Reviewed, UniProtKB/Swiss-Prot Q4ZWE0 (ENO2_PSEU2)

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:	Psyr_1482

Organism

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

Taxonomic identifier

205918 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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_0000267080
Regions
	Region	366 – 369	4	Substrate binding By similarity
Sites
	Active site	207	1	Proton donor By similarity
	Active site	339	1	Proton acceptor By similarity
	Metal binding	244	1	Magnesium By similarity
	Metal binding	287	1	Magnesium By similarity
	Metal binding	314	1	Magnesium By similarity
	Binding site	156	1	Substrate By similarity
	Binding site	166	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Binding site	314	1	Substrate By similarity
	Binding site	339	1	Substrate (covalent); in inhibited form By similarity
	Binding site	390	1	Substrate By similarity
Amino acid modifications
	Modified residue	281	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4ZWE0-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: FAE71E15B6043CB4	FASTA	427	46,037
	10 20 30 40 50 60 MKTQIQAIHA REILDSRGNP TVEVDVTLEC GAMGRASVPS GASTGAHEAV ELRDKDTQRY 70 80 90 100 110 120 SGKGVLKAVS NVNTEILESL RGMNAIDQEQ IDHLMIKLDG TSDKSRLGGN AILGVSLAVA 130 140 150 160 170 180 RAAASALNLP LFQYLGGEQA ARMPVPMFNI LNGGVHANWQ GPDFQEFMIA PTGAGSFKEA 190 200 210 220 230 240 LRWGSEVYHE LKAVLKDAGY STAVGDEGGF APALKKNSDA IELIIKAIER AGYTPGSQIE 250 260 270 280 290 300 IAIDPASSGF YENGLYHLRS EGRKVDAQEL INLYSSWVDK YPIAVLEDGL AEDDWSGWKL 310 320 330 340 350 360 LNAALGDRIE LVGDDLFVTN VERIQRGITE NVANAVLIKP NQIGTLTETK AAIEMAYGAN 370 380 390 400 410 420 WGAMVSHRSG ETVDSSIADL TVAMGTGHLK TGAPCRGERV EKYNQFLRIE EDLGSRAFYA GHDAFVR

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: AAY36532.1.
RefSeq	YP_234570.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3366981.
GenomeReviews	Gene locus Psyr_1482 in contig CP000075_GR.
KEGG	psb:Psyr_1482.
NMPDR	fig|205918.4.peg.1966.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q4ZWE0.
Enzyme and pathway databases
BioCyc	PSYR205918:PSYR_1482-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_PSEU2

Accession

Primary (citable) accession number: Q4ZWE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 7, 2005
Last modified:	November 25, 2008
This is version 36 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)