Reviewed, UniProtKB/Swiss-Prot Q604M4 (ENO2_METCA)

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
Synonyms:	eno-2
Ordered Locus Names:	MCA2515

Organism

Methylococcus capsulatus [Complete proteome] [HAMAP]

Taxonomic identifier

414 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	427 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 – 427	427	Enolase 2		PRO_0000133920
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)
	Q604M4-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: E702454A2825E7DF	FASTA	427	45,343
	10 20 30 40 50 60 MSKIVDILAR EILDSRGNPT VQAEVILDSG AEGSAMVPSG ASTGAREAIE LRDGDASRYG 70 80 90 100 110 120 GKGVLKAVEN VRGPIKAALT GMDAADQAAI DRRLIELDGS DNKGVLGANA ILAVSLATAH 130 140 150 160 170 180 AAAADAKKPL YAYLNRSGEF LLPVPMMNII NGGAHADNSI DMQEFMILPV GAPSFREALR 190 200 210 220 230 240 YGAEVFHALK KVLSDRGLAT GVGDEGGFAP NLPSNEAAIG IILEAIEKAG YRPGEDICLG 250 260 270 280 290 300 LDVASSEFYS DGIYTLASEG RRFTSEEFSD HLAAWVDKYP IVSIEDGMAE NDWHGWGIHT 310 320 330 340 350 360 DRLGRRIQLV GDDLFVTNPA ILKQGIEARI ANSILIKVNQ IGTLTETLEA IHIARKAGYT 370 380 390 400 410 420 SVVSHRSGET EGTTIADIAV ATCTGQIKTG SLSRSDRIAK YNRLLKIEEE LGDKARYGGR GAVKNLA

References

[1]

"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017282 Genomic DNA. Translation: AAU91336.1.
RefSeq	YP_114926.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3103072.
GenomeReviews	Gene locus MCA2515 in contig AE017282_GR.
KEGG	mca:MCA2515.
NMPDR	fig|243233.4.peg.2451.
TIGR	MCA2515.
Phylogenomic databases
HOGENOM	Q604M4.
Enzyme and pathway databases
BioCyc	MCAP243233:MCA_2515-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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO2_METCA

Accession

Primary (citable) accession number: Q604M4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	November 23, 2004
Last modified:	November 25, 2008
This is version 37 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)