Q12VE5 (ENO_METBU) 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:	Mbur_1687

Organism

Methanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]

Taxonomic identifier

259564 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanococcoides

Protein attributes

Sequence length	425 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 – 425	425	Enolase HAMAP MF_00318		PRO_0000267141
Regions
	Region	369 – 372	4	Substrate binding By similarity
Sites
	Active site	214	1	Proton donor By similarity
	Active site	342	1	Proton acceptor By similarity
	Metal binding	250	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	317	1	Magnesium By similarity
	Binding site	162	1	Substrate By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	291	1	Substrate By similarity
	Binding site	317	1	Substrate By similarity
	Binding site	342	1	Substrate (covalent); in inhibited form By similarity
	Binding site	393	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12VE5 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 405E36A46D352755	FASTA	425	45,606
	10 20 30 40 50 60 MNSISEEAKY TIQKVHAREI LDSRGNPTVE VDIYTGCGFG RASVPSGAST GSNEALELRD 70 80 90 100 110 120 KDADRYNGKG VLKAVDNINK TLSKELLGMD ARNQREIDEL MIALDGTENK KTFGANAILG 130 140 150 160 170 180 ISMATAKAAA DSLGIALYRY LGGTNAFALP VPTMNVINGG KHAGNDLSIQ EFMIQPKGAD 190 200 210 220 230 240 TFSNALRMGA ETYHALGKVL EDKYGASATN VGYEGGYAPP ISTTADALDA LVSAIEEAGY 250 260 270 280 290 300 TESEISIGLD SAASEFFDGD KYFIDGNKLA PAELVDYYLD LIETYPILSI EDPFHEESFE 310 320 330 340 350 360 DFAALTSEAW DTIIVGDDLF VTNVNRLAKG IEMEAANALL LKVNQIGTIS ESFDAANLAQ 370 380 390 400 410 420 RNGYSVVVSH RSAETEDTMI ADISVAIGGD LIKTGAPARS ERTAKYNQLL RIEEDLGDAA RYVQL

References

[1]

"Complete sequence of Methanococcoides burtonii DSM 6242." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 6242.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000300 Genomic DNA. Translation: ABE52581.1.
RefSeq	YP_566331.1. NC_007955.1.
3D structure databases
ProteinModelPortal	Q12VE5.
SMR	Q12VE5. Positions 7-417.
ModBase	Search...
Protein-protein interaction databases
STRING	Q12VE5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3998083.
GenomeReviews	Gene locus Mbur_1687 in contig CP000300_GR.
KEGG	mbu:Mbur_1687.
NMPDR	fig|259564.8.peg.1609.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04113.
HOGENOM	HBG726599.
OMA	DNMMIEM.
PhylomeDB	Q12VE5.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	MBUR259564:MBUR_1687-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_METBU

Accession

Primary (citable) accession number: Q12VE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program