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

 ENO_EHRCJ               Reviewed;         421 AA.
Q3YRX9;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 1.
07-JUN-2017, entry version 91.
RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
Name=eno {ECO:0000255|HAMAP-Rule:MF_00318};
OrderedLocusNames=Ecaj_0489;
Ehrlichia canis (strain Jake).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Anaplasmataceae; Ehrlichia.
NCBI_TaxID=269484;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Jake;
PubMed=16707693; DOI=10.1128/JB.01837-05;
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
Kyrpides N.C.;
"The genome of the obligately intracellular bacterium Ehrlichia canis
reveals themes of complex membrane structure and immune evasion
strategies.";
J. Bacteriol. 188:4015-4023(2006).
-!- FUNCTION: Catalyzes the reversible conversion of 2-
phosphoglycerate into phosphoenolpyruvate. It is essential for the
degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00318};
-!- ENZYME 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:0000255|HAMAP-Rule:MF_00318}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
Rule:MF_00318}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
{ECO:0000255|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:0000255|HAMAP-Rule:MF_00318}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
Rule:MF_00318}.
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EMBL; CP000107; AAZ68526.1; -; Genomic_DNA.
RefSeq; WP_011304604.1; NC_007354.1.
ProteinModelPortal; Q3YRX9; -.
SMR; Q3YRX9; -.
STRING; 269484.Ecaj_0489; -.
EnsemblBacteria; AAZ68526; AAZ68526; Ecaj_0489.
KEGG; ecn:Ecaj_0489; -.
eggNOG; ENOG4105C70; Bacteria.
eggNOG; COG0148; LUCA.
HOGENOM; HOG000072174; -.
KO; K01689; -.
OMA; EFMIIPV; -.
OrthoDB; POG091H02DK; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000000435; Chromosome.
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:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; IPR034390; Enolase-like_superfamily.
InterPro; IPR020810; Enolase_C.
InterPro; IPR029065; Enolase_C-like.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
InterPro; IPR029017; Enolase_N-like.
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.
SFLD; SFLDS00001; Enolase; 1.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
Metal-binding; Secreted.
CHAIN 1 421 Enolase.
/FTId=PRO_0000267029.
REGION 364 367 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00318}.
ACT_SITE 207 207 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
ACT_SITE 337 337 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 244 244 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 285 285 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
METAL 312 312 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 157 157 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 166 166 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 285 285 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 312 312 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
BINDING 337 337 Substrate (covalent); in inhibited form.
{ECO:0000255|HAMAP-Rule:MF_00318}.
BINDING 388 388 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00318}.
SEQUENCE 421 AA; 46584 MW; 68054444A7ADF022 CRC64;
MSNITINKIL ARQILDSRGY PTIEAEVILS NNTKAKACVP SGASVGKFEA VELRDNDKNY
YNGYGVTKAV NIINSEIAPQ IIGMNTLNQE KIDNTLIKID GTDNKSRIGA NSTLAVSLAI
AKAAASTLNI PLYQYIGGIN AKVLPTPLIN VINGGMHADN NLDFQEFMII PNGANKFEDA
MRMSAEVFFK LKQILKSKQY NTSVGDEGGF APNIKTNNEV FEIIIDAIEK SGYKMYKDFS
LGLDVAASTF YKDQKYKFAD YEFNTQELVE YYKNITSQYP IISLEDPIAE EDTNGWKLIT
QELGNKIQIV GDDLFVTNCK LIQNGIQNNL ANAVLIKPNQ IGTLTETFNA IRLAQKNNYN
TIISHRSGET EDTTISHIAV AANCGQIKTG SLSRSERLAK YNELLYIEKQ LDISAIYYGA
L


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