ENO_CLODI
ID ENO_CLODI Reviewed; 57 AA.
AC Q7M0V7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=2-phosphoglycerate dehydratase;
DE Flags: Fragments;
OS Clostridioides difficile (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496;
RN [1] {ECO:0000312|PIR:A61009}
RP PROTEIN SEQUENCE.
RC STRAIN=68750 {ECO:0000269|PubMed:2474559};
RX PubMed=2474559; DOI=10.1016/s0378-4347(00)82764-4;
RA Bisseret F., Keith G., Rihn B., Amiri I., Werneburg B., Girardot R.,
RA Baldacini O., Green G., Nguyen V.K., Monteil H.;
RT "Clostridium difficile toxin B: characterization and sequence of three
RT peptides.";
RL J. Chromatogr. A 490:91-100(1989).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis (By similarity).
CC {ECO:0000250|UniProtKB:P0A6P9}.
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;
CC Evidence={ECO:0000250|UniProtKB:P0A6P9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A6P9};
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC {ECO:0000250|UniProtKB:P0A6P9};
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:0000250|UniProtKB:P0A6P9}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface. Note=Fractions
CC of enolase are present in both the cytoplasm and on the cell surface.
CC The export of enolase possibly depends on the covalent binding to the
CC substrate; once secreted, it remains attached to the bacterial cell
CC surface (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255}.
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DR PIR; A61009; A61009.
DR AlphaFoldDB; Q7M0V7; -.
DR SMR; Q7M0V7; -.
DR UniPathway; UPA00109; UER00187.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.120; -; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR020810; Enolase_C.
DR Pfam; PF00113; Enolase_C; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW Metal-binding; Secreted.
FT CHAIN <1..>57
FT /note="Enolase"
FT /id="PRO_0000284772"
FT ACT_SITE 25
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 46..>48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT NON_CONS 38..39
FT /evidence="ECO:0000303|PubMed:2474559"
FT NON_CONS 48..49
FT /evidence="ECO:0000303|PubMed:2474559"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:2474559"
FT NON_TER 57
FT /evidence="ECO:0000312|PIR:A61009"
SQ SEQUENCE 57 AA; 6042 MW; 9CB0C9F1E449E6A0 CRC64;
MGAEVFHSLK KVLGEKGLAS GVGDEGGFAP NLGSNIRRAG YTAVISHRVA KYNQLLR
