Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6BTB1 (ENO1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:DEHA2D02112g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length439 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-KW

   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 – 439439Enolase 1
PRO_0000134050

Regions

Region375 – 3784Substrate binding By similarity

Sites

Active site2121Proton donor By similarity
Active site3481Proton acceptor By similarity
Metal binding2471Magnesium By similarity
Metal binding2961Magnesium By similarity
Metal binding3231Magnesium By similarity
Binding site1601Substrate By similarity
Binding site1691Substrate By similarity
Binding site2961Substrate By similarity
Binding site3231Substrate By similarity
Binding site3991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6BTB1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 952B68D40BDDE285

FASTA43947,578
        10         20         30         40         50         60 
MTISKVHSRY VYDSRGNPTV EVDVTTENGL FRAIVPSGAS TGINEAMELR DGDKSKWQGK 

        70         80         90        100        110        120 
GVTKAVDNVN KTIAPHLIKS GLDEKNQEEI DSFLLKLDGT PNKRSLGANA ILGVSLAVAK 

       130        140        150        160        170        180 
AGAAAKQVPL YRHIADISKS KQDKYVLPVP FQNVLNGGSH AGGSLAFQEF MIAPTNAPSF 

       190        200        210        220        230        240 
SEALRIGSEV YHHLKSLTKS KYGQSAGNVG DEGGVAPDIE TPEEALDLIV ASIEKAGYKG 

       250        260        270        280        290        300 
KVSIALDVAS SEFYKDGKYD LDFKNPNSDK SKWLSGDQLA DLYESLIDNY PIISIEDPFS 

       310        320        330        340        350        360 
EEDWDAWSNF YPKVASKLQI VGDDLTVTNP IFIKKAIEKK AANALLLKVN QIGTLTESIK 

       370        380        390        400        410        420 
AAQLAFSDKW GVMVSHRSGE TEDHIIADIV VGLRTGQIKT GAPSRSERLA KLNQILRIEQ 

       430 
ELGDDAVYSG KGFHTAQNL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR382136 Genomic DNA. Translation: CAG86691.1.
RefSeqXP_458559.1. XM_458559.1.

3D structure databases

ProteinModelPortalQ6BTB1.
SMRQ6BTB1. Positions 3-439.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6BTB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2901509.
GenomeReviewsGene locus DEHA2D02112g in contig CR382136_GR.
KEGGdha:DEHA2D02112g.

Phylogenomic databases

eggNOGfuNOG04478.
HOGENOMHBG726599.
OMARHIADIS.
OrthoDBEOG48WG9D.

Family and domain databases

InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
KOK01689.
PANTHERPTHR11902. Enolase. 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_DEBHA
AccessionPrimary (citable) accession number: Q6BTB1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 16, 2004
Last modified: December 14, 2011
This is version 57 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents