ENO_STRP6
ID ENO_STRP6 Reviewed; 435 AA.
AC Q5XD01; P82479;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=M6_Spy0577;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-10; 17-34; 106-140; 181-191; 197-224; 256-270;
RP 313-331; 345-395 AND 408-413, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=JRS4 / Serotype M6;
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
RN [3]
RP PROTEIN SEQUENCE OF 2-51; 195-209 AND 367-372, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND BINDING TO PLASMINOGEN.
RC STRAIN=D471 / Serotype M6;
RX PubMed=9603964; DOI=10.1074/jbc.273.23.14503;
RA Pancholi V., Fischetti V.A.;
RT "Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface
RT of pathogenic streptococci.";
RL J. Biol. Chem. 273:14503-14515(1998).
RN [4]
RP MUTAGENESIS OF LYS-428; LYS-434 AND LYS-435.
RC STRAIN=D471 / Serotype M6;
RX PubMed=14688086; DOI=10.1128/iai.72.1.94-105.2004;
RA Derbise A., Song Y.P., Parikh S., Fischetti V.A., Pancholi V.;
RT "Role of the C-terminal lysine residues of streptococcal surface enolase in
RT Glu- and Lys-plasminogen-binding activities of group A streptococci.";
RL Infect. Immun. 72:94-105(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. Binds plasminogen when expressed on the
CC bacterial cell surface, potentially allowing the bacterium to acquire
CC surface-associated proteolytic activity, which in turn contributes to
CC tissue invasion and virulence. {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:9603964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00318};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
CC -!- ACTIVITY REGULATION: The covalent binding to the substrate causes
CC inactivation of the enzyme, and possibly serves as a signal for the
CC export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.49 mM for 2-phospho-D-glycerate {ECO:0000269|PubMed:9603964};
CC Vmax=31.25 mmol/min/mg enzyme {ECO:0000269|PubMed:9603964};
CC Note=Catalytically active also when expressed on the bacterial cell
CC surface.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:9603964}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318,
CC ECO:0000269|PubMed:9603964}. Cell surface {ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:9603964}. Note=Fractions of enolase
CC are present in both the cytoplasm and on the cell surface. The export
CC of enolase possibly depends on the covalent binding to the substrate;
CC once secreted, it remains attached to the cell surface.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT86712.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP000003; AAT86712.1; ALT_FRAME; Genomic_DNA.
DR PDB; 3ZLF; X-ray; 2.15 A; A/B/C/D=1-435.
DR PDB; 3ZLG; X-ray; 2.10 A; A/B/C/D=1-435.
DR PDB; 3ZLH; X-ray; 2.90 A; A/B/C/D=1-435.
DR PDBsum; 3ZLF; -.
DR PDBsum; 3ZLG; -.
DR PDBsum; 3ZLH; -.
DR AlphaFoldDB; Q5XD01; -.
DR SMR; Q5XD01; -.
DR PRIDE; Q5XD01; -.
DR EnsemblBacteria; AAT86712; AAT86712; M6_Spy0577.
DR KEGG; spa:M6_Spy0577; -.
DR HOGENOM; CLU_031223_0_1_9; -.
DR SABIO-RK; Q5XD01; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000001167; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; IDA:CAFA.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:CAFA.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase;
KW Magnesium; Metal-binding; Secreted; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9603964, ECO:0000269|Ref.2"
FT CHAIN 2..435
FT /note="Enolase"
FT /id="PRO_0000133984"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 344
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 371..374
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT SITE 428
FT /note="Important for binding of plasminogen"
FT SITE 434
FT /note="Important for binding of plasminogen"
FT SITE 435
FT /note="Important for binding of plasminogen"
FT MUTAGEN 428
FT /note="K->L: No effect on catalytic activity; significant
FT decrease in the ability to bind Glu- and Lys-plasminogen."
FT /evidence="ECO:0000269|PubMed:14688086"
FT MUTAGEN 434
FT /note="K->L: No effect on catalytic activity; significant
FT decrease in the ability to bind Glu- and Lys-plasminogen."
FT /evidence="ECO:0000269|PubMed:14688086"
FT MUTAGEN 435
FT /note="K->L: No effect on catalytic activity; significant
FT decrease in the ability to bind Glu- and Lys-plasminogen."
FT /evidence="ECO:0000269|PubMed:14688086"
FT CONFLICT 42
FT /note="S -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="G -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:3ZLG"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3ZLG"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:3ZLG"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3ZLG"
FT TURN 320..324
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:3ZLG"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 402..418
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:3ZLG"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3ZLF"
SQ 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
