Reviewed, UniProtKB/Swiss-Prot Q6BTB1 (ENO1_DEBHA)

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:	DEHA2D02112g

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 + 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 – 439	439	Enolase 1		PRO_0000134050
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)
	Q6BTB1-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 952B68D40BDDE285	FASTA	439	47,578
	10 20 30 40 50 60 MTISKVHSRY VYDSRGNPTV EVDVTTENGL FRAIVPSGAS TGINEAMELR DGDKSKWQGK 70 80 90 100 110 120 GVTKAVDNVN KTIAPHLIKS GLDEKNQEEI DSFLLKLDGT PNKRSLGANA ILGVSLAVAK 130 140 150 160 170 180 AGAAAKQVPL YRHIADISKS KQDKYVLPVP FQNVLNGGSH AGGSLAFQEF MIAPTNAPSF 190 200 210 220 230 240 SEALRIGSEV YHHLKSLTKS KYGQSAGNVG DEGGVAPDIE TPEEALDLIV ASIEKAGYKG 250 260 270 280 290 300 KVSIALDVAS SEFYKDGKYD LDFKNPNSDK SKWLSGDQLA DLYESLIDNY PIISIEDPFS 310 320 330 340 350 360 EEDWDAWSNF YPKVASKLQI VGDDLTVTNP IFIKKAIEKK AANALLLKVN QIGTLTESIK 370 380 390 400 410 420 AAQLAFSDKW GVMVSHRSGE TEDHIIADIV VGLRTGQIKT GAPSRSERLA KLNQILRIEQ 430 ELGDDAVYSG KGFHTAQNL

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	CR382136 Genomic DNA. Translation: CAG86691.1.
RefSeq	XP_458559.1.
3D structure databases
SMR	Q6BTB1. Positions 3-439.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BTB1.
Genome annotation databases
GeneID	2901509.
GenomeReviews	Gene locus DEHA2D02112g in contig CR382136_GR.
KEGG	dha:DEHA0D02805g.
Phylogenomic databases
HOGENOM	Q6BTB1.
OMA	INDTIAP.
Enzyme and pathway databases
BRENDA	4.2.1.11. 74267.
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_DEBHA

Accession

Primary (citable) accession number: Q6BTB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)