Q8TUV6 (ENO_METKA) 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:	MK1647

Organism

Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)

Taxonomic identifier

190192 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

Protein attributes

Sequence length	427 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 – 427	427	Enolase HAMAP MF_00318		PRO_0000134025
Regions
	Region	365 – 368	4	Substrate binding By similarity
Sites
	Active site	206	1	Proton donor By similarity
	Active site	338	1	Proton acceptor By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	286	1	Magnesium By similarity
	Metal binding	313	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	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)
	Q8TUV6 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: C7D9738D77BFC8C4	FASTA	427	46,163
	10 20 30 40 50 60 MPRIVSVKAR EVLDSRGEPT VEVEVELEDG TVGRAMVPSG ASTGTYEALE LRDGDDRYGG 70 80 90 100 110 120 KGVRRAVRNV EEIIAPEIEG LDATAQPDID RTMIELDGTE NKSHLGANAI LGVSLAVARA 130 140 150 160 170 180 AAKSLGIPLY RYLGGPTARR LPVPFMNVIN GGEHAGNELD FQEHMIVPHG FESFSEALRA 190 200 210 220 230 240 GVETYHVLGE LLEEEYGPIA TNVGDEGGYA PPMKDTVEPL DVLVEAIEEA GYAPGKEIAL 250 260 270 280 290 300 ALDAAASEFY DEDSGTYRAY GQKYTRDELI DVYKDLVSQY PIVSIEDPLH EEDFRGFAKI 310 320 330 340 350 360 TEELGDKVQI VGDDLFVTNP DRLRKGIEMG AANALLLKVN QIGTLTEAVE AGELALQHGY 370 380 390 400 410 420 GVMVSHRSGD TEDPFIADLA VALGCGQIKT GAPARSSRTA KYNRLLRIEE DLAGAAEFGP RNDFFLP

References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009439 Genomic DNA. Translation: AAM02860.1.
RefSeq	NP_614930.1. NC_003551.1.
3D structure databases
ProteinModelPortal	Q8TUV6.
SMR	Q8TUV6. Positions 4-422.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1478242.
GenomeReviews	Gene locus MK1647 in contig AE009439_GR.
KEGG	mka:MK1647.
NMPDR	fig|190192.1.peg.1643.
Phylogenomic databases
HOGENOM	HBG726599.
OMA	EAWSYFY.
PhylomeDB	Q8TUV6.
Enzyme and pathway databases
BioCyc	MKAN190192:MK1647-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_METKA

Accession

Primary (citable) accession number: Q8TUV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program