Reviewed, UniProtKB/Swiss-Prot P30575 (ENO1_CANAL)

Names and origin

Protein names

Recommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

Gene names

Name:	ENO1
ORF Names:	CaO19.395, CaO19.8025

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 440	440	Enolase 1		PRO_0000134043
Regions
	Region	376 – 379	4	Substrate binding By similarity
	Compositional bias	118 – 126	9	Poly-Ala
Sites
	Active site	213	1	Proton donor By similarity
	Active site	349	1	Proton acceptor By similarity
	Metal binding	248	1	Magnesium By similarity
	Metal binding	297	1	Magnesium By similarity
	Metal binding	324	1	Magnesium By similarity
	Binding site	161	1	Substrate By similarity
	Binding site	170	1	Substrate By similarity
	Binding site	297	1	Substrate By similarity
	Binding site	324	1	Substrate By similarity
	Binding site	400	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30575-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 6621AFD66F275C49	FASTA	440	47,232
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the Candida albicans enolase gene." Mason A.B., Buckley H.R., Gorman J.A. J. Bacteriol. 175:2632-2639(1993) [PubMed: 8478328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64385 / 1001.
[2]	"Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme." Sundstrom P., Aliaga G.R. J. Bacteriol. 174:6789-6799(1992) [PubMed: 1400228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning and nucleotide sequence analysis of the Candida albicans enolase gene." Franklyn K.M., Warmington J.R. FEMS Microbiol. Lett. 111:101-107(1993) [PubMed: 8359671] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: KEMH5.
[4]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L04943 Genomic DNA. Translation: AAB46358.1. M93712 mRNA. Translation: AAA34341.1. L10290 Genomic DNA. Translation: AAA71939.1. AACQ01000177 Genomic DNA. Translation: EAK92675.1. AACQ01000176 Genomic DNA. Translation: EAK92704.1.
PIR	A40624.
RefSeq	XP_711883.1. XP_711912.1.
3D structure databases
HSSP	HSSP built from PDB template 4ENL based on UniProtKB P00924.
SMR	P30575. Positions 5-440.
ModBase	Search...
2-D gel databases
COMPLUYEAST-2DPAGE	P30575.
Genome annotation databases
GeneID	3646484. 3646493.
Organism-specific databases
CGD	CAL0004953. ENO1.
Phylogenomic databases
OMA	P30575. SDSSKWL.
Enzyme and pathway databases
BRENDA	4.2.1.11. 1124.
Family and domain databases
InterPro	IPR000941. Enolase. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO1_CANAL

Accession

Primary (citable) accession number: P30575
Secondary accession number(s): Q59QC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)