ID   ENO_CAMFE               Reviewed;         207 AA.
AC   O30885;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
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: Fragment;
GN   Name=eno;
OS   Campylobacter fetus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=84-32 / 23D;
RX   PubMed=9393719; DOI=10.1128/jb.179.23.7523-7529.1997;
RA   Dworkin J., Shedd O.L., Blaser M.J.;
RT   "Nested DNA inversion of Campylobacter fetus S-layer genes is recA
RT   dependent.";
RL   J. Bacteriol. 179:7523-7529(1997).
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). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}.
CC       Cell surface {ECO:0000250}. Note=Fractions of enolase are present in
CC       both the cytoplasm and on the cell surface. The export of enolase
CC       possibly depends on the covalent binding to the substrate; once
CC       secreted, it remains attached to the cell surface (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; AF020677; AAB86924.1; -; Genomic_DNA.
DR   AlphaFoldDB; O30885; -.
DR   SMR; O30885; -.
DR   STRING; 983328.AFGH01000004_gene1013; -.
DR   UniPathway; UPA00109; UER00187.
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:InterPro.
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   Gene3D; 3.30.390.10; -; 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; IPR020811; Enolase_N.
DR   PANTHER; PTHR11902; PTHR11902; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Secreted.
FT   CHAIN           1..>207
FT                   /note="Enolase"
FT                   /id="PRO_0000133860"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         207
SQ   SEQUENCE   207 AA;  21833 MW;  B6752AC9624EB383 CRC64;
     MVIVKKISAI EVLDSRGNPT IKTKVELCDG SIGEAIVPSG ASTGKRERLE LRDGGEAFGG
     KGVLKAIKNV NSMIAEEICG KDAYNQKAID DAMLALDGTD NYSRIGANAV LGVSMAVARA
     AANSLNIPLY RYLGGANACT LPVPMFNIIN GGAHANNSVD FQEFMIMPFG FSKFSNALRA
     ATEVYQTLKK ILNDLGHSTA VGDEGGF