Enolase - Agrobacterium tumefaciens (strain C58 / ATCC 33970)

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Q8UFH1 (ENO_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase

Gene names

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

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
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. HAMAP MF_00318
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. HAMAP MF_00318
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. HAMAP MF_00318
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 Reference proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
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

Substrate binding By similarity

Sites

Active site

204

Proton donor By similarity

Active site

336

Proton acceptor By similarity

Metal binding

241

Magnesium By similarity

Metal binding

284

Magnesium By similarity

Metal binding

311

Magnesium By similarity

Binding site

154

Substrate By similarity

Binding site

163

Substrate By similarity

Binding site

284

Substrate By similarity

Binding site

311

Substrate By similarity

Binding site

336

Substrate (covalent); in inhibited form By similarity

Binding site

387

Substrate By similarity

Amino acid modifications

Modified residue

278

Phosphotyrosine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8UFH1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 84892005DEC0666F
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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

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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. Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.
[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. Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C58 / ATCC 33970.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE007869 Genomic DNA. Translation: AAK87218.1.
PIR	A97533. AB2752.
RefSeq	NP_354433.1. NC_003062.2.
3D structure databases
ProteinModelPortal	Q8UFH1.
SMR	Q8UFH1. Positions 2-418.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8UFH1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1133464.
GenomeReviews	Gene locus Atu1426 in contig AE007869_GR.
KEGG	atu:Atu1426.
PATRIC	20812627. VBIAgrTum91616_1448.
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	QEYMIMP.
PhylomeDB	Q8UFH1.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	ATUM176299-1:ATU1426-MONOMER.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
KO	K01689.
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.
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:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents