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UniProtKB/Swiss-Prot entry P51555

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ENO1_ENTHI
Primary accession number P51555
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Enolase 1
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase
2-phospho-D-glycerate hydro-lyase
Gene name
Name: ENL-1
From
Entamoeba histolytica [TaxID: 5759] 
Taxonomy Eukaryota; Amoebozoa; Archamoebae; Entamoebidae; Entamoeba.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=HM-1:IMSS;
DOI=10.1016/0166-6851(94)00201-W; PubMed=7723780 [NCBI, ExPASy, EBI, Israel, Japan]
Beanan M.J., Bailey G.B.;
"The primary structure of an Entamoeba histolytica enolase.";
Mol. Biochem. Parasitol. 69:119-121(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U09736; AAA80166.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q9NDH8; 1OEP. [HSSP ENTRY / PDB]
ModBase P51555.
Ontologies
GO
GO:0000015; Cellular component: phosphopyruvate hydratase complex (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
Other
ProtoNet P51555.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   436  436     Enolase 1. PRO_0000134080
REGION   374   377  4     Substrate binding (By similarity). 
ACT_SITE   208   208        Proton donor (By similarity). 
ACT_SITE   347   347        Proton acceptor (By similarity). 
METAL   243   243        Magnesium (By similarity). 
METAL   296   296        Magnesium (By similarity). 
METAL   322   322        Magnesium (By similarity). 
BINDING   156   156        Substrate (By similarity). 
BINDING   165   165        Substrate (By similarity). 
BINDING   296   296        Substrate (By similarity). 
BINDING   322   322        Substrate (By similarity). 
BINDING   398   398        Substrate (By similarity). 
Sequence information
Length: 436 AA [This is the length of the unprocessed precursor] Molecular weight: 47327 Da [This is the MW of the unprocessed precursor] CRC64: BFBA693A65B44289 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSIQKVHARE ILDSRGNPTI EVEITTGKGM FRSCVPSGAS TGVHEAVELR DGDKKRYGGK 

        70         80         90        100        110        120 
GVLKAVENVN TIIGPALLGK NVLNQAELDE MMIKLDGTNN KGKLGANAIL GCSMSICRAA 

       130        140        150        160        170        180 
AAEKGLPLYK YLAELTGHKE MTMPVPCFNV INGGAHAGNA LAMQEFMICP TGATNFHEAL 

       190        200        210        220        230        240 
RMAAETYQCL KVVIKAKYGQ DATNVGDEGG FAPNVSGARE ALDLLVEAIA KAGYTGKIEI 

       250        260        270        280        290        300 
AMDCAASEFY NEETKKYDLG KKIPADKKDP SLVKDVDGLI AEYVDYGKHY PIASIEDPFA 

       310        320        330        340        350        360 
EDDWAAWNKF TVEHGNFQIV GDDLLVTNPA RVQMAMDKNA CNSVLIKVNQ IGTLTETFKT 

       370        380        390        400        410        420 
IKMAQEKGWG VMASHRSGET EDTFIADLVV GLNCKQIKTG APCRSERLCK YNQLMRIEEE 

       430 
LGNIPYAGKN WRNSTA
P51555 in FASTA format

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