[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC BAA-334 / TIGR4; DOI=10.1126/science.1061217; PubMed=11463916 [NCBI, ExPASy, EBI, Israel, Japan] Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.; "Complete genome sequence of a virulent isolate of Streptococcus pneumoniae."; Science 293:498-506(2001).
[2]	PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, BINDING TO PLASMINOGEN, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-433 AND LYS-434. STRAIN=ATCC 11733 / Seroytpe 2; PubMed=11442827 [NCBI, ExPASy, EBI, Israel, Japan] Bergmann S., Rohde M., Chhatwal G.S., Hammerschmidt S.; "alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface."; Mol. Microbiol. 40:1273-1287(2001).
[3]	PROTEIN SEQUENCE OF 2-31, ENZYMATIC ACTIVITY, SUBCELLULAR LOCATION, BINDING TO PLASMINOGEN, AND IMMUNOGENICITY. PubMed=12435062 [NCBI, ExPASy, EBI, Israel, Japan] Whiting G.C., Evans J.T., Patel S., Gillespie S.H.; "Purification of native alpha-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic."; J. Med. Microbiol. 51:837-843(2002).
[4]	PLASMINOGEN-BINDING MOTIF, AND MUTAGENESIS OF LYS-251; GLU-252; LYS-254; LYS-433 AND LYS-434. STRAIN=ATCC 11733 / Seroytpe 2, and D39 / Serotype 2; DOI=10.1046/j.1365-2958.2003.03557.x; PubMed=12828639 [NCBI, ExPASy, EBI, Israel, Japan] Bergmann S., Wild D., Diekmann O., Frank R., Bracht D., Chhatwal G.S., Hammerschmidt S.; "Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae."; Mol. Microbiol. 49:411-423(2003).
[5]	ROLE OF PLASMINOGEN-BINDING MOTIF ON DEGRADATION OF EXTRACELLULAR MATRIX. STRAIN=D39 / Serotype 2; DOI=10.1267/THRO05020304; PubMed=16113819 [NCBI, ExPASy, EBI, Israel, Japan] Bergmann S., Rohde M., Preissner K.T., Hammerschmidt S.; "The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration."; Thromb. Haemost. 94:304-311(2005).
[6]	EPITOPE MAPPING, AND ANTIGENICITY. STRAIN=ATCC 11733 / Seroytpe 2; DOI=10.1099/mic.0.28747-0; PubMed=16622048 [NCBI, ExPASy, EBI, Israel, Japan] Kolberg J., Aase A., Bergmann S., Herstad T.K., Roedal G., Frank R., Rohde M., Hammerschmidt S.; "Streptococcus pneumoniae enolase is important for plasminogen binding despite low abundance of enolase protein on the bacterial cell surface."; Microbiology 152:1307-1317(2006).
[7]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). STRAIN=ATCC 11733 / Seroytpe 2; DOI=10.1016/j.jmb.2004.08.088; PubMed=15476816 [NCBI, ExPASy, EBI, Israel, Japan] Ehinger S., Schubert W.-D., Bergmann S., Hammerschmidt S., Heinz D.W.; "Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites."; J. Mol. Biol. 343:997-1005(2004).

Comments

FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.
CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer (By similarity).
ENZYME REGULATION: The covalent binding to the substrate of a small fraction of enolase causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein (By similarity).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=4.5 mM for 2-phospho-D-glycerate;
V_max=2.792 µmol/min/mg enzyme;
Note=Catalytically active also when expressed on the bacterial cell surface;
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5 .
SUBUNIT: Homooctamer. Forms a ring-shaped structure.
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, probably in complex with plasminogen.
SIMILARITY: Belongs to the enolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE005672; AAK75238.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E95130; E95130.

RefSeq

NP_345598.1; -.

3D structure databases

PDB

1W6T; X-ray; 2.10 A; A/B=1-434.

[ExPASy / RCSB / EBI]

PDBsum

1W6T; -.

ModBase

Q97QS2.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004634;	Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00318; -; 1.
PBIL [Tree]

InterPro

IPR000941; Enolase.
Graphical view of domain structure.

PANTHER

PTHR11902; Enolase; 1.

Pfam

PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001400; Enolase; 1.

PRINTS

PR00148; ENOLASE.

