Reviewed, UniProtKB/Swiss-Prot Q6FTW6 (ENO1_CANGA)

Names and origin

Protein names

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

Gene names

Name:	ENO1
Ordered Locus Names:	CAGL0F08261g

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	438 AA.
Sequence status	Complete.
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 – 438	438	Enolase 1		PRO_0000134044
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)
	Q6FTW6-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A5C39636C234E43E	FASTA	438	47,282
	10 20 30 40 50 60 MSVTKVHART VYDSRGNPTV EVEVYTKDGM FRAIVPSGAS TGSHEALELR DGDKSKWEGK 70 80 90 100 110 120 GVTKAVSNVN DIIGPKLIES KLDVKDQKAI DEFMIKLDGT KNKSKLGANA ILGVSLAVAR 130 140 150 160 170 180 AGAAAKGVPL YQHIAELADM KKEPYVIPCP FFNVLNGGVH AGGNLALQEF LIAPVGAESF 190 200 210 220 230 240 HEALRLGSEV YHKLKALAKK RIGSSAGNVG DEGGIAPSLS TPFEALDLIY DAIKEAGHEG 250 260 270 280 290 300 KVKIAMDPAS SEFFQGDKYD LDFKNPHPDA KNKLSGAQLG DYYKTILEKY PIVSLEDPFA 310 320 330 340 350 360 EDDWEAWTNF FPKAGVQIIA DDLTVTNPER IQTAIDKKTA DCLLLKVNQI GSLTESINSA 370 380 390 400 410 420 KLAYGAGWGV QVSHRSGETE DTFIADLVVG LRTGQIKSGS LARSERLAKW NQILRIEEEL 430 GASNTIFAGA KFHKGQLL

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
EMBL GenBank DDBJ	CR380952 Genomic DNA. Translation: CAG59252.1.
RefSeq	XP_446328.1.
3D structure databases
SMR	Q6FTW6. Positions 2-438.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FTW6.
Genome annotation databases
GeneID	2887972.
GenomeReviews	Gene locus CAGL0F08261g in contig CR380952_GR.
KEGG	cgr:CAGL0F08261g.
Phylogenomic databases
eggNOG	fuNOG04478.
HOGENOM	HBG726599.
OMA	KVHARTV.
OrthoDB	EOG91G4M7.
PhylomeDB	Q6FTW6.
Enzyme and pathway databases
BRENDA	4.2.1.11. 189220.
Family and domain databases
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO1_CANGA

Accession

Primary (citable) accession number: Q6FTW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)