Reviewed, UniProtKB/Swiss-Prot Q8UFH1 (ENO_AGRT5)

Names and origin

Protein names

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

Gene names

Name:	eno
Ordered Locus Names:	Atu1426
ORF Names:	AGR_C_2631

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	424 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 – 424	424	Enolase HAMAP MF_00318		PRO_0000133829
Regions
	Region	363 – 366	4	Substrate binding By similarity
Sites
	Active site	204	1	Proton donor By similarity
	Active site	336	1	Proton acceptor By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	284	1	Magnesium By similarity
	Metal binding	311	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	311	1	Substrate By similarity
	Binding site	336	1	Substrate (covalent); in inhibited form By similarity
	Binding site	387	1	Substrate By similarity
Amino acid modifications
	Modified residue	278	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8UFH1-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 84892005DEC0666F	FASTA	424	45,142
	10 20 30 40 50 60 MTAITDIIAR EILDSRGNPT VEVDVYLEDG SMGRAAVPSG ASTGAHEAVE LRDGGKRYLG 70 80 90 100 110 120 KGVEKAVEAV NTEIFDAIGG FDAENQIQID QMMIALDGTP NKSRLGANAI LGVSLAIAKA 130 140 150 160 170 180 AAEASGLPLY RYVGGPNAHL LPVPMMNIIN GGAHADNPID FQEFMILPVG AENIREAVRM 190 200 210 220 230 240 GSEVFHTLKK ELSAQGHNTN VGDEGGFAPG LESAPAALDF IMKSIEKAGY RPGEDMYVGL 250 260 270 280 290 300 DCASTEFFKD GKYVLEGEGR TLEPGAMAEY LAELVNKYPI ISVEDGMAED DWEGWKTLTD 310 320 330 340 350 360 LVGNKCQLVG DDLFVTNSAR LRDGIKMGVA NSILVKVNQI GSLSETLDAV ETAHKAGYTA 370 380 390 400 410 420 VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRLAKY NQLIRIEEML GPQAAYAGRS ILRG

References

[1]

"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE007869 Genomic DNA. Translation: AAK87218.1.
PIR	A97533. AB2752.
RefSeq	NP_354433.1.
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
ModBase	Search...
Genome annotation databases
GeneID	1133464.
GenomeReviews	Gene locus Atu1426 in contig AE007869_GR.
KEGG	atc:AGR_C_2631. atu:Atu1426.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8UFH1.
OMA	Q8UFH1. DIAVGTN.
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

ENO_AGRT5

Accession

Primary (citable) accession number: Q8UFH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 53 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)