ProDom

PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Genome annotation databases

GeneID

931642; -.

GenomeReviews

AE005672_GR; SP_1128.

KEGG

spn:SP_1128; -.

TIGR

SP_1128; -.

Phylogenomic databases

HOGENOM

Q97QS2; -.

Other

ProtoNet

Q97QS2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted; Virulence.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 434`	`434`	`Enolase.`	`PRO_0000133980`
`REGION`	`55 63`	`9`	`Antigenic epitope.`
`REGION`	`370 373`	`4`	`Substrate binding (By similarity).`
`MOTIF`	`248 256`	`9`	`Plasminogen-binding.`
`ACT_SITE`	`205 205`		`Proton donor (By similarity).`
`ACT_SITE`	`343 343`		`Proton acceptor (By similarity).`
`METAL`	`242 242`		`Magnesium (By similarity).`
`METAL`	`291 291`		`Magnesium (By similarity).`
`METAL`	`318 318`		`Magnesium (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`291 291`		`Substrate (By similarity).`
`BINDING`	`318 318`		`Substrate (By similarity).`
`BINDING`	`343 343`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`394 394`		`Substrate (By similarity).`
`MOD_RES`	`285 285`		`Phosphotyrosine (By similarity).`
`MUTAGEN`	`251 251`		`K->L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with G-252 and L-254.`
`MUTAGEN`	`252 252`		`E->G: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and L-254.`
`MUTAGEN`	`254 254`		`K->L: Great decrease in ability to bind plasminogen. Decrease in virulence; when associated with L-251 and G-252.`
`MUTAGEN`	`433 433`		`K->L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-434.`
`MUTAGEN`	`434 434`		`K->L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions.`
`MUTAGEN`	`434 434`		`K->L: Decrease in ability to bind plasminogen under denaturing conditions. No effect on ability to bind plasminogen under non-denaturing conditions. Loss of ability to form homooctamers. Decrease in virulence; when associated with L-433.`
`CONFLICT`	`2 2`		`Missing (in Ref. 2; AA sequence).`
`CONFLICT`	`20 20`		`T -> P (in Ref. 2; AA sequence).`
`CONFLICT`	`24 24`		`E -> G (in Ref. 3; AA sequence).`
`STRAND`	`3 13`	`11`
`STRAND`	`19 27`	`9`
`STRAND`	`32 36`	`5`
`HELIX`	`59 61`	`3`
`HELIX`	`65 73`	`9`
`HELIX`	`75 79`	`5`
`HELIX`	`87 98`	`12`
`TURN`	`104 106`	`3`
`HELIX`	`108 126`	`19`
`HELIX`	`130 135`	`6`
`STRAND`	`147 151`	`5`
`HELIX`	`153 155`	`3`
`STRAND`	`157 159`	`3`
`STRAND`	`163 168`	`6`
`HELIX`	`175 195`	`21`
`HELIX`	`215 228`	`14`
`TURN`	`233 235`	`3`
`STRAND`	`238 242`	`5`
`HELIX`	`245 248`	`4`
`HELIX`	`259 262`	`4`
`HELIX`	`271 284`	`14`
`STRAND`	`287 292`	`6`
`HELIX`	`299 309`	`11`
`TURN`	`310 312`	`3`
`STRAND`	`313 318`	`6`
`TURN`	`319 323`	`5`
`HELIX`	`325 334`	`10`
`STRAND`	`338 342`	`5`
`HELIX`	`344 347`	`4`
`HELIX`	`350 362`	`13`
`STRAND`	`366 370`	`5`
`HELIX`	`380 387`	`8`
`STRAND`	`392 394`	`3`
`STRAND`	`398 400`	`3`
`HELIX`	`401 417`	`17`
`HELIX`	`418 420`	`3`
`HELIX`	`425 428`	`4`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47103 Da [This is the MW of the unprocessed precursor]

CRC64: 0D64F8F04BBB99C4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG 

        70         80         90        100        110        120 
GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR 

       130        140        150        160        170        180 
AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR 

       190        200        210        220        230        240 
YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG 

       250        260        270        280        290        300 
FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD 

       310        320        330        340        350        360 
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA 

       370        380        390        400        410        420 
KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV 

       430 
AEYRGLKSFY NLKK

Q97QS2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools