P57492 (ENO_BUCAI) Reviewed, UniProtKB/Swiss-Prot

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:	BU417

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Acyrthosiphon pisum)

Protein attributes

Sequence length	434 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-Rule MF_00318
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule 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-Rule MF_00318
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule 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-Rule 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: 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 – 434	434	Enolase HAMAP-Rule MF_00318		PRO_0000133855
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	209	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	291	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	343	1	Substrate (covalent); in inhibited form By similarity
	Binding site	394	1	Substrate By similarity
Amino acid modifications
	Modified residue	285	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57492 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: D3F5FD25D8F52D40	FASTA	434	47,428
	10 20 30 40 50 60 MSKITKIIAR EIIDSRGNPT VESEVHLEGG FVGLASSPSG ASTGSLEALE LRDENKDRFM 70 80 90 100 110 120 GKGVEKAVSL INEKISIALK NKNARNQSDI DHIMIDLDGT INKSKLGANA ILSVSLAVAK 130 140 150 160 170 180 AAAASKRMPL YAHIAEINET PGVFSMPLPM INIINGGKHA NNNIDIQEFM IQPISAKTVK 190 200 210 220 230 240 ESIRIGCEIF HALGELLKEK GMSTTVGDEG GYAPNLKSNE EALNIIQDAI QKTKYKLGQD 250 260 270 280 290 300 IRLAIDCAAS ELYNKNEKKY NLKGENISFS SKEFTHYLEK LSQKYPIVSI EDGQDESDWE 310 320 330 340 350 360 GFLYQTHVLG NKIQLVGDDL FVTNKNILKK GIKKGIANSI LIKLNQIGTL TETLEAIKTA 370 380 390 400 410 420 KQANYGVIIS HRSGETEDAS IADLSVGTSS GQIKTGSMSR SDRTSKYNQL IRIEENLGTK 430 YAPFHGLREI KSAF

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB13115.1.
RefSeq	NP_240229.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57492.
SMR	P57492. Positions 2-431.
ModBase	Search...
Proteomic databases
PRIDE	P57492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB13115; BAB13115; BAB13115.
GeneID	1109765.
KEGG	buc:BU417.
PATRIC	21244374. VBIBucAph127364_0426.
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HOG000072174.
KO	K01689.
OMA	EYMIMPL.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	BAPH107806:GBZJ-417-MONOMER.
UniPathway	UPA00109; UER00187.
Family and domain databases
HAMAP	MF_00318. Enolase.
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
PANTHER	PTHR11902. PTHR11902. 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_BUCAI

Accession

Primary (citable) accession number: P57492

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program