Reviewed, UniProtKB/Swiss-Prot Q886M3 (ENO1_PSESM)

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
Synonyms:	eno-1
Ordered Locus Names:	PSPTO_1554

Organism

Pseudomonas syringae pv. tomato [Complete proteome] [HAMAP]

Taxonomic identifier

323 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	428 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
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 – 428	428	Enolase 1		PRO_0000133951
Regions
	Region	367 – 370	4	Substrate binding By similarity
Sites
	Active site	209	1	Proton donor By similarity
	Active site	340	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	288	1	Magnesium By similarity
	Metal binding	315	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	315	1	Substrate By similarity
	Binding site	340	1	Substrate (covalent); in inhibited form By similarity
	Binding site	391	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q886M3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E6EDCBF3FF55514E	FASTA	428	45,623
	10 20 30 40 50 60 MAKIVDIKGR EVLDSRGNPT VEADVLLDNG IIGSACAPSG ASTGSREALE LRDGDKSRYM 70 80 90 100 110 120 GKGVLKAVAN INGPIRDLLL GKDPVDQKAL DHAMIALDAT ENKASLGANA ILAVSLAAAK 130 140 150 160 170 180 AAAQDQDLPL YAHIANLNGT PGVYSMPVPM MNIINGGEHA DNNIDIQEFM IQPVGAKSFA 190 200 210 220 230 240 EALRWGTEIF HHLKAVLKAR GLNTAVGDEG GFAPNLASNK EALEAIAEAV ANAGYTLGTD 250 260 270 280 290 300 VTLALDCAAS EFYKNGKYTL SEEGEYSSAE FAEYLAELTR KHPIISIEDG LDESDWDGWK 310 320 330 340 350 360 VLTEKIGEKV QLVGDDLFVT NTKILKEGID KNIANSILIK FNQIGTLTET LEAIQMAKAA 370 380 390 400 410 420 GYTAIISHRS GETEDSTIAD LAVGTSAGQI KTGSLCRSDR VSKYNQLLRI EEQLGSKAVY RGRAEFRG

References

[1]

"The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000." Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.M., Zafar N. , Zhou L., Liu J., Yuan Q., Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A. Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003) [PubMed: 12928499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DC3000.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016853 Genomic DNA. Translation: AAO55074.1.
RefSeq	NP_791379.1.
3D structure databases
HSSP	HSSP built from PDB template 1E9I based on UniProtKB P08324.
SMR	Q886M3. Positions 2-428.
ModBase	Search...
Genome annotation databases
GeneID	1183191.
GenomeReviews	Gene locus PSPTO_1554 in contig AE016853_GR.
KEGG	pst:PSPTO_1554.
NMPDR	fig|223283.1.peg.1517.
TIGR	PSPTO_1554.
Phylogenomic databases
HOGENOM	Q886M3.
Enzyme and pathway databases
BioCyc	PSYR223283:PSPTO_1554-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

ENO1_PSESM

Accession

Primary (citable) accession number: Q886M3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	November 25, 2008
This is version 51 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)