Reviewed, UniProtKB/Swiss-Prot Q9F3P9 (ENO2_STRCO)

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:	SCO7638
ORF Names:	SC10F4.11c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	434 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 + 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.
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 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: 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: 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 – 434	434	Enolase 2 HAMAP MF_00318		PRO_0000133977
Regions
	Region	372 – 375	4	Substrate binding By similarity
Sites
	Active site	213	1	Proton donor By similarity
	Active site	345	1	Proton acceptor By similarity
	Metal binding	250	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity
	Metal binding	320	1	Magnesium By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity
	Binding site	345	1	Substrate (covalent); in inhibited form By similarity
	Binding site	396	1	Substrate By similarity
Amino acid modifications
	Modified residue	287	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9F3P9-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 435A1CC0629DC0A0	FASTA	434	45,534
	10 20 30 40 50 60 MSATAVEPAA AIETVTARRI IDSRGNPTVE VDVVLEDGSL GRAAVPSGAS TGAREAVELR 70 80 90 100 110 120 DEDPTRWHGK GVDRAVAHVN GEIAASVRGR DAADQAGLDA ALIALDGTAA KSRLGANALL 130 140 150 160 170 180 GVSLAAAKAA AAARRQPLYR YLGGADAHLL PLPMMNIVNG GAHADNPLDF QEFMIVPVGA 190 200 210 220 230 240 DTFAEAVRMG SEVFHTLRRD LLAAGHSTGV GDEGGFAPAL RTAEEALDFV VAAIERTGYR 250 260 270 280 290 300 AGPDIGLVMD PASSEFFRDG GYDYAGEGVR RSPAEHADHL AGLIDAYPVV SIEDPMAEDD 310 320 330 340 350 360 LDGWRELTDR VGDRCQLTGD DVFCTDEALV REGIRTGVGN SVLVKVNQIG TLTEALATVA 370 380 390 400 410 420 TAHEAGWTVV MSHRSGETED TTIADLAVAT GCGQIKTGSL SRSDRTAKYN RLIRIEEELG 430 ASARFAGRSA LRRV

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939132 Genomic DNA. Translation: CAC16971.1.
RefSeq	NP_631678.1.
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
ModBase	Search...
Genome annotation databases
GeneID	1103076.
GenomeReviews	Gene locus SCO7638 in contig AL645882_GR.
KEGG	sco:SCO7638.
NMPDR	fig|100226.1.peg.7569.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9F3P9.
OMA	LDGWREL.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO7638-MON.
BRENDA	4.2.1.11. 1084.
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_STRCO

Accession

Primary (citable) accession number: Q9F3P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 55 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)