Reviewed, UniProtKB/Swiss-Prot Q9F2Q3 (ENO1_STRCO)

Names and origin

Protein names

Recommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1

Gene names

Name:	eno1
Ordered Locus Names:	SCO3096
ORF Names:	SCE41.05c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	426 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 – 426	426	Enolase 1 HAMAP MF_00318		PRO_0000133976
Regions
	Region	362 – 365	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	335	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	283	1	Magnesium By similarity
	Metal binding	310	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	283	1	Substrate By similarity
	Binding site	310	1	Substrate By similarity
	Binding site	335	1	Substrate (covalent); in inhibited form By similarity
	Binding site	386	1	Substrate By similarity
Amino acid modifications
	Modified residue	277	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9F2Q3-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 63AED7B7A4E15001	FASTA	426	45,483
	10 20 30 40 50 60 MPSIDVVVAR EILDSRGNPT VEVEVGLDDG STGRAAVPSG ASTGAFEAIE LRDGDPSRYL 70 80 90 100 110 120 GKGVEKAVLA VIEQIGPELV GYDATEQRLI DQAMFDLDAT DNKGSLGANA ILGVSLAVAH 130 140 150 160 170 180 AASEASDLPL FRYLGGPNAH LLPVPMMNIL NGGSHADSNV DIQEFMIAPI GAESFSEALR 190 200 210 220 230 240 WGAEVYHTLK KVLKNKGLAT GLGDEGGFAP NLGSNREALD LILEAIKEAG YTPGEQIALA 250 260 270 280 290 300 LDVAASEFYK DGSYAFEGKN RSAAEMTEYY AELVEAYPLV SIEDPLFEDD WDGWNTITAK 310 320 330 340 350 360 LGDKVQLVGD DLFVTNPERL ARGIEENSAN ALLVKVNQIG SLTETLDAVE LAQRNGFKCM 370 380 390 400 410 420 MSHRSGETED VTIADLAVAT NCGQIKTGAP ARSERVAKYN QLLRIEEILD DAAVYAGRSA FPRFKG

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	AL939115 Genomic DNA. Translation: CAC09537.1.
RefSeq	NP_627314.1.
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
ModBase	Search...
Genome annotation databases
GeneID	1098530.
GenomeReviews	Gene locus SCO3096 in contig AL645882_GR.
KEGG	sco:SCO3096.
NMPDR	fig|100226.1.peg.3057.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9F2Q3.
OMA	Q9F2Q3. DIAVGTN.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO3096-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

ENO1_STRCO

Accession

Primary (citable) accession number: Q9F2Q3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 54 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)