteinModelPortaliQ60173.
SMRiQ60173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60173.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni362 – 365Substrate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
InParanoidiQ60173.
KOiK01689.
OMAiEFMIIPV.
PhylomeDBiQ60173.

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.
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.

Q60173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDERFEIKDI VAREVIDSRG NPTVEVEVIT KGNGYGSAIV PSGASTGTHE
60 70 80 90 100
ALELRDKEKR FGGKGVLMAV ENVNSIIRPE ILGYDARMQR EIDTIMIELD
110 120 130 140 150
GTPNKSRLGA NAILAVSLAV AKAAAATAKI PLYKYLGGFN SYVMPVPMMN
160 170 180 190 200
VINGGKHAGN DLDLQEFMIM PVGATSISEA VRMGSEVYHV LKNVILEKYG
210 220 230 240 250
KNAVNVGDEG GFAPPLKTSR EALDLLTESV KKAGYEDEVV FALDAAASEF
260 270 280 290 300
YKDGYYYVEG KKLTREELLD YYKALVDEYP IVSIEDPFHE EDFEGFAMIT
310 320 330 340 350
KELDIQIVGD DLFVTNVERL RKGIEMKAAN ALLLKVNQIG TLSEAVDAAQ
360 370 380 390 400
LAFRNGYGVV VSHRSGETED TTIADLSVAL NSGQIKTGAP ARGERTAKYN
410 420
QLIRIEQELG LSKYAGRNFR CPF
Length:423
Mass (Da):46,298
Last modified:February 21, 2001 - v2
Checksum:i9C9BB163E64BF577
GO

Sequence cautioni

The sequence AAB98220 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98220.1. Different initiation.
PIRiA64329.
RefSeqiWP_064496902.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98220; AAB98220; MJ_0232.
GeneIDi1451085.
KEGGimja:MJ_0232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98220.1. Different initiation.
PIRiA64329.
RefSeqiWP_064496902.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA6X-ray1.85A/B1-423[»]
ProteinModelPortaliQ60173.
SMRiQ60173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0232.

Proteomic databases

PRIDEiQ60173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98220; AAB98220; MJ_0232.
GeneIDi1451085.
KEGGimja:MJ_0232.

Phylogenomic databases

eggNOGiarCOG01169. Archaea.
COG0148. LUCA.
InParanoidiQ60173.
KOiK01689.
OMAiEFMIIPV.
PhylomeDBiQ60173.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

Miscellaneous databases

EvolutionaryTraceiQ60173.

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.
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 nameiENO_METJA
AccessioniPrimary (citable) accession number: Q60173
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: November 2, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.