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Protein

Enolase 1

Gene

ENO1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Glyceraldehyde-3-phosphate dehydrogenase (TDH3)
  2. Phosphoglycerate kinase (PGK1)
  3. Phosphoglycerate mutase (GPM1)
  4. Enolase 1 (ENO1)
  5. Pyruvate kinase (I503_01989), Pyruvate kinase (CDC19)
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 sitei161 – 1611SubstrateBy similarity
Binding sitei170 – 1701SubstrateBy similarity
Active sitei213 – 2131Proton donorBy similarity
Metal bindingi248 – 2481MagnesiumBy similarity
Metal bindingi297 – 2971MagnesiumBy similarity
Binding sitei297 – 2971SubstrateBy similarity
Metal bindingi324 – 3241MagnesiumBy similarity
Binding sitei324 – 3241SubstrateBy similarity
Active sitei349 – 3491Proton acceptorBy similarity
Binding sitei400 – 4001SubstrateBy similarity

GO - Molecular functioni

  • high molecular weight kininogen binding Source: CGD
  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: CGD

GO - Biological processi

  • entry into host Source: CGD
  • filamentous growth Source: CGD
  • filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
  • gluconeogenesis Source: CGD
  • glycolytic process Source: CGD
  • induction by symbiont of host defense response Source: CGD
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 1 (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase
Gene namesi
Name:ENO1
ORF Names:CaO19.395, CaO19.8025
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000185645. ENO1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: CGD
  • cytosol Source: CGD
  • extracellular region Source: CGD
  • fungal-type cell wall Source: CGD
  • hyphal cell wall Source: CGD
  • intracellular Source: CGD
  • membrane Source: CGD
  • nucleus Source: CGD
  • phosphopyruvate hydratase complex Source: CGD
  • plasma membrane Source: CGD
  • yeast-form cell wall Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Protein family/group databases

Allergomei785. Cand a Enolase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Enolase 1PRO_0000134043Add
BLAST

Proteomic databases

PRIDEiP30575.

2D gel databases

COMPLUYEAST-2DPAGEP30575.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • high molecular weight kininogen binding Source: CGD

Protein-protein interaction databases

BioGridi1229577. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP30575.
SMRiP30575. Positions 5-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni376 – 3794Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 1269Poly-Ala

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

InParanoidiP30575.
KOiK01689.
OrthoDBiEOG7JHMFP.

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.

P30575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYATKIHAR YVYDSRGNPT VEVDFTTDKG LFRSIVPSGA STGVHEALEL
60 70 80 90 100
RDGDKSKWLG KGVLKAVANV NDIIAPALIK AKIDVVDQAK IDEFLLSLDG
110 120 130 140 150
TPNKSKLGAN AILGVSLAAA NAAAAAQGIP LYKHIANISN AKKGKFVLPV
160 170 180 190 200
PFQNVLNGGS HAGGALAFQE FMIAPTGVST FSEALRIGSE VYHNLKSLTK
210 220 230 240 250
KKYGQSAGNV GDEGGVAPDI KTPKEALDLI MDAIDKAGYK GKVGIAMDVA
260 270 280 290 300
SSEFYKDGKY DLDFKNPESD PSKWLSGPQL ADLYEQLISE YPIVSIEDPF
310 320 330 340 350
AEDDWDAWVH FFERVGDKIQ IVGDDLTVTN PTRIKTAIEK KAANALLLKV
360 370 380 390 400
NQIGTLTESI QAANDSYAAG WGVMVSHRSG ETEDTFIADL SVGLRSGQIK
410 420 430 440
TGAPARSERL AKLNQILRIE EELGSEAIYA GKDFQKASQL
Length:440
Mass (Da):47,232
Last modified:April 1, 1993 - v1
Checksum:i6621AFD66F275C49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04943 Genomic DNA. Translation: AAB46358.1.
M93712 mRNA. Translation: AAA34341.1.
L10290 Genomic DNA. Translation: AAA71939.1.
AACQ01000177 Genomic DNA. Translation: EAK92675.1.
AACQ01000176 Genomic DNA. Translation: EAK92704.1.
PIRiA40624.
RefSeqiXP_711883.1. XM_706790.1.
XP_711912.1. XM_706819.1.

Genome annotation databases

EnsemblFungiiEAK92675; EAK92675; CaO19.395.
EAK92704; EAK92704; CaO19.8025.
GeneIDi3646484.
3646493.
KEGGical:CaO19.395.
cal:CaO19.8025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04943 Genomic DNA. Translation: AAB46358.1.
M93712 mRNA. Translation: AAA34341.1.
L10290 Genomic DNA. Translation: AAA71939.1.
AACQ01000177 Genomic DNA. Translation: EAK92675.1.
AACQ01000176 Genomic DNA. Translation: EAK92704.1.
PIRiA40624.
RefSeqiXP_711883.1. XM_706790.1.
XP_711912.1. XM_706819.1.

3D structure databases

ProteinModelPortaliP30575.
SMRiP30575. Positions 5-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1229577. 1 interaction.

Protein family/group databases

Allergomei785. Cand a Enolase.

2D gel databases

COMPLUYEAST-2DPAGEP30575.

Proteomic databases

PRIDEiP30575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK92675; EAK92675; CaO19.395.
EAK92704; EAK92704; CaO19.8025.
GeneIDi3646484.
3646493.
KEGGical:CaO19.395.
cal:CaO19.8025.

Organism-specific databases

CGDiCAL0000185645. ENO1.

Phylogenomic databases

InParanoidiP30575.
KOiK01689.
OrthoDBiEOG7JHMFP.

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

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the Candida albicans enolase gene."
    Mason A.B., Buckley H.R., Gorman J.A.
    J. Bacteriol. 175:2632-2639(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 64385 / 1001.
  2. "Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme."
    Sundstrom P., Aliaga G.R.
    J. Bacteriol. 174:6789-6799(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and nucleotide sequence analysis of the Candida albicans enolase gene."
    Franklyn K.M., Warmington J.R.
    FEMS Microbiol. Lett. 111:101-107(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KEMH5.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.

Entry informationi

Entry nameiENO1_CANAL
AccessioniPrimary (citable) accession number: P30575
Secondary accession number(s): Q59QC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 11, 2016
This is version 119 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

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.