ID   ENO_DORPE               Reviewed;         434 AA.
AC   O02654;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
OS   Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX   NCBI_TaxID=1051067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8587650; DOI=10.1007/bf00970738;
RA   Chun J.T., Gioio A.E., Crispino M., Giuditta A., Kaplan B.B.;
RT   "Characterization of squid enolase mRNA: sequence analysis, tissue
RT   distribution, and axonal localization.";
RL   Neurochem. Res. 20:923-930(1995).
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Mg(2+) is required for catalysis and for stabilizing the dimer.
CC       {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; S80961; AAB50731.1; -; mRNA.
DR   AlphaFoldDB; O02654; -.
DR   SMR; O02654; -.
DR   UniPathway; UPA00109; UER00187.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..434
FT                   /note="Enolase"
FT                   /id="PRO_0000134086"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         371..374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  47426 MW;  BFCFFD8B098B8DD2 CRC64;
     MVIKKVHSRQ IFDSRGNPTV EVDLWTDKGM FRAAVPSGAS TGIYEALEMR DKDAKNYHGK
     TLFNAVGNVN KIIAPALVDK KMDEKDQTAV DNFLLALDGT ENKNKLGANA ILGVSLAVCK
     AGAAAKGVPL YRHIADLAGN KEVILPVPAF NVINGGSHAG NKLAMQEFMI LPTGAKNFTE
     AMKMGTEVYH HLKSVIKKKY GQDACNVGDE GGFAPNILDN KEGLELLKTA IANAGYTAEI
     EIGMDVAASE FCKEKKYDLD FKNPDSNPND WLTSDQLADV YKDFVKNYPV VSIEDPFDQD
     DWEAYTKMTK DMDIQIVGDD LLVTNPKRVQ KGIDLKAANA LLLKVNQIGS VTESIQACKM
     SQDAGWGVMV SHRSGETEDT FIADLVVGLC TGQIKTGAPC RSERLAKYNQ ILRIEEELGD
     KAVFAGKKFR NPLK