[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 64385 / 1001; PubMed=8478328 [NCBI, ExPASy, EBI, Israel, Japan] Mason A.B., Buckley H.R., Gorman J.A.; "Molecular cloning and characterization of the Candida albicans enolase gene."; J. Bacteriol. 175:2632-2639(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1400228 [NCBI, ExPASy, EBI, Israel, Japan] Sundstrom P., Aliaga G.R.; "Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme."; J. Bacteriol. 174:6789-6799(1992).
[3]	NUCLEOTIDE SEQUENCE. STRAIN=KEMH5; DOI=10.1016/0378-1097(93)90189-9; PubMed=8359671 [NCBI, ExPASy, EBI, Israel, Japan] Franklyn K.M., Warmington J.R.; "Cloning and nucleotide sequence analysis of the Candida albicans enolase gene."; FEMS Microbiol. Lett. 111:101-107(1993).

Comments

CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

L04943; AAB46358.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M93712; AAA34341.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L10290; AAA71939.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40624; A40624.

3D structure databases

HSSP

P00924; 4ENL. [HSSP ENTRY / PDB]

P30575; 5-440.

2D gel databases

P30575; -.

Organism-specific databases

CGD

CAL0004953; ENO1.

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`	`1 440`	`440`	`Enolase 1.`	`PRO_0000134043`
`REGION`	`376 379`	`4`	`Substrate binding (By similarity).`
`COMPBIAS`	`118 126`	`9`	`Poly-Ala.`
`ACT_SITE`	`213 213`		`Proton donor (By similarity).`
`ACT_SITE`	`349 349`		`Proton acceptor (By similarity).`
`METAL`	`248 248`		`Magnesium (By similarity).`
`METAL`	`297 297`		`Magnesium (By similarity).`
`METAL`	`324 324`		`Magnesium (By similarity).`
`BINDING`	`161 161`		`Substrate (By similarity).`
`BINDING`	`170 170`		`Substrate (By similarity).`
`BINDING`	`297 297`		`Substrate (By similarity).`
`BINDING`	`324 324`		`Substrate (By similarity).`
`BINDING`	`400 400`		`Substrate (By similarity).`

Sequence information

Length: 440 AA [This is the length of the unprocessed precursor]

Molecular weight: 47232 Da [This is the MW of the unprocessed precursor]

CRC64: 6621AFD66F275C49 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYATKIHAR YVYDSRGNPT VEVDFTTDKG LFRSIVPSGA STGVHEALEL RDGDKSKWLG 

        70         80         90        100        110        120 
KGVLKAVANV NDIIAPALIK AKIDVVDQAK IDEFLLSLDG TPNKSKLGAN AILGVSLAAA 

       130        140        150        160        170        180 
NAAAAAQGIP LYKHIANISN AKKGKFVLPV PFQNVLNGGS HAGGALAFQE FMIAPTGVST 

       190        200        210        220        230        240 
FSEALRIGSE VYHNLKSLTK KKYGQSAGNV GDEGGVAPDI KTPKEALDLI MDAIDKAGYK 

       250        260        270        280        290        300 
GKVGIAMDVA SSEFYKDGKY DLDFKNPESD PSKWLSGPQL ADLYEQLISE YPIVSIEDPF 

       310        320        330        340        350        360 
AEDDWDAWVH FFERVGDKIQ IVGDDLTVTN PTRIKTAIEK KAANALLLKV NQIGTLTESI 

       370        380        390        400        410        420 
QAANDSYAAG WGVMVSHRSG ETEDTFIADL SVGLRSGQIK TGAPARSERL AKLNQILRIE 

       430        440 
EELGSEAIYA GKDFQKASQL

P30575 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