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Entry: A0A292Z7P5_9PSEU
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ID   A0A292Z7P5_9PSEU        Unreviewed;       430 AA.
AC   A0A292Z7P5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318};
DE            EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318};
GN   Name=eno {ECO:0000256|HAMAP-Rule:MF_00318};
GN   ORFNames=TOK_1181 {ECO:0000313|EMBL:GAY12634.1};
OS   Pseudonocardia sp. N23.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY12634.1, ECO:0000313|Proteomes:UP000222857};
RN   [1] {ECO:0000313|EMBL:GAY12634.1, ECO:0000313|Proteomes:UP000222857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N23 {ECO:0000313|EMBL:GAY12634.1,
RC   ECO:0000313|Proteomes:UP000222857};
RA   Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT   "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT   dioxane-degrading ability.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC       into phosphoenolpyruvate. It is essential for the degradation of
CC       carbohydrates via glycolysis. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC         ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00318};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00318};
CC   -!- ACTIVITY REGULATION: The covalent binding to the substrate causes
CC       inactivation of the enzyme, and possibly serves as a signal for the
CC       export of the protein. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031,
CC       ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}.
CC       Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface
CC       {ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC       present in both the cytoplasm and on the cell surface. The export of
CC       enolase possibly depends on the covalent binding to the substrate; once
CC       secreted, it remains attached to the cell surface. {ECO:0000256|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC       {ECO:0000256|ARBA:ARBA00009604, ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAY12634.1}.
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DR   EMBL; BEGX01000128; GAY12634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292Z7P5; -.
DR   OrthoDB; 9804716at2; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000222857; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   HAMAP; MF_00318; Enolase; 1.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   NCBIfam; TIGR01060; eno; 1.
DR   PANTHER; PTHR11902; ENOLASE; 1.
DR   PANTHER; PTHR11902:SF1; ENOLASE; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   SFLD; SFLDF00002; enolase; 1.
DR   SFLD; SFLDG00178; enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00318};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00318};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00318};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00318};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN          4..134
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          139..424
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        336
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         363..366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   430 AA;  45135 MW;  38A40D7FDEA692D9 CRC64;
     MAVIEQVGAR EILDSRGNPT VEVEVALDDG TLARAAVPSG ASTGEHEAVE LRDGDAKRYG
     GKGVEKAVMA VLDEIGPELT GMEAVDQRLV DQRLVDLDGT NDKSRLGANA LLGVSLAVAK
     AAAESSGLEL FRYIGGPNAH VLPVPMMNIL NGGAHADTSV DVQEFMIAPI GAESFREALR
     WGTEVYHALK SVLKKNGLAT GLGDEGGFAP DVAGGTRGAL ELIASAVETT GFTLGTDVVL
     ALDVAATEFH DKGDYSYEGK KLSSADLSAV WASLVDDFPL VSIEDPLSED DWDGWVALTS
     AIGDKVQIVG DDLFVTNPER LEDGILRGAA NALLVKVNQI GTLSETLDAV TLAHSSGYRC
     MMSHRSGETE DTTIADLAVA TGCGQIKTGA PARSERVAKY NQLLRIEEAL GDAARYAGEL
     AFPRYAVPQG
//
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