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Protein

Enolase

Gene
N/A
Organism
Neocallimastix frontalis (Rumen fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Mg2+ is required for catalysis and for stabilizing the dimer.By similarity

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. Glyceraldehyde-3-phosphate dehydrogenase (GAP2), Glyceraldehyde-3-phosphate dehydrogenase (GAP1)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Enolase
  5. Pyruvate kinase (PK2)
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 sitei159 – 1591SubstrateBy similarity
Binding sitei168 – 1681SubstrateBy similarity
Active sitei211 – 2111Proton donorBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Metal bindingi295 – 2951MagnesiumBy similarity
Binding sitei295 – 2951SubstrateBy similarity
Metal bindingi322 – 3221MagnesiumBy similarity
Binding sitei322 – 3221SubstrateBy similarity
Active sitei347 – 3471Proton acceptorBy similarity
Binding sitei398 – 3981SubstrateBy similarity

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:
Enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
OrganismiNeocallimastix frontalis (Rumen fungus)
Taxonomic identifieri4757 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeNeocallimastix

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436EnolasePRO_0000134053Add
BLAST

Proteomic databases

PRIDEiP42894.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GE6model-A2-436[»]
ProteinModelPortaliP42894.
SMRiP42894. Positions 2-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 3774Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

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.

P42894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAITKVHARQ IFDSRGNPTV EVEVTTDKGL FRAAVPSGAS TGVHEALELR
60 70 80 90 100
DGIKADYVGK GVLKAVENVN KTIAPALVAA NLDVKNQKAV DDFLLKLDGT
110 120 130 140 150
PNKSKLGANA ILGVSLAVAR AGAADKGVPL YQHLGELAGN KGPWILPVPS
160 170 180 190 200
MNVLNGGSHA GNKLAMQEFM ILPTGAKSFT EALKMGSEVY HALKSVIKAK
210 220 230 240 250
YGQDACNVGD EGGFAPNIQD NKEGLELLNE AIAKAGYTGK VKIGMDVASS
260 270 280 290 300
EFYKDGKYDL DFKNPNSDPS KWISGEELGQ FYKEITSEYP IVSIEDPYDQ
310 320 330 340 350
DDFESWSKFR ADMQDKIQIV GDDLTVTNPK RIAMAIEKKA CNGLLLKVNQ
360 370 380 390 400
IGTVSESIQA ALDAFNDGWG VMVSHRSGET EDTFIADLVV GLKSGQIKTG
410 420 430
APCRSERLAK YNQLLRIEEE LGANATYAGE NFRRPF
Length:436
Mass (Da):47,017
Last modified:November 1, 1995 - v1
Checksum:i56EBD2FA1B722841
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80474 Genomic DNA. Translation: CAA56645.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80474 Genomic DNA. Translation: CAA56645.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GE6model-A2-436[»]
ProteinModelPortaliP42894.
SMRiP42894. Positions 2-435.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP42894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.

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. "Neocallimastix frontalis enolase gene, enol: first report of an intron in an anaerobic fungus."
    Durand R., Fischer M., Rascle C., Fevre M.
    Microbiology 141:1301-1308(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MCH3.

Entry informationi

Entry nameiENO_NEOFR
AccessioniPrimary (citable) accession number: P42894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.