ID   ENO_SHEB5               Reviewed;         431 AA.
AC   A3D795;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Sbal_3127;
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000563; ABN62608.1; -; Genomic_DNA.
DR   RefSeq; WP_006082616.1; NC_009052.1.
DR   AlphaFoldDB; A3D795; -.
DR   SMR; A3D795; -.
DR   STRING; 325240.Sbal_3127; -.
DR   EnsemblBacteria; ABN62608; ABN62608; Sbal_3127.
DR   GeneID; 11773332; -.
DR   KEGG; sbl:Sbal_3127; -.
DR   HOGENOM; CLU_031223_2_1_6; -.
DR   OMA; EFMIIPV; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000001557; 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   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Secreted.
FT   CHAIN           1..431
FT                   /note="Enolase"
FT                   /id="PRO_1000019245"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         368..371
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ   SEQUENCE   431 AA;  45818 MW;  D330B2C6D8406D45 CRC64;
     MAKIINVIGR EIMDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRYL
     GKGVLTAVAN VNDLIRTALL GKDATAQAEL DQIMIDLDGT ENKDKLGANA ILAVSLAAAK
     AAAAFKGIPL YAHIAELNGT PGQYSMPVPM MNILNGGEHA DNNVDIQEFM VQPVGAKTFR
     EALRMGAEIF HTLKKVLHDK GLSTSVGDEG GFAPNLASNA DALAIIKEAV ELAGYKLGTD
     VTLALDCAAS EFYKDGKYDL AGEGKVFDSN GFSDFLKSLA DQYPIVSIED GLDESDWDGW
     AYQTQIMGDK IQLVGDDLFV TNTKILTRGI ENGIANSILI KFNQIGSLTE TLAAIRMAKE
     AGYTAVISHR SGETEDSTIA DLAVGTAAGQ IKTGSLCRSD RVAKYNQLLR IEEQLGEKAP
     YRGLKEIKGQ A