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

 I3R8A0_HALMT            Unreviewed;       399 AA.
I3R8A0;
05-SEP-2012, integrated into UniProtKB/TrEMBL.
05-SEP-2012, sequence version 1.
12-SEP-2018, entry version 50.
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:AFK20460.1};
OrderedLocusNames=HFX_2784 {ECO:0000313|EMBL:AFK20460.1};
ORFNames=BM92_14725 {ECO:0000313|EMBL:AHZ23822.1},
C439_15710 {ECO:0000313|EMBL:ELZ98245.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK20460.1, ECO:0000313|Proteomes:UP000006469};
[1] {ECO:0000313|EMBL:AFK20460.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20460.1};
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2] {ECO:0000313|EMBL:AFK20460.1, ECO:0000313|Proteomes:UP000006469}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000006469}, and
CGMCC 1.2087 {ECO:0000313|EMBL:AFK20460.1};
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3] {ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000011603};
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:ELZ98245.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ATCC 33500 {ECO:0000313|EMBL:ELZ98245.1};
PubMed=25393412;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[5] {ECO:0000313|EMBL:AHZ23822.1, ECO:0000313|Proteomes:UP000027075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ23822.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000027075};
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AFK20460.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
Wang L., Yang H., Xiang H.;
Submitted (MAY-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: 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};
-!- 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}.
-----------------------------------------------------------------------
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EMBL; CP001868; AFK20460.1; -; Genomic_DNA.
EMBL; CP007551; AHZ23822.1; -; Genomic_DNA.
EMBL; AOLO01000013; ELZ98245.1; -; Genomic_DNA.
RefSeq; WP_004060262.1; NZ_CP007551.1.
EnsemblBacteria; AFK20460; AFK20460; HFX_2784.
EnsemblBacteria; AHZ23822; AHZ23822; BM92_14725.
EnsemblBacteria; ELZ98245; ELZ98245; C439_15710.
GeneID; 13028940; -.
KEGG; hme:HFX_2784; -.
PATRIC; fig|523841.21.peg.3170; -.
KO; K01689; -.
OMA; QEFLVVP; -.
OrthoDB; POG093Z03D9; -.
BioCyc; HMED523841:G1HBL-1944-MONOMER; -.
UniPathway; UPA00109; UER00187.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; 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; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR034390; Enolase-like_superfamily.
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.
SFLD; SFLDS00001; 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:UP000006469};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00318};
Lyase {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000313|EMBL:AFK20460.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
Pyruvate {ECO:0000313|EMBL:AFK20460.1};
Reference proteome {ECO:0000313|Proteomes:UP000006469};
Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
DOMAIN 4 124 Enolase_N. {ECO:0000259|SMART:SM01193}.
DOMAIN 130 398 Enolase_C. {ECO:0000259|SMART:SM01192}.
REGION 352 355 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
ACT_SITE 196 196 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
ACT_SITE 325 325 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
METAL 232 232 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 273 273 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 300 300 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
BINDING 146 146 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 155 155 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 273 273 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 300 300 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 325 325 Substrate (covalent); in inhibited form.
{ECO:0000256|HAMAP-Rule:MF_00318}.
BINDING 376 376 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
SEQUENCE 399 AA; 42064 MW; 36F3603B91D77A81 CRC64;
MTRITSVSLR RVLDSRGNPT VEADVLTESG GFGRAAAPSG ASTGEYEAIE LPPTEAIAAA
RRHAVPRLVG EVHAGNQREV DAALRAADGS ENFSEIGANS AVAISMAAAK AGADVLGAPL
YQHLGGAFRG DNFPTPLGNV IGGGEHAKEA TNIQEFLAAP VGAPSVSEAV FANAKVHARA
SEILDERDVP AAKGDEGAWA PAVSDADAFE IMAEAVSDVE DELGFEIRFG LDIAASEMFE
DGVYHYGDET KTTDEQIDYV AEMVDEYDLV YVEDPLDEND YEGFAELTDR VGDRTLICGD
DLFVTNVDRL QDGIDVGAAN SILIKPNQIG TLTDAFDAVE LAARNGMDAV ISHRSGETED
TTIAHLAVAT DAPFIKTGTV QGERTAKLNE LIRIADDAV


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