Reviewed, UniProtKB/Swiss-Prot P37869 (ENO_BACSU)

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:	BSU33900

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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 at Lys-339 of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
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 at Lys-339; once secreted, it remains attached to the bacterial cell surface.
Post-translational modification	Phosphorylated during sporulation.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis Sporulation
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW
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
	Initiator methionine	1	1	Removed
	Chain	2 – 430	429	Enolase		PRO_0000133841
Regions
	Region	366 – 369	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	339	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	287	1	Magnesium By similarity
	Metal binding	314	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	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
	Binding site	390	1	Substrate By similarity
Amino acid modifications
	Modified residue	141	1	Phosphothreonine
	Modified residue	259	1	Phosphoserine
	Modified residue	281	1	Phosphotyrosine
	Modified residue	325	1	Phosphoserine
Experimental info
	Sequence conflict	45	1	E → Q in AAA21681. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37869-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C82B60F49D11AE68	FASTA	430	46,581
	10 20 30 40 50 60 MPYIVDVYAR EVLDSRGNPT VEVEVYTETG AFGRALVPSG ASTGEYEAVE LRDGDKDRYL 70 80 90 100 110 120 GKGVLTAVNN VNEIIAPELL GFDVTEQNAI DQLLIELDGT ENKGKLGANA ILGVSMACAR 130 140 150 160 170 180 AAADFLQIPL YQYLGGFNSK TLPVPMMNIV NGGEHADNNV DIQEFMIMPV GAPNFREALR 190 200 210 220 230 240 MGAQIFHSLK SVLSAKGLNT AVGDEGGFAP NLGSNEEALQ TIVEAIEKAG FKPGEEVKLA 250 260 270 280 290 300 MDAASSEFYN KEDGKYHLSG EGVVKTSAEM VDWYEELVSK YPIISIEDGL DENDWEGHKL 310 320 330 340 350 360 LTERLGKKVQ LVGDDLFVTN TKKLSEGIKN GVGNSILIKV NQIGTLTETF DAIEMAKRAG 370 380 390 400 410 420 YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV AKYNQLLRIE DQLAETAQYH 430 GINSFYNLNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis." Leyva-Vazquez M.A., Setlow P. J. Bacteriol. 176:3903-3910(1994) [PubMed: 8021172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis." Mitchell C., Morris P.W., Vary J.C. J. Bacteriol. 174:2474-2477(1992) [PubMed: 1556067] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, PHOSPHORYLATION.
[4]	"A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis." Brown C.K., Kuhlman P.L., Mattingly S., Slates K., Calie P.J., Farrar W.W. J. Protein Chem. 17:855-866(1998) [PubMed: 9988532] [Abstract] Cited for: CHARACTERIZATION, SUBUNIT.
[5]	"Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?" Boeel G., Pichereau V., Mijakovic I., Maze A., Poncet S., Gillet S., Giard J.-C., Hartke A., Auffray Y., Deutscher J. J. Mol. Biol. 337:485-496(2004) [PubMed: 15003462] [Abstract] Cited for: SUBSTRATE BINDING AT LYS-339. Strain: 168.
[6]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; SER-259; TYR-281 AND SER-325, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L29475 Genomic DNA. Translation: AAA21681.1. Z99121 Genomic DNA. Translation: CAB15395.1.
PIR	B69620.
RefSeq	NP_391270.1.
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
SMR	P37869. Positions 3-427, 4-428.
ModBase	Search...
Genome annotation databases
GeneID	938641.
GenomeReviews	Gene locus BSU33900 in contig AL009126_GR.
KEGG	bsu:BSU33900.
NMPDR	fig|224308.1.peg.3396.
Organism-specific databases
SubtiList	BG10899. eno. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P37869.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3387-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...
Other Resources
LinkHub	P37869.

Entry information

Entry name

ENO_BACSU

Accession

Primary (citable) accession number: P37869
Secondary accession number(s): O32249

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 85 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)