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Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

 ENO_STRPN               Reviewed;         434 AA.
Q97QS2;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=SP_1128;
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=170187;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
PubMed=11463916; DOI=10.1126/science.1061217;
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, FUNCTION IN VIRULENCE,
BINDING TO PLASMINOGEN, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
OF LYS-433 AND LYS-434.
STRAIN=ATCC 11733 / Seroytpe 2;
PubMed=11442827; DOI=10.1046/j.1365-2958.2001.02448.x;
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, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, BINDING TO PLASMINOGEN, AND IMMUNOGENICITY.
PubMed=12435062;
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;
PubMed=12828639; DOI=10.1046/j.1365-2958.2003.03557.x;
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]
FUNCTION OF PLASMINOGEN-BINDING MOTIF ON DEGRADATION OF EXTRACELLULAR
MATRIX.
STRAIN=D39 / Serotype 2;
PubMed=16113819; DOI=10.1267/THRO05020304;
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;
PubMed=16622048; DOI=10.1099/mic.0.28747-0;
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;
PubMed=15476816; DOI=10.1016/j.jmb.2004.08.088;
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).
-!- 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. {ECO:0000255|HAMAP-
Rule:MF_00318, ECO:0000269|PubMed:11442827,
ECO:0000269|PubMed:12435062, ECO:0000269|PubMed:16113819}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318,
ECO:0000269|PubMed:12435062}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
-!- 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. {ECO:0000255|HAMAP-Rule:MF_00318}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.5 mM for 2-phospho-D-glycerate
{ECO:0000269|PubMed:11442827};
Vmax=2.792 umol/min/mg enzyme {ECO:0000269|PubMed:11442827};
Note=Catalytically active also when expressed on the bacterial
cell surface.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- SUBUNIT: Homooctamer. Forms a ring-shaped structure.
-!- INTERACTION:
Q9S400:aroA; NbExp=2; IntAct=EBI-2207206, EBI-2207276;
Q97PR0:asnS; NbExp=2; IntAct=EBI-2207206, EBI-2207302;
P95830:dnaJ; NbExp=2; IntAct=EBI-2207206, EBI-2207079;
Q97SE6:gatA; NbExp=2; IntAct=EBI-2207206, EBI-2207039;
Q97SE7:gatB; NbExp=2; IntAct=EBI-2207206, EBI-2207023;
Q97SE5:gatC; NbExp=2; IntAct=EBI-2207206, EBI-2207053;
Q97NG1:gltX; NbExp=2; IntAct=EBI-2207206, EBI-2207733;
Q97NV3:groS; NbExp=2; IntAct=EBI-2207206, EBI-2206949;
Q97S73:grpE; NbExp=2; IntAct=EBI-2207206, EBI-2207065;
Q97RS9:lysS; NbExp=3; IntAct=EBI-2207206, EBI-2207121;
P65887:purA; NbExp=2; IntAct=EBI-2207206, EBI-2206955;
P65946:pyrR; NbExp=2; IntAct=EBI-2207206, EBI-2207248;
Q97SR4:uppS; NbExp=2; IntAct=EBI-2207206, EBI-2206983;
Q97QP2:xerS; NbExp=2; IntAct=EBI-2207206, EBI-2207218;
-!- 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 cell surface, probably in complex with
plasminogen.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
Rule:MF_00318}.
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EMBL; AE005672; AAK75238.1; -; Genomic_DNA.
PIR; E95130; E95130.
RefSeq; WP_000022813.1; NZ_AKVY01000001.1.
PDB; 1W6T; X-ray; 2.10 A; A/B=1-434.
PDBsum; 1W6T; -.
ProteinModelPortal; Q97QS2; -.
SMR; Q97QS2; -.
IntAct; Q97QS2; 14.
PRIDE; Q97QS2; -.
EnsemblBacteria; AAK75238; AAK75238; SP_1128.
GeneID; 31536454; -.
KEGG; spn:SP_1128; -.
eggNOG; ENOG4105C70; Bacteria.
eggNOG; COG0148; LUCA.
HOGENOM; HOG000072174; -.
KO; K01689; -.
OMA; EFMIIPV; -.
SABIO-RK; Q97QS2; -.
UniPathway; UPA00109; UER00187.
EvolutionaryTrace; Q97QS2; -.
Proteomes; UP000000585; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR034390; Enolase-like_superfamily.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SFLD; SFLDG00178; enolase; 1.
SFLD; SFLDS00001; Enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Glycolysis; Lyase; Magnesium; Metal-binding; Secreted; Virulence.
CHAIN 1 434 Enolase.
/FTId=PRO_0000133980.
REGION 55 63 Antigenic epitope.
REGION 370 373 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00318}.
MOTIF 248 256 Plasminogen-binding.
