Reviewed, UniProtKB/Swiss-Prot Q6FQY4 (ENO2_CANGA)

Names and origin

Protein names

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

Gene names

Name:	ENO2
Ordered Locus Names:	CAGL0I02486g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Glycolysis
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
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 – 437	437	Enolase 2		PRO_0000134045
Regions
	Region	373 – 376	4	Substrate binding By similarity
Sites
	Active site	212	1	Proton donor By similarity
	Active site	346	1	Proton acceptor By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Metal binding	321	1	Magnesium By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	169	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	321	1	Substrate By similarity
	Binding site	397	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FQY4-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: D8DAE343A84EB6B1	FASTA	437	46,739
	10 20 30 40 50 60 MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGIHEALEMR DGDKSKWLGK 70 80 90 100 110 120 GVENAVKNVN DVIAPAFVKA NVDIKDQKAV DDLLLSLDGT ANKSKLGANA ILGVSMAAAR 130 140 150 160 170 180 AAAAEKNVPL YQHLADLSDS KTSPFVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKSF 190 200 210 220 230 240 REAMRIGSEV YHNLKSLTKK RYGSSAGNVG DEGGVAPDIQ TAEEALDLIV DAIKAAGHEG 250 260 270 280 290 300 KVKIGLDCAS SEFFKDGKYD LDFKNPNSDA SKWLSGPQLA DLYHSLVKKY PIVSIEDPFA 310 320 330 340 350 360 EDDWEAWSHF FKTAGVQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GSLSESIKAA 370 380 390 400 410 420 QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 430 GDKAVYAGDN FHHGFKL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380955 Genomic DNA. Translation: CAG60297.1.
RefSeq	XP_447360.1.
3D structure databases
SMR	Q6FQY4. Positions 2-437.
ModBase	Search...
Genome annotation databases
GeneID	2889384.
KEGG	cgr:CAGL0I02486g.
Phylogenomic databases
HOGENOM	Q6FQY4.
OMA	Q6FQY4. SDSSKWL.
Enzyme and pathway databases
BRENDA	4.2.1.11. 189220.
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

ENO2_CANGA

Accession

Primary (citable) accession number: Q6FQY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)