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ENO_THEKO
ID   ENO_THEKO               Reviewed;         430 AA.
AC   Q5JEV6;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE            EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN   Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=TK2106;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC       into phosphoenolpyruvate. It is essential for the degradation of
CC       carbohydrates via glycolysis. {ECO:0000255|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:0000255|HAMAP-
CC         Rule:MF_00318};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00318}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
CC       Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
CC       {ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
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DR   EMBL; AP006878; BAD86295.1; -; Genomic_DNA.
DR   RefSeq; WP_011251056.1; NC_006624.1.
DR   AlphaFoldDB; Q5JEV6; -.
DR   SMR; Q5JEV6; -.
DR   IntAct; Q5JEV6; 1.
DR   MINT; Q5JEV6; -.
DR   STRING; 69014.TK2106; -.
DR   EnsemblBacteria; BAD86295; BAD86295; TK2106.
DR   GeneID; 3233916; -.
DR   KEGG; tko:TK2106; -.
DR   PATRIC; fig|69014.16.peg.2062; -.
DR   eggNOG; arCOG01169; Archaea.
DR   HOGENOM; CLU_031223_2_1_2; -.
DR   InParanoid; Q5JEV6; -.
DR   OMA; EFMIIPV; -.
DR   OrthoDB; 23221at2157; -.
DR   PhylomeDB; Q5JEV6; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000000536; Chromosome.
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; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 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   PANTHER; PTHR11902; PTHR11902; 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   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Secreted.
FT   CHAIN           1..430
FT                   /note="Enolase"
FT                   /id="PRO_0000134033"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         367..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ   SEQUENCE   430 AA;  46792 MW;  1CFF5D3C2D38257E CRC64;
     MENPFEITNV IAREILDSRG NPTVEVEVYT PISMGRAAVP SGASTGTHEA LELRDGGSRY
     HGKGVRRAVE NVNKIIAPEI IGMDVTWQRD IDTLMLELDG TENKSNLGAN AILGVSLAVA
     KAAANALGLP LYQYIGGTNA YVMPVPMSNV INGGVHAGNE LDFQEFMIMP VGADSFREAI
     RWVSETYHVL KKVIMEKYGR NAVNVGDEGG FAPPMKEVTE PLDVLIKAIE EAGYKPGDEI
     AFALDAASSE FFDGEKGKYV VAGKEYDKGE LLELYRELVT TYPIVSIEDP FHEEDWEGFV
     MITKELGSKV QIVGDDLFVT NPKRIRKGIE MGAANALLLK VNQIGTLSEA IDAAYTSFRA
     GYGVVVSHRS GETEDATIAD LAVALNAGQI KTGAPARSDR NAKYNQLIRI EEELEGIAVY
     PGKKFRNPFL
 
 
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