Reviewed, UniProtKB/Swiss-Prot Q6BI20 (ENO2_DEBHA)

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:	DEHA0G14927g

Organism

Debaryomyces hansenii (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

4959 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	439 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 + H(2)O.
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	CytoplasmBy 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: InterPro
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 439	439	Enolase 2		PRO_0000134051
Regions
	Region	375 – 378	4	Substrate binding By similarity
Sites
	Active site	212	1	Proton donor By similarity
	Active site	348	1	Proton acceptor By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	296	1	Magnesium By similarity
	Metal binding	323	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	323	1	Substrate By similarity
	Binding site	399	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6BI20-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 434D235716664DB9	FASTA	439	47,239
	10 20 30 40 50 60 MAVTKLFARY VYDSRGNPTV EVDLTTDKGL FRSIVPSGAS TGIHEALELR DGDKSKWLGK 70 80 90 100 110 120 GVTKAVANVN ELIAPAFVKA NLDVTNQSAV DDFLNKLDGT PNKSKLGANA ILGVSLATAK 130 140 150 160 170 180 AAAAEKNVPL YQHLADISGS KQDKFVLPVP FQNVLNGGSH AGGALAFQEF MIVPTDAPTF 190 200 210 220 230 240 SEALRMGSEV YHNLKSLTKK KYGQSAGNVG DEGGVAPDIG SPREALDLIM DAIDKAGYKG 250 260 270 280 290 300 KIGIALDVAA SEFYKDGKYD LDFKNPNSDE SKWLSGEQLA SLYEELINEY PIVSIEDPFG 310 320 330 340 350 360 EDDWDAWVHF YSKVSSKVQI VGDDLTVTNP LRIKTAIEKK AANALLLKVN QIGSLTESIK 370 380 390 400 410 420 AAQDSFDATW GVMVSHRSGE TEDTFIADLS VGLRAGQIKT GAPARSERLA KLNQILRIEE 430 ELGDKAIYAG KNFHAASQL

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 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR382139 Genomic DNA. Translation: CAG90637.1.
RefSeq	XP_462151.1.
3D structure databases
SMR	Q6BI20. Positions 2-439.
ModBase	Search...
Genome annotation databases
GeneID	2905065.
KEGG	dha:DEHA0G14927g.
Phylogenomic databases
HOGENOM	Q6BI20.
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_DEBHA

Accession

Primary (citable) accession number: Q6BI20

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)