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ENO_BRUA1
ID   ENO_BRUA1               Reviewed;         425 AA.
AC   B2S5Y3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
GN   OrderedLocusNames=BAbS19_I10730;
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=430066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19;
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA   Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
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   -!- 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; CP000887; ACD72580.1; -; Genomic_DNA.
DR   RefSeq; WP_002964261.1; NC_010742.1.
DR   AlphaFoldDB; B2S5Y3; -.
DR   SMR; B2S5Y3; -.
DR   EnsemblBacteria; ACD72580; ACD72580; BAbS19_I10730.
DR   GeneID; 45052176; -.
DR   GeneID; 55590816; -.
DR   KEGG; bmc:BAbS19_I10730; -.
DR   HOGENOM; CLU_031223_2_1_5; -.
DR   OMA; EFMIIPV; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000002565; Chromosome 1.
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..425
FT                   /note="Enolase"
FT                   /id="PRO_1000115835"
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"
SQ   SEQUENCE   425 AA;  45261 MW;  A148573BD4696545 CRC64;
     MTAIIDIVGR EILDSRGNPT VEVDVVLEDG SFGRAAVPSG ASTGAHEAVE LRDGGSRYLG
     KGVEKAVEVV NGKIFDAIAG MDAESQLLID QTLIDLDGSA NKGNLGANAI LGVSLAVAKA
     AAQASGLPLY RYVGGTNAHV LPVPMMNIIN GGAHADNPID FQEFMILPVG ATSIREAVRY
     GSEVFHTLKK RLKDAGHNTN VGDEGGFAPN LKNAQAALDF IMESIEKAGF KPGEDIALGL
     DCAATEFFKD GNYVYEGERK TRDPKAQAKY LAKLASDYPI VTIEDGMAED DWEGWKYLTD
     LIGNKCQLVG DDLFVTNSAR LRDGIRLGVA NSILVKVNQI GSLSETLDAV ETAHKAGYTA
     VMSHRSGETE DSTIADLAVA TNCGQIKTGS LARSDRTAKY NQLIRIEEEL GKQARYAGRS
     ALKLL
 
 
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