Reviewed, UniProtKB/Swiss-Prot Q4ZWQ8 (ENO1_PSEU2)

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:	Psyr_1363

Organism

Pseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]

Taxonomic identifier

205918 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae

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 + 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
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 – 428	428	Enolase 1 HAMAP MF_00318		PRO_0000267079
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)
	Q4ZWQ8-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: FDBAD70A041D2C4F	FASTA	428	45,682
	10 20 30 40 50 60 MAKIVDIKGR EVLDSRGNPT VEADVLLDNG IIGSACAPSG ASTGSREALE LRDGDKSRYM 70 80 90 100 110 120 GKGVLKAVAN INGPIRDLLL GKDPVDQKAL DHAMIELDGT ENKASLGANA ILAVSLAAAK 130 140 150 160 170 180 AAAQDQDLPL YAHIANLNGT PGVYSMPVPM MNIINGGEHA DNNIDIQEFM IQPVGAKSFA 190 200 210 220 230 240 EGLRWGTEIF HHLKAVLKAR GLNTAVGDEG GFAPNLASNK EALDAIAEAV ANAGYTLGTD 250 260 270 280 290 300 VTLALDCAAS EFYKNGKYKL SEEGEYSSAE FAEYLAELTR KHPIISIEDG LDESDWDGWK 310 320 330 340 350 360 ILTDKIGEKT QLVGDDLFVT NTKILKEGID KKIANSILIK FNQIGTLTET LEAIQMAKAA 370 380 390 400 410 420 GYTAIISHRS GETEDSTIAD LAVGTSAGQI KTGSLCRSDR VSKYNQLLRI EEQLGSKAVY RGRAEFRG

References

[1]

"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000." Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E. Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed: 16043691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000075 Genomic DNA. Translation: AAY36414.1.
RefSeq	YP_234452.1.
3D structure databases
SMR	Q4ZWQ8. Positions 2-428.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4ZWQ8.
Genome annotation databases
GeneID	3366858.
GenomeReviews	Gene locus Psyr_1363 in contig CP000075_GR.
KEGG	psb:Psyr_1363.
NMPDR	fig|205918.4.peg.1848.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q4ZWQ8.
OMA	DIAVGTN.
Enzyme and pathway databases
BioCyc	PSYR205918:PSYR_1363-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_PSEU2

Accession

Primary (citable) accession number: Q4ZWQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 7, 2005
Last modified:	November 3, 2009
This is version 40 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)