O59605 (ENO_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase

Gene names

Name:	eno
Ordered Locus Names:	PH1942

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus horikoshii

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis By similarity. HAMAP-Rule MF_00318
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer By similarity.
Enzyme regulation	The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein By similarity. HAMAP-Rule MF_00318
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318
Subcellular location	Cytoplasm. Secreted. Cell surface. Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the archaeal cell surface By similarity. HAMAP-Rule MF_00318
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 428	428	Enolase HAMAP-Rule MF_00318		PRO_0000134032
Regions
	Region	365 – 368	4	Substrate binding By similarity
Sites
	Active site	208	1	Proton donor By similarity
	Active site	338	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	286	1	Magnesium By similarity
	Metal binding	313	1	Magnesium By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	313	1	Substrate By similarity
	Binding site	338	1	Substrate (covalent); in inhibited form By similarity
	Binding site	389	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59605 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: BA91C397DBEAAC02	FASTA	428	46,697
	10 20 30 40 50 60 MENPYEITAI VAREILDSRG NPTVEVDVHT PIAMGRAAVP SGASTGTHEA VELRDGGKRY 70 80 90 100 110 120 HGKGVRRAVE NVNKIIAPEL IGMDVRWQRE IDKLLIELDG TENKSNLGAN AILAVSLAVA 130 140 150 160 170 180 KAAANSLELP LYQYLGGVNA YVLPVPLSNV INGGVHAGNE LDFQEFMIMP IGASSFREAI 190 200 210 220 230 240 RWVSETYHVL KRVIMGKYGK NAVNVGDEGG FAPPMKEVTE PLDALIKAIE EAGYKPGDEI 250 260 270 280 290 300 ALAIDAASSE FFKDGKYIVG GKEYTREELL DLYKELVSTY PIVSIEDPFH EEDWEGFVMI 310 320 330 340 350 360 TNELGKKIQI VGDDLFVTNP RRLKKGIELG AANALLLKVN QIGTLTEAMD AAYTAFRAGY 370 380 390 400 410 420 SVIVSHRSGE TEDTTIADLA VALNAGQIKT GAPARSDRNA KYNQLIRIEE ELEGIAVYAG KNFRKVFF

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA31069.1.
PIR	F71209.
RefSeq	NP_143772.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59605.
SMR	O59605. Positions 1-427.
ModBase	Search...
Protein-protein interaction databases
STRING	70601.PH1942.
Proteomic databases
PRIDE	O59605.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA31069; BAA31069; BAA31069.
GeneID	1442791.
KEGG	pho:PH1942.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HOG000072173.
KO	K01689.
OMA	EYMIMPL.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	PHOR70601:GJWR-1949-MONOMER.
UniPathway	UPA00109; UER00187.
Family and domain databases
HAMAP	MF_00318. Enolase.
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 1 hit.
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

ENO_PYRHO

Accession

Primary (citable) accession number: O59605

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program