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

 A0A1B4X3L0_9PSED        Unreviewed;       429 AA.
A0A1B4X3L0;
02-NOV-2016, integrated into UniProtKB/TrEMBL.
02-NOV-2016, sequence version 1.
22-NOV-2017, entry version 8.
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};
ORFNames=LAB08_4109 {ECO:0000313|EMBL:BAV29379.1};
Pseudomonas sp. LAB-08.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=143813 {ECO:0000313|EMBL:BAV29379.1};
[1] {ECO:0000313|EMBL:BAV29379.1}
NUCLEOTIDE SEQUENCE.
Suzuki K., Fatma A., Inuzuka Y., Tashiro Y., Futamata H.;
"Draft genome sequence of Pseudomonassp. LAB-08 isolated from TCE
contaminated aquifer soil.";
Submitted (APR-2016) 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};
-!- 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}.
-!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
complex involved in RNA processing and mRNA degradation.
{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; AP017423; BAV29379.1; -; Genomic_DNA.
UniPathway; UPA00109; UER00187.
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.
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.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
3: Inferred from homology;
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00318};
Lyase {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000313|EMBL:BAV29379.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
Pyruvate {ECO:0000313|EMBL:BAV29379.1};
Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
DOMAIN 4 134 Enolase_N. {ECO:0000259|SMART:SM01193}.
DOMAIN 143 429 Enolase_C. {ECO:0000259|SMART:SM01192}.
REGION 368 371 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
ACT_SITE 209 209 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
ACT_SITE 341 341 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-1}.
METAL 246 246 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 289 289 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
METAL 316 316 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00318}.
BINDING 159 159 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 168 168 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 289 289 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 316 316 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
BINDING 341 341 Substrate (covalent); in inhibited form.
{ECO:0000256|HAMAP-Rule:MF_00318}.
BINDING 392 392 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00318,
ECO:0000256|PIRSR:PIRSR001400-2}.
SEQUENCE 429 AA; 45557 MW; E892D7AB57FA18C5 CRC64;
MAKIVDIKGR EVLDSRGNPT VEADVLLDNG IIGSACAPSG ASTGSREALE LRDGDKSRYL
GKGVLKAVAN INGPIRDLLK GTDPSDQKAL DLAMIKLDGT ENKATLGANA ILAVSLAAAK
AAAQDQDLPL YAHIANLNGT PGVYSMPVPM MNIINGGEHA DNNVDIQEFM VQPVGAKSFS
EGLRMGTEIF HHLKAVLKAR GLSTAVGDEG GFAPNLASNE DALKVISEAV ANAGYKLGTD
VTLALDCAAS EFYEDGKYNL SGEGQVFTAE GFADYLKGLT ERYPIISIED GLDESDWAGW
KILTDKIGEK TQLVGDDLFV TNTKILKEGI DKKIANSILI KFNQIGTLTE TLEAIQMAKA
AGYTAVISHR SGETEDSTIA DLAVGTSAGQ IKTGSLCRSD RVSKYNQLLR IEEQLNGKAK
YNGRSEFRG


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