Reviewed, UniProtKB/Swiss-Prot A0PW55 (ENO_MYCUA)

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:	MUL_4631

Organism

Mycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]

Taxonomic identifier

362242 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

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 + 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
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
Molecule processing
	Chain	1 – 428	428	Enolase
Regions
	Region	361 – 364	4	Substrate binding By similarity
Sites
	Active site	204	1	Proton donor By similarity
	Active site	334	1	Proton acceptor By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	282	1	Magnesium By similarity
	Metal binding	309	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
	Binding site	309	1	Substrate By similarity
	Binding site	334	1	Substrate (covalent); in inhibited form By similarity
	Binding site	385	1	Substrate By similarity
Amino acid modifications
	Modified residue	276	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0PW55-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 58A29D49E5EBF57F	FASTA	428	44,736
	10 20 30 40 50 60 MPIIEQVGAR EILDSRGNPT VEVEVALIDG TFARAAVPSG ASTGEHEAVE LRDGGDRYGG 70 80 90 100 110 120 KGVKKAVEAV LDEIGPAVIG LNADDQRLVD QALVDLDGTP DKSRLGGNSI LGVSLAVAKA 130 140 150 160 170 180 ASESAELPLF RYIGGPNAHI LPVPMMNILN GGAHADTGVD IQEFMVAPIG APSFSEALRW 190 200 210 220 230 240 GAEVYHALKA VLKKAGLSTG LGDEGGFAPD VASTTAALDL ISQAIEAAGF KPGVDVALAL 250 260 270 280 290 300 DAAANEFHAD GSYTFEGTPR TAAQMTEFYA GLLGSYPVVS IEDPLYENDW DGWAALTAEI 310 320 330 340 350 360 GDRVQIVGDD VFVTNPERLE EGIDRGVANA LLVKVNQIGT LTETLDAVAL AHHSGYRTMI 370 380 390 400 410 420 SHRSGETEDT IIADLAVAVG SGQIKTGAPA RSERVAKYNQ LLRIEEALGD AARYAGDLAF PRFVADPK

References

[1]

"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer." Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T. Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000325 Genomic DNA. Translation: ABL06574.1.
RefSeq	YP_908045.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4550802.
GenomeReviews	Gene locus MUL_4631 in contig CP000325_GR.
KEGG	mul:MUL_4631.
Organism-specific databases
BuruList	MUL_4631.
CMR	Search...
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]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ENO_MYCUA

Accession

Primary (citable) accession number: A0PW55

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	January 9, 2007
Last modified:	July 22, 2008
This is version 18 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)