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Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

 A0A0A3J4Z2_9BACI        Unreviewed;       430 AA.
A0A0A3J4Z2;
04-FEB-2015, integrated into UniProtKB/TrEMBL.
04-FEB-2015, sequence version 1.
08-MAY-2019, entry version 27.
RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318};
EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318};
AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318};
AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318};
Name=eno {ECO:0000256|HAMAP-Rule:MF_00318,
ECO:0000313|EMBL:KGR90750.1};
ORFNames=CD30_09430 {ECO:0000313|EMBL:KGR90750.1};
Lysinibacillus massiliensis 4400831 = CIP 108448 = CCUG 49529.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
Lysinibacillus.
NCBI_TaxID=1211035 {ECO:0000313|EMBL:KGR90750.1, ECO:0000313|Proteomes:UP000030595};
[1] {ECO:0000313|EMBL:KGR90750.1, ECO:0000313|Proteomes:UP000030595}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CCUG 49529 {ECO:0000313|EMBL:KGR90750.1,
ECO:0000313|Proteomes:UP000030595};
Zhang F., Wang G., Zhang L.;
"Draft genome sequence of Lysinibacillus massiliensis CCUG 49529.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the reversible conversion of 2-
phosphoglycerate into phosphoenolpyruvate. It is essential for the
degradation of carbohydrates via glycolysis. {ECO:0000256|HAMAP-
Rule:MF_00318}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000256|HAMAP-
Rule:MF_00318};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00318};
-!- ACTIVITY REGULATION: The covalent binding to the substrate causes
inactivation of the enzyme, and possibly serves as a signal for
the export of the protein. {ECO:0000256|HAMAP-Rule:MF_00318}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|HAMAP-
Rule:MF_00318}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}.
Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface
{ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
present in both the cytoplasm and on the cell surface. The export
of enolase possibly depends on the covalent binding to the
substrate; once secreted, it remains attached to the cell surface.
{ECO:0000256|HAMAP-Rule:MF_00318}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000256|HAMAP-
Rule:MF_00318}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KGR90750.1}.
-----------------------------------------------------------------------
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EMBL; JPVQ01000014; KGR90750.1; -; Genomic_DNA.
RefSeq; WP_036175663.1; NZ_JPVQ01000014.1.
STRING; 1211035.CD30_09430; -.
EnsemblBacteria; KGR90750; KGR90750; CD30_09430.
OrthoDB; 533698at2; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000030595; Unassembled WGS sequence.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SFLD; SFLDG00178; enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000030595};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00318};
Lyase {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000313|EMBL:KGR90750.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
Reference proteome {ECO:0000313|Proteomes:UP000030595};
Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
DOMAIN 4 135 Enolase_N. {ECO:0000259|SMART:SM01193}.
DOMAIN 140 428 Enolase_C. {ECO:0000259|SMART:SM01192}.
REGION 367 370 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
ACT_SITE 206 206 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
ACT_SITE 340 340 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
METAL 243 243 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 288 288 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 315 315 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
BINDING 156 156 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 165 165 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 288 288 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 315 315 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 340 340 Substrate (covalent); in inhibited form.
{ECO:0000256|HAMAP-Rule:MF_00318}.
BINDING 391 391 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
SEQUENCE 430 AA; 46403 MW; 0433F7118B2BCCC4 CRC64;
MPFITQVYAR EVLDSRGNPT VEVEVFTESG AFGRAIVPSG ASTGEYEAVE LRDGDKSRYL
GKGVLNAVEN VNTIIAEELE GNYSVLDQVV IDKALIELDG TENKGKLGAN AILGVSLAVA
HAAADYLDIP LYQYLGGVNA KQLPVPMMNI LNGGAHADNN VDIQEFMVMP VGAESFRHAL
RMGAEIFHNL KAVLKEKGYN TAVGDEGGFA PNLGSNEEAI TVILEAIEKA GYKAGEEVRI
ALDVASSELY NKEDGKYHLS GEGVVKTSEE MVAWYDELTS KYPIISIEDG LDENDWAGHK
LLTERIGKRV QLVGDDLFVT NTNKLAQGIE QGVGNSILIK VNQIGTLTET LDAIEMAKRA
GYTAVISHRS GESEDSTIAD IAVATNAGQI KTGAPSRTDR VAKYNQLLRI EDQLSATAQY
LGLKSFYNLK


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