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

 ENO_STRP6               Reviewed;         435 AA.
Q5XD01; P82479;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 107.
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=M6_Spy0577;
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=286636;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-946 / MGAS10394;
PubMed=15272401; DOI=10.1086/422697;
Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
"Progress toward characterization of the group A Streptococcus
metagenome: complete genome sequence of a macrolide-resistant serotype
M6 strain.";
J. Infect. Dis. 190:727-738(2004).
[2]
PROTEIN SEQUENCE OF 2-10; 17-34; 106-140; 181-191; 197-224; 256-270;
313-331; 345-395 AND 408-413, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=JRS4 / Serotype M6;
Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
VanBogelen R.A.;
"Two-dimensional gel electrophoresis map of Streptococcus pyogenes
proteins.";
Submitted (MAY-2000) to UniProtKB.
[3]
PROTEIN SEQUENCE OF 2-51; 195-209 AND 367-372, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND BINDING TO
PLASMINOGEN.
STRAIN=D471 / Serotype M6;
PubMed=9603964; DOI=10.1074/jbc.273.23.14503;
Pancholi V., Fischetti V.A.;
"Alpha-enolase, a novel strong plasmin(ogen) binding protein on the
surface of pathogenic streptococci.";
J. Biol. Chem. 273:14503-14515(1998).
[4]
MUTAGENESIS OF LYS-428; LYS-434 AND LYS-435.
STRAIN=D471 / Serotype M6;
PubMed=14688086; DOI=10.1128/IAI.72.1.94-105.2004;
Derbise A., Song Y.P., Parikh S., Fischetti V.A., Pancholi V.;
"Role of the C-terminal lysine residues of streptococcal surface
enolase in Glu- and Lys-plasminogen-binding activities of group A
streptococci.";
Infect. Immun. 72:94-105(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 on the bacterial cell surface, potentially allowing
the bacterium to acquire surface-associated proteolytic activity,
which in turn contributes to tissue invasion and virulence.
{ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:9603964}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318}.
-!- 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=1.49 mM for 2-phospho-D-glycerate
{ECO:0000269|PubMed:9603964};
Vmax=31.25 mmol/min/mg enzyme {ECO:0000269|PubMed:9603964};
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}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318,
ECO:0000269|PubMed:9603964}. Secreted {ECO:0000255|HAMAP-
Rule:MF_00318, ECO:0000269|PubMed:9603964}. Cell surface
{ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:9603964}.
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.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- SEQUENCE CAUTION:
Sequence=AAT86712.1; Type=Frameshift; Positions=40; Evidence={ECO:0000305};
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EMBL; CP000003; AAT86712.1; ALT_FRAME; Genomic_DNA.
PDB; 3ZLF; X-ray; 2.15 A; A/B/C/D=1-435.
PDB; 3ZLG; X-ray; 2.10 A; A/B/C/D=1-435.
PDB; 3ZLH; X-ray; 2.90 A; A/B/C/D=1-435.
PDBsum; 3ZLF; -.
PDBsum; 3ZLG; -.
PDBsum; 3ZLH; -.
ProteinModelPortal; Q5XD01; -.
SMR; Q5XD01; -.
EnsemblBacteria; AAT86712; AAT86712; M6_Spy0577.
KEGG; spa:M6_Spy0577; -.
HOGENOM; HOG000072174; -.
KO; K01689; -.
SABIO-RK; Q5XD01; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000001167; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
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.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9603964,
ECO:0000269|Ref.2}.
CHAIN 2 435 Enolase.
/FTId=PRO_0000133984.
REGION 371 374 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00318}.
ACT_SITE 205 205 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
ACT_SITE 344 344 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 243 243 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 292 292 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 319 319 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 292 292 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 319 319 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 344 344 Substrate (covalent); in inhibited form.
{ECO:0000255|HAMAP-Rule:MF_00318}.
BINDING 395 395 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
SITE 428 428 Important for binding of plasminogen.
SITE 434 434 Important for binding of plasminogen.
SITE 435 435 Important for binding of plasminogen.
MUTAGEN 428 428 K->L: No effect on catalytic activity;
significant decrease in the ability to
bind Glu- and Lys-plasminogen.
{ECO:0000269|PubMed:14688086}.
MUTAGEN 434 434 K->L: No effect on catalytic activity;
significant decrease in the ability to
bind Glu- and Lys-plasminogen.
{ECO:0000269|PubMed:14688086}.
