ENO_LISMO
ID ENO_LISMO Reviewed; 430 AA.
AC P64074; Q928I3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=lmo2455;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP PROTEIN SEQUENCE OF 2-13, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, FUNCTION IN VIRULENCE, AND BINDING TO PLASMINOGEN.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=15378750; DOI=10.1002/pmic.200400928;
RA Schaumburg J., Diekmann O., Hagendorff P., Bergmann S., Rohde M.,
RA Hammerschmidt S., Jaensch L., Wehland J., Kaerst U.;
RT "The cell wall subproteome of Listeria monocytogenes.";
RL Proteomics 4:2991-3006(2004).
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). Binds plasminogen when
CC expressed on the bacterial cell surface, potentially allowing the
CC bacterium to acquire surface-associated proteolytic activity, which in
CC turn contributes to tissue invasion and virulence. {ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:15378750}.
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 -!- 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:15378750}. Secreted {ECO:0000255|HAMAP-
CC Rule:MF_00318, ECO:0000269|PubMed:15378750}. Cell surface
CC {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15378750}.
CC Note=Fractions of enolase are present in both the cytoplasm and on the
CC cell surface. The export of enolase possibly depends on the covalent
CC binding to the substrate; once secreted, it remains attached to the
CC cell surface.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; AL591983; CAD00533.1; -; Genomic_DNA.
DR PIR; AG1381; AG1381.
DR RefSeq; NP_465978.1; NC_003210.1.
DR RefSeq; WP_003727923.1; NZ_CP023861.1.
DR AlphaFoldDB; P64074; -.
DR SMR; P64074; -.
DR STRING; 169963.lmo2455; -.
DR PaxDb; P64074; -.
DR EnsemblBacteria; CAD00533; CAD00533; CAD00533.
DR GeneID; 61190324; -.
DR GeneID; 987382; -.
DR KEGG; lmo:lmo2455; -.
DR PATRIC; fig|169963.11.peg.2514; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_9; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P64074; -.
DR BioCyc; LMON169963:LMO2455-MON; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW Metal-binding; Reference proteome; Secreted; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15378750"
FT CHAIN 2..430
FT /note="Enolase"
FT /id="PRO_0000133916"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 339
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 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 339
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 366..369
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ SEQUENCE 430 AA; 46472 MW; C53695893820F905 CRC64;
MSIITEVYAR EVLDSRGNPT VEVEVYTEAG AFGRALVPSG ASTGEYEAVE LRDGDKARYL
GKGVLKAVEN VNDIIADKII GFDVTDQIGI DKAMIELDGT PNKGKLGANA ILGVSLAAAR
AAADELGVHL YEYLGGVNGK VLPVPMMNIL NGGEHADNNV DVQEFMVMPV GAPNFKEALR
MGAEILHALK AVLKGKGLNT GVGDEGGFAP NLKSNEEALE TIMQAIKDAG YKPGEEVKLA
MDAASSEFYN RETGKYELKG EGVTRTSEEM VTWYEEMITK YPIISIEDGL DENDWDGFKL
LTERIGDRVQ LVGDDLFVTN TTKLKEGIEK GIANSILIKV NQIGTLTETL DAIEMAKRAG
YTAVISHRSG ETEDSTIADI AVATNAGQIK TGAPTRTDRV AKYNQLLRIE DNLADLAEYH
GNDTFYNLKK
