Q8U477 (ENO_PYRFU) 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:	PF0215

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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_0000134031
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)
	Q8U477 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: CDC48BE361E32BC6	FASTA	430	46,835
	10 20 30 40 50 60 MENPYEIVGV VAREILDSRG NPTVEVDVYT HVGMGRAAVP SGASTGTHEA LELRDGGKRY 70 80 90 100 110 120 HGKGVRRAVE NVNKIIAPEL IGMDVRWQRE IDALLLELDG TENKSNVGAN AILAVSLAVA 130 140 150 160 170 180 KAAANSLELP LYQYLGGVNA YVLPVPLSNV INGGVHAGND LDFQEFMIMP IGADSFREAI 190 200 210 220 230 240 RWVSETYHVL KKVIMEKYGK NAVNVGDEGG FAPPMKEVTE PLDVLIKAIE EAGYKPGDEI 250 260 270 280 290 300 ALALDVASSE LFNEETGKYV VGGKEYDRGE LLELYKDLTS TYPIVSIEDP FHEEDWEGFV 310 320 330 340 350 360 MITKELGHKV QIVGDDLFVT NPKRLRKGIE LGAANALLLK VNQIGTLSEA MDAAFTAFRA 370 380 390 400 410 420 GYGVIVSHRS GETEDATIAD LAVALNAGQI KTGAPARSDR NAKYNQLIRI EEELEGVAVY 430 AGKRFRKVFF

References

[1]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009950 Genomic DNA. Translation: AAL80339.1.
RefSeq	NP_577944.1. NC_003413.1.
3D structure databases
ProteinModelPortal	Q8U477.
SMR	Q8U477. Positions 1-429.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000004305; EBPYRP00000004166; EBPYRG00000004305.
GeneID	1468047.
GenomeReviews	Gene locus PF0215 in contig AE009950_GR.
KEGG	pfu:PF0215.
NMPDR	fig|186497.1.peg.218.
Phylogenomic databases
GeneTree	EBGT00050000022630.
HOGENOM	HBG726599.
OMA	QAVDHIN.
PhylomeDB	Q8U477.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11818.
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_PYRFU

Accession

Primary (citable) accession number: Q8U477

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program