[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

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: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the enolase family.

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:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
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]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From 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

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools