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Protein

Enolase 2

Gene

ENO2

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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 1 (GPD1), Glyceraldehyde-3-phosphate dehydrogenase 2 (GPD2)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase (GPM1), Phosphoglycerate mutase (CAGL0K01705g)
  4. Enolase 1 (ENO1), Enolase 2 (ENO2)
  5. Pyruvate kinase 2 (PYK2), Pyruvate kinase 1 (PYK1)
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 sitei160SubstrateBy similarity1
Binding sitei169SubstrateBy similarity1
Active sitei212Proton donorBy similarity1
Metal bindingi247MagnesiumBy similarity1
Metal bindingi296MagnesiumBy similarity1
Binding sitei296SubstrateBy similarity1
Metal bindingi321MagnesiumBy similarity1
Binding sitei321SubstrateBy similarity1
Active sitei346Proton acceptorBy similarity1
Binding sitei397SubstrateBy similarity1

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 2 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2
2-phosphoglycerate dehydratase 2
Gene namesi
Name:ENO2
Ordered Locus Names:CAGL0I02486g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
Proteomesi
  • UP000002428 Componenti: Chromosome I

Organism-specific databases

CGDiCAL0130514. ENO1.
EuPathDBiFungiDB:CAGL0I02486g.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001340451 – 437Enolase 2Add BLAST437

Proteomic databases

PRIDEiQ6FQY4.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi284593.XP_447360.1.

Structurei

3D structure databases

ProteinModelPortaliQ6FQY4.
SMRiQ6FQY4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni373 – 376Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
InParanoidiQ6FQY4.
KOiK01689.
OMAiEFMIIPV.
OrthoDBiEOG092C2W5X.

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.

Q6FQY4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGIHEALEMR
60 70 80 90 100
DGDKSKWLGK GVENAVKNVN DVIAPAFVKA NVDIKDQKAV DDLLLSLDGT
110 120 130 140 150
ANKSKLGANA ILGVSMAAAR AAAAEKNVPL YQHLADLSDS KTSPFVLPVP
160 170 180 190 200
FLNVLNGGSH AGGALALQEF MIAPTGAKSF REAMRIGSEV YHNLKSLTKK
210 220 230 240 250
RYGSSAGNVG DEGGVAPDIQ TAEEALDLIV DAIKAAGHEG KVKIGLDCAS
260 270 280 290 300
SEFFKDGKYD LDFKNPNSDA SKWLSGPQLA DLYHSLVKKY PIVSIEDPFA
310 320 330 340 350
EDDWEAWSHF FKTAGVQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI
360 370 380 390 400
GSLSESIKAA QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA
410 420 430
PARSERLAKL NQLLRIEEEL GDKAVYAGDN FHHGFKL
Length:437
Mass (Da):46,739
Last modified:July 19, 2004 - v1
Checksum:iD8DAE343A84EB6B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380955 Genomic DNA. Translation: CAG60297.1.
RefSeqiXP_447360.1. XM_447360.1.

Genome annotation databases

EnsemblFungiiCAG60297; CAG60297; CAGL0I02486g.
GeneIDi2889384.
KEGGicgr:CAGL0I02486g.

Similar proteinsi

Entry informationi

Entry nameiENO2_CANGA
AccessioniPrimary (citable) accession number: Q6FQY4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2004
Last modified: September 27, 2017
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families