ACT_SITE 205 205 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
ACT_SITE 343 343 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 242 242 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 291 291 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 318 318 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 155 155 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 164 164 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 291 291 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 318 318 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 343 343 Substrate (covalent); in inhibited form.
{ECO:0000255|HAMAP-Rule:MF_00318}.
BINDING 394 394 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
MUTAGEN 251 251 K->L: Great decrease in ability to bind
plasminogen. Decrease in virulence; when
associated with G-252 and L-254.
{ECO:0000269|PubMed:12828639}.
MUTAGEN 252 252 E->G: Great decrease in ability to bind
plasminogen. Decrease in virulence; when
associated with L-251 and L-254.
{ECO:0000269|PubMed:12828639}.
MUTAGEN 254 254 K->L: Great decrease in ability to bind
plasminogen. Decrease in virulence; when
associated with L-251 and G-252.
{ECO:0000269|PubMed:12828639}.
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.
{ECO:0000269|PubMed:11442827,
ECO:0000269|PubMed:12828639}.
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.
{ECO:0000269|PubMed:11442827,
ECO:0000269|PubMed:12828639}.
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.
{ECO:0000269|PubMed:11442827,
ECO:0000269|PubMed:12828639}.
CONFLICT 2 2 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 20 20 T -> P (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 24 24 E -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 3 13 {ECO:0000244|PDB:1W6T}.
STRAND 19 27 {ECO:0000244|PDB:1W6T}.
STRAND 32 36 {ECO:0000244|PDB:1W6T}.
HELIX 59 61 {ECO:0000244|PDB:1W6T}.
HELIX 65 73 {ECO:0000244|PDB:1W6T}.
HELIX 75 79 {ECO:0000244|PDB:1W6T}.
HELIX 87 98 {ECO:0000244|PDB:1W6T}.
TURN 104 106 {ECO:0000244|PDB:1W6T}.
HELIX 108 126 {ECO:0000244|PDB:1W6T}.
HELIX 130 135 {ECO:0000244|PDB:1W6T}.
STRAND 147 151 {ECO:0000244|PDB:1W6T}.
HELIX 153 155 {ECO:0000244|PDB:1W6T}.
STRAND 157 159 {ECO:0000244|PDB:1W6T}.
STRAND 163 168 {ECO:0000244|PDB:1W6T}.
HELIX 175 195 {ECO:0000244|PDB:1W6T}.
HELIX 215 228 {ECO:0000244|PDB:1W6T}.
TURN 233 235 {ECO:0000244|PDB:1W6T}.
STRAND 238 242 {ECO:0000244|PDB:1W6T}.
HELIX 245 248 {ECO:0000244|PDB:1W6T}.
HELIX 259 262 {ECO:0000244|PDB:1W6T}.
HELIX 271 284 {ECO:0000244|PDB:1W6T}.
STRAND 287 292 {ECO:0000244|PDB:1W6T}.
HELIX 299 309 {ECO:0000244|PDB:1W6T}.
TURN 310 312 {ECO:0000244|PDB:1W6T}.
STRAND 313 318 {ECO:0000244|PDB:1W6T}.
TURN 319 323 {ECO:0000244|PDB:1W6T}.
HELIX 325 334 {ECO:0000244|PDB:1W6T}.
STRAND 338 342 {ECO:0000244|PDB:1W6T}.
HELIX 344 347 {ECO:0000244|PDB:1W6T}.
HELIX 350 362 {ECO:0000244|PDB:1W6T}.
STRAND 366 370 {ECO:0000244|PDB:1W6T}.
HELIX 380 387 {ECO:0000244|PDB:1W6T}.
STRAND 392 394 {ECO:0000244|PDB:1W6T}.
STRAND 398 400 {ECO:0000244|PDB:1W6T}.
HELIX 401 417 {ECO:0000244|PDB:1W6T}.
HELIX 418 420 {ECO:0000244|PDB:1W6T}.
HELIX 425 428 {ECO:0000244|PDB:1W6T}.
SEQUENCE 434 AA; 47103 MW; 0D64F8F04BBB99C4 CRC64;
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYG
GLGTQKAVDN VNNIIAEAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR
AAADYLEIPL YSYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMILPV GAPTFKEALR
YGAEIFHALK KILKSRGLET AVGDEGGFAP RFEGTEDGVE TILAAIEAAG YVPGKDVFIG
FDCASSEFYD KERKVYDYTK FEGEGAAVRT SAEQIDYLEE LVNKYPIITI EDGMDENDWD
GWKALTERLG KKVQLVGDDF FVTNTDYLAR GIQEGAANSI LIKVNQIGTL TETFEAIEMA
KEAGYTAVVS HRSGETEDST IADIAVATNA GQIKTGSLSR TDRIAKYNQL LRIEDQLGEV
AEYRGLKSFY NLKK


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