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

 F7XUS2_MIDMI            Unreviewed;       412 AA.
F7XUS2;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
25-OCT-2017, entry version 46.
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:AEI88421.1};
OrderedLocusNames=midi_00099 {ECO:0000313|EMBL:AEI88421.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88421.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI88421.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI88421.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- 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: 2-phospho-D-glycerate = phosphoenolpyruvate +
H(2)O. {ECO:0000256|HAMAP-Rule:MF_00318}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|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: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}.
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EMBL; CP002130; AEI88421.1; -; Genomic_DNA.
RefSeq; WP_013950637.1; NC_015722.1.
ProteinModelPortal; F7XUS2; -.
STRING; 696127.midi_00099; -.
EnsemblBacteria; AEI88421; AEI88421; midi_00099.
KEGG; mmn:midi_00099; -.
eggNOG; ENOG4105C70; Bacteria.
eggNOG; COG0148; LUCA.
KO; K01689; -.
OMA; EFMIIPV; -.
OrthoDB; POG091H02DK; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000006639; 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: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; IPR034390; Enolase-like_superfamily.
InterPro; IPR020810; Enolase_C.
InterPro; IPR036849; Enolase_C-like_sf.
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 {ECO:0000313|Proteomes:UP000006639};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00318};
Lyase {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000313|EMBL:AEI88421.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
Reference proteome {ECO:0000313|Proteomes:UP000006639};
Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
DOMAIN 4 134 Enolase_N. {ECO:0000259|SMART:SM01193}.
DOMAIN 140 411 Enolase_C. {ECO:0000259|SMART:SM01192}.
REGION 364 367 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
ACT_SITE 205 205 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
ACT_SITE 337 337 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
METAL 242 242 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 285 285 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 312 312 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 285 285 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 312 312 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 337 337 Substrate (covalent); in inhibited form.
{ECO:0000256|HAMAP-Rule:MF_00318}.
BINDING 388 388 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
SEQUENCE 412 AA; 44526 MW; F6E1C6F027F3C00A CRC64;
MFTVQRVKAR QILDSRGNPT VEVDLALSSG AFGRAAVPSG ASVGSREAIE LRDDNKNIYA
GKGVLGAVKN VNTVIAARIL NKNFAEQKVF DAALIDLDGT ETKELLGANA ILAVSIAFAK
AAASQMNINL FQLISQKRYP VRMPTPMLNL INGGAHADNP IDIQEFMIVP KADNISSSLE
IAAAVFHNLK STLKKMGHST NVGDEGGFAP NLRSTELVLD ILSESILKSG LTLGENVEIA
LDIAATELFK GSFYHLKGEK TKLNSAEFAL YHKKLIDTYQ ICSIEDPMAE NDLEGWKIVT
DLIGNKVQLV GDDIFVTNKS ILEQGIKKGL ANALLVKMNQ VGTLTETLQA VDLAYQNGYE
TIVSHRSGET EDTTIAHLAV GIGSKYIKAG SICRTDRVCK YNELLRVSES LC


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