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Q6FTW6 (ENO1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Enolase 1
EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase 1
2-phosphoglycerate dehydratase 1
Gene names
Name:ENO1
Ordered Locus Names:CAGL0F08261g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer By similarity.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Enolase 1
PRO_0000134044

Regions

Region373 – 3764Substrate binding By similarity

Sites

Active site2121Proton donor By similarity
Active site3461Proton acceptor By similarity
Metal binding2471Magnesium By similarity
Metal binding2961Magnesium By similarity
Metal binding3211Magnesium By similarity
Binding site1601Substrate By similarity
Binding site1691Substrate By similarity
Binding site2961Substrate By similarity
Binding site3211Substrate By similarity
Binding site3971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FTW6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: A5C39636C234E43E

FASTA43847,282
        10         20         30         40         50         60 
MSVTKVHART VYDSRGNPTV EVEVYTKDGM FRAIVPSGAS TGSHEALELR DGDKSKWEGK 

        70         80         90        100        110        120 
GVTKAVSNVN DIIGPKLIES KLDVKDQKAI DEFMIKLDGT KNKSKLGANA ILGVSLAVAR 

       130        140        150        160        170        180 
AGAAAKGVPL YQHIAELADM KKEPYVIPCP FFNVLNGGVH AGGNLALQEF LIAPVGAESF 

       190        200        210        220        230        240 
HEALRLGSEV YHKLKALAKK RIGSSAGNVG DEGGIAPSLS TPFEALDLIY DAIKEAGHEG 

       250        260        270        280        290        300 
KVKIAMDPAS SEFFQGDKYD LDFKNPHPDA KNKLSGAQLG DYYKTILEKY PIVSLEDPFA 

       310        320        330        340        350        360 
EDDWEAWTNF FPKAGVQIIA DDLTVTNPER IQTAIDKKTA DCLLLKVNQI GSLTESINSA 

       370        380        390        400        410        420 
KLAYGAGWGV QVSHRSGETE DTFIADLVVG LRTGQIKSGS LARSERLAKW NQILRIEEEL 

       430 
GASNTIFAGA KFHKGQLL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380952 Genomic DNA. Translation: CAG59252.1.
RefSeqXP_446328.1. XM_446328.1.

3D structure databases

ProteinModelPortalQ6FTW6.
SMRQ6FTW6. Positions 2-438.
ModBaseSearch...

Proteomic databases

PRIDEQ6FTW6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2887972.
KEGGcgr:CAGL0F08261g.

Phylogenomic databases

HOGENOMHOG000072174.
KOK01689.
OMAYLGGCFA.
OrthoDBEOG48WG9D.

Enzyme and pathway databases

UniPathwayUPA00109; UER00187.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENO1_CANGA
AccessionPrimary (citable) accession number: Q6FTW6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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