Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei157 – 1571SubstrateUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei209 – 2091Proton donorUniRule annotation
Metal bindingi244 – 2441MagnesiumUniRule annotation
Metal bindingi285 – 2851MagnesiumUniRule annotation
Binding sitei285 – 2851SubstrateUniRule annotation
Metal bindingi310 – 3101MagnesiumUniRule annotation
Binding sitei310 – 3101SubstrateUniRule annotation
Active sitei335 – 3351Proton acceptorUniRule annotation
Binding sitei335 – 3351Substrate (covalent); in inhibited formUniRule annotation
Binding sitei386 – 3861SubstrateUniRule annotation

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423EnolasePRO_0000134024Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243232.MJ_0232.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi6 – 1611Combined sources
Beta strandi22 – 309Combined sources
Beta strandi35 – 395Combined sources
Beta strandi48 – 503Combined sources
Helixi60 – 634Combined sources
Helixi67 – 759Combined sources
Helixi77 – 815Combined sources
Helixi89 – 10012Combined sources
Turni106 – 1083Combined sources
Helixi110 – 12819Combined sources
Helixi132 – 1376Combined sources
Beta strandi149 – 1535Combined sources
Turni156 – 1583Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi163 – 1708Combined sources
Helixi177 – 19923Combined sources
Helixi219 – 23315Combined sources
Turni236 – 2383Combined sources
Beta strandi240 – 2445Combined sources
Helixi247 – 2504Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi261 – 2633Combined sources
Helixi265 – 27814Combined sources
Beta strandi281 – 2855Combined sources
Helixi293 – 30210Combined sources
Beta strandi303 – 3108Combined sources
Turni311 – 3155Combined sources
Helixi317 – 32610Combined sources
Beta strandi330 – 3345Combined sources
Helixi336 – 3394Combined sources
Helixi342 – 35312Combined sources
Turni354 – 3563Combined sources
Beta strandi358 – 3625Combined sources
Helixi372 – 3798Combined sources
Beta strandi383 – 3864Combined sources
Helixi393 – 40816Combined sources
Beta strandi409 – 4113Combined sources
Helixi416 – 4183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA6X-ray1.85A/B1-423[»]
ProteinModelPortaliQ60173.
SMRiQ60173. Positions 1-423.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60173.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni362 – 3654Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the enolase family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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 AAB98220.1 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.

Genome annotation databases

EnsemblBacteriaiAAB98220; AAB98220; MJ_0232.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA6X-ray1.85A/B1-423[»]
ProteinModelPortaliQ60173.
SMRiQ60173. Positions 1-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98220; AAB98220; MJ_0232.
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

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

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: May 11, 2016
This is version 113 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.