ID   ENO_ALLMI               Reviewed;         395 AA.
AC   P42897;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 90.
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;
DE   Flags: Fragment;
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8146164; DOI=10.1073/pnas.91.7.2621;
RA   Hedges S.B.;
RT   "Molecular evidence for the origin of birds.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2621-2624(1994).
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; L28078; AAA53671.1; -; mRNA.
DR   PIR; I50026; I50026.
DR   AlphaFoldDB; P42897; -.
DR   SMR; P42897; -.
DR   PRIDE; P42897; -.
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..>395
FT                   /note="Enolase"
FT                   /id="PRO_0000134095"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         348..351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         395
SQ   SEQUENCE   395 AA;  42884 MW;  B43E91228E9110B5 CRC64;
     DLYTSKGLFR AAVPSGASTG IYEALELRDN DKTRFMGKGV SKAVAHVNKT IAPALISKNI
     SVVEQEKIDR LMLEMDGSEN KSKFGANAIL GVSLAVCKAG AAEKGVPLYR HIADLAGNPE
     VILPVPAFNV INGGSHAGNK LAMQEFMILP VGAESFKEAM RIGAEVYHNL KNVIKEKYGK
     DATNVGDEGG FAPNILENKE ALELLKNAIN KAGYSDKIVI GMDVAASEFY RDGKYDLDFK
     SPDDPSRYIT PDQLADLYKS FVKNYPVVSI EDPFDQDDWA AWKKFTASVG IQVVGDDLTV
     TNPKRIAKAV DDKACNCLLL KVNQIGSVTE SLQACKLAQS NGWGVMVSHR SGETEDTFIA
     DLVVGLCTGQ IKTGAPCRSE RLAKYