ENO_LEGPH
ID ENO_LEGPH Reviewed; 422 AA.
AC Q5ZTX1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=lpg2037;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC into phosphoenolpyruvate. It is essential for the degradation of
CC carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318}.
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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00318}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC present in both the cytoplasm and on the cell surface. The export of
CC enolase possibly depends on the covalent binding to the substrate; once
CC secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC Rule:MF_00318}.
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DR EMBL; AE017354; AAU28106.1; -; Genomic_DNA.
DR RefSeq; WP_010947753.1; NC_002942.5.
DR RefSeq; YP_096053.1; NC_002942.5.
DR PDB; 6NB2; X-ray; 1.85 A; A/B=1-422.
DR PDBsum; 6NB2; -.
DR AlphaFoldDB; Q5ZTX1; -.
DR SMR; Q5ZTX1; -.
DR STRING; 272624.lpg2037; -.
DR PaxDb; Q5ZTX1; -.
DR PRIDE; Q5ZTX1; -.
DR EnsemblBacteria; AAU28106; AAU28106; lpg2037.
DR GeneID; 66491169; -.
DR KEGG; lpn:lpg2037; -.
DR PATRIC; fig|272624.6.peg.2134; -.
DR eggNOG; COG0148; Bacteria.
DR HOGENOM; CLU_031223_2_1_6; -.
DR OMA; EFMIIPV; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000000609; 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; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
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; Glycolysis; Lyase; Magnesium; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..422
FT /note="Enolase"
FT /id="PRO_0000133909"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT ACT_SITE 336
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 336
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 363..366
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT STRAND 2..12
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:6NB2"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 107..125
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:6NB2"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:6NB2"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:6NB2"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:6NB2"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:6NB2"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:6NB2"
SQ SEQUENCE 422 AA; 46217 MW; 455A6CE57E61BB28 CRC64;
MHIHKIQARE ILDSRGNPTI EADVTLTTGI IGRASVPSGA STGSREACEL RDNDPKRYAG
KGVQKAVKHV NNEINQALQG LSVEDQENLD RILCQLDNTE NKSHLGANAI LATSLACARA
RALSLNQPLY MTLNQGDMMT MPVPMMNILN GGAHADNNVD IQEFMIMPIG APDFPVALQM
GTEIFHVLKS VLKKQGLNTA VGDEGGFAPN IQSNRQALDL LSEAIEKAGF RLGEDIVFAL
DVAASELFNE GFYHMYSENQ KFDSHQLIEY YANLISSYPI VSIEDGLDEK DWSGWKQLTT
HLGNKVQLVG DDLFVTNPKI LREGIAQGIA NAILIKVNQI GTLSETRQAI KLAYDNGYRC
VMSHRSGETE DTFIADLAVA SGCGQIKTGS LCRTDRTAKY NQLLRINELA SLPYAGKNIL
KR
