A0B7E8 (ENO_METTP) 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:	Mthe_0833

Organism

Methanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]

Taxonomic identifier

349307 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosaetaceae › Methanosaeta

Protein attributes

Sequence length	420 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
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 – 420	420	Enolase HAMAP MF_00318		PRO_0000280882
Regions
	Region	360 – 363	4	Substrate binding By similarity
Sites
	Active site	206	1	Proton donor By similarity
	Active site	333	1	Proton acceptor By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	282	1	Magnesium By similarity
	Metal binding	308	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
	Binding site	308	1	Substrate By similarity
	Binding site	333	1	Substrate (covalent); in inhibited form By similarity
	Binding site	384	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0B7E8 [UniParc]. Last modified November 28, 2006. Version 1. Checksum: 25692E4F80FCD7BF	FASTA	420	45,276
	10 20 30 40 50 60 MSLEIEKIHA REILDSRGNP TVEVDVWTCC GFGRAAVPSG ASTGTYEALE LRDGGDRYDG 70 80 90 100 110 120 KGVLKAVRNV NEVIGPKLIG MDVIDQRGVD QIMIEMDGTP NKSNLGANAI LGVSLAVAKA 130 140 150 160 170 180 AASSLGMPLY RYLGGVSATR LPVPSLNVLN GGKHAGNDLS IQEFMIEPWG ADSFSEALRM 190 200 210 220 230 240 AAETYHALGR ILRGKYGNVA TNVGFEGGYA PPISKTRDAL DAIMAALDVT GYTEEIKLGL 250 260 270 280 290 300 DSAASSFYLD GGYSVDDNRL SPGELIDFYV ELVKTYPIVL IEDPFEENAF EEFAELTKKL 310 320 330 340 350 360 PDTIIVGDDL YVTNMARIEK GIRMRSTNAL LLKLNQIGTV SEAFDAATLA YRNSFKVMVS 370 380 390 400 410 420 HRSAETEDSA LADVSVAIGA ELIKTGAPAR SERNAKYNQL LRIQEALGSS ASYAGRRRWS

References

[1]

"Complete sequence of Methanosaeta thermophila PT." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Smith K.S., Ingram-Smith C., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 6194 / PT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000477 Genomic DNA. Translation: ABK14622.1.
RefSeq	YP_843262.1. NC_008553.1.
3D structure databases
ProteinModelPortal	A0B7E8.
SMR	A0B7E8. Positions 3-416.
ModBase	Search...
Protein-protein interaction databases
STRING	A0B7E8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4462976.
GenomeReviews	Gene locus Mthe_0833 in contig CP000477_GR.
KEGG	mtp:Mthe_0833.
NMPDR	fig|349307.7.peg.862.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04113.
HOGENOM	HBG726599.
OMA	EAWSYFY.
PhylomeDB	A0B7E8.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	MTHE349307:MTHE_0833-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_METTP

Accession

Primary (citable) accession number: A0B7E8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	November 28, 2006
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program