Q5JEV6 (ENO_PYRKO) 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:	TK2106

Organism

Pyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Thermococcus kodakaraensis (strain KOD1))

Taxonomic identifier

69014 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length	430 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 MF_00318
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP 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 MF_00318
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP 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 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 Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro 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 – 430	430	Enolase HAMAP MF_00318		PRO_0000134033
Regions
	Region	367 – 370	4	Substrate binding By similarity
Sites
	Active site	208	1	Proton donor By similarity
	Active site	340	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	288	1	Magnesium By similarity
	Metal binding	315	1	Magnesium By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	315	1	Substrate By similarity
	Binding site	340	1	Substrate (covalent); in inhibited form By similarity
	Binding site	391	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5JEV6 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 1CFF5D3C2D38257E	FASTA	430	46,792
	10 20 30 40 50 60 MENPFEITNV IAREILDSRG NPTVEVEVYT PISMGRAAVP SGASTGTHEA LELRDGGSRY 70 80 90 100 110 120 HGKGVRRAVE NVNKIIAPEI IGMDVTWQRD IDTLMLELDG TENKSNLGAN AILGVSLAVA 130 140 150 160 170 180 KAAANALGLP LYQYIGGTNA YVMPVPMSNV INGGVHAGNE LDFQEFMIMP VGADSFREAI 190 200 210 220 230 240 RWVSETYHVL KKVIMEKYGR NAVNVGDEGG FAPPMKEVTE PLDVLIKAIE EAGYKPGDEI 250 260 270 280 290 300 AFALDAASSE FFDGEKGKYV VAGKEYDKGE LLELYRELVT TYPIVSIEDP FHEEDWEGFV 310 320 330 340 350 360 MITKELGSKV QIVGDDLFVT NPKRIRKGIE MGAANALLLK VNQIGTLSEA IDAAYTSFRA 370 380 390 400 410 420 GYGVVVSHRS GETEDATIAD LAVALNAGQI KTGAPARSDR NAKYNQLIRI EEELEGIAVY 430 PGKKFRNPFL

References

[1]

"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes." Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T. Genome Res. 15:352-363(2005) [PubMed: 15710748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006878 Genomic DNA. Translation: BAD86295.1.
RefSeq	YP_184519.1. NC_006624.1.
3D structure databases
ProteinModelPortal	Q5JEV6.
SMR	Q5JEV6. Positions 1-429.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000006987; EBPYRP00000006768; EBPYRG00000006986.
GeneID	3233916.
GenomeReviews	Gene locus TK2106 in contig AP006878_GR.
KEGG	tko:TK2106.
NMPDR	fig|69014.3.peg.2107.
Phylogenomic databases
eggNOG	arNOG04113.
GeneTree	EBGT00050000022630.
HOGENOM	HBG726599.
OMA	QAVDHIN.
PhylomeDB	Q5JEV6.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	TKOD69014:TK2106-MONOMER.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
KO	K01689.
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.
TIGRFAMs	TIGR01060. Eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO_PYRKO

Accession

Primary (citable) accession number: Q5JEV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	February 15, 2005
Last modified:	November 16, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program