MUTAGEN 435 435 K->L: No effect on catalytic activity;
significant decrease in the ability to
bind Glu- and Lys-plasminogen.
{ECO:0000269|PubMed:14688086}.
CONFLICT 42 42 S -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 44 44 G -> T (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 367 367 T -> S (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 3 13 {ECO:0000244|PDB:3ZLG}.
STRAND 19 27 {ECO:0000244|PDB:3ZLG}.
STRAND 32 36 {ECO:0000244|PDB:3ZLG}.
STRAND 44 47 {ECO:0000244|PDB:3ZLG}.
HELIX 59 61 {ECO:0000244|PDB:3ZLG}.
HELIX 65 73 {ECO:0000244|PDB:3ZLG}.
HELIX 75 79 {ECO:0000244|PDB:3ZLG}.
HELIX 87 98 {ECO:0000244|PDB:3ZLG}.
TURN 104 106 {ECO:0000244|PDB:3ZLG}.
HELIX 108 126 {ECO:0000244|PDB:3ZLG}.
HELIX 130 135 {ECO:0000244|PDB:3ZLG}.
STRAND 144 151 {ECO:0000244|PDB:3ZLG}.
HELIX 153 155 {ECO:0000244|PDB:3ZLG}.
STRAND 157 159 {ECO:0000244|PDB:3ZLG}.
STRAND 163 168 {ECO:0000244|PDB:3ZLG}.
HELIX 175 195 {ECO:0000244|PDB:3ZLG}.
HELIX 215 228 {ECO:0000244|PDB:3ZLG}.
STRAND 237 243 {ECO:0000244|PDB:3ZLG}.
HELIX 246 249 {ECO:0000244|PDB:3ZLG}.
TURN 252 255 {ECO:0000244|PDB:3ZLG}.
STRAND 256 258 {ECO:0000244|PDB:3ZLG}.
HELIX 260 263 {ECO:0000244|PDB:3ZLG}.
HELIX 272 285 {ECO:0000244|PDB:3ZLG}.
STRAND 288 293 {ECO:0000244|PDB:3ZLG}.
HELIX 300 310 {ECO:0000244|PDB:3ZLG}.
TURN 311 313 {ECO:0000244|PDB:3ZLG}.
STRAND 314 319 {ECO:0000244|PDB:3ZLG}.
TURN 320 324 {ECO:0000244|PDB:3ZLG}.
HELIX 326 334 {ECO:0000244|PDB:3ZLG}.
STRAND 339 343 {ECO:0000244|PDB:3ZLG}.
HELIX 345 348 {ECO:0000244|PDB:3ZLG}.
HELIX 351 363 {ECO:0000244|PDB:3ZLG}.
STRAND 367 371 {ECO:0000244|PDB:3ZLG}.
HELIX 381 388 {ECO:0000244|PDB:3ZLG}.
STRAND 393 395 {ECO:0000244|PDB:3ZLG}.
STRAND 399 401 {ECO:0000244|PDB:3ZLG}.
HELIX 402 418 {ECO:0000244|PDB:3ZLG}.
HELIX 419 421 {ECO:0000244|PDB:3ZLG}.
HELIX 426 429 {ECO:0000244|PDB:3ZLG}.
HELIX 431 433 {ECO:0000244|PDB:3ZLF}.
SEQUENCE 435 AA; 47355 MW; 5E285F357966C572 CRC64;
MSIITDVYAR EVLDSRGNPT LEVEVYTESG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYL
GLGTQKAVDN VNNIIAKAII GYDVRDQQAI DRAMIALDGT PNKGKLGANA ILGVSIAVAR
AAADYLEVPL YTYLGGFNTK VLPTPMMNII NGGSHSDAPI AFQEFMIMPV GAPTFKEGLR
WGAEVFHALK KILKERGLVT AVGDEGGFAP KFEGTEDGVE TILKAIEAAG YEAGENGIMI
GFDCASSEFY DKERKVYDYT KFEGEGAAVR TSAEQVDYLE ELVNKYPIIT IEDGMDENDW
DGWKVLTERL GKRVQLVGDD FFVTNTEYLA RGIKENAANS ILIKVNQIGT LTETFEAIEM
AKEAGYTAVV SHRSGETEDS TIADIAVATN AGQIKTGSLS RTDRIAKYNQ LLRIEDQLGE
VAQYKGIKSF YNLKK


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