Reviewed, UniProtKB/Swiss-Prot Q1LP64 (ENO2_RALME)

Names and origin

Protein names

Recommended name:
    Enolase 2
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 2
    2-phospho-D-glycerate hydro-lyase 2

Gene names

Name:	eno2
Ordered Locus Names:	Rmet_1176

Organism

Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]

Taxonomic identifier

266264 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
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.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
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 bacterial cell surface By similarity.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	cell surface Inferred from electronic annotation. Source: HAMAP extracellular region Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 425	425	Enolase 2		PRO_0000267085
Regions
	Region	364 – 367	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	337	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	285	1	Magnesium By similarity
	Metal binding	312	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	285	1	Substrate By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	337	1	Substrate (covalent); in inhibited form By similarity
	Binding site	388	1	Substrate By similarity
Amino acid modifications
	Modified residue	279	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1LP64-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 9752442518E0F051	FASTA	425	45,532
	10 20 30 40 50 60 MSKVAEIRGL EVLDSRGNPT VEVEVVLDDG AVGRAIVPSG ASTGAREAVE LRDADPRRYL 70 80 90 100 110 120 GRGVLRAVQA VNTELCEALL GRDAGDQPEI DTIMIDLDGT PDKRRLGANA LLGVSLAVAH 130 140 150 160 170 180 AAAMSNGLPL FAYLGGERAS LLPVPLINVI NGGAHADNAL DFQEFMIVPA GAPTFTEAVR 190 200 210 220 230 240 ASAEVFHTLR AMLKAAGYTT NVGDEGGFAP EFHAAEEALD ILVAAIAKAG YRPGEDIALA 250 260 270 280 290 300 IDPAASELYV NGSYVYQGEG VERSREEQVA YLVRLADRYP IVSIEDGMAE DDAMGWQLLT 310 320 330 340 350 360 RQLGKRCQLV GDDVFCTHPT LLRQGVEQGM ANAILVKANQ IGTLSEMRET VRVAHGYAYS 370 380 390 400 410 420 AVMSHRSGET EDVTIADLAV ALRCGQIKTG SMSRADRTAK YNRLLRIERE LGSRAEYAGA LLRRR

References

[1]

"Complete sequence of the chromosome of Ralstonia metallidurans CH34." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000352 Genomic DNA. Translation: ABF08062.1.
RefSeq	YP_583331.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4037976.
GenomeReviews	Gene locus Rmet_1176 in contig CP000352_GR.
KEGG	rme:Rmet_1176.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1LP64.
Enzyme and pathway databases
BioCyc	RMET266264:RMET_1176-MON.
Family and domain databases
HAMAP	MF_00318. [Tree]
InterPro	IPR000941. Enolase. [Graphical view]
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.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO2_RALME

Accession

Primary (citable) accession number: Q1LP64

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	May 30, 2006
Last modified:	November 25, 2008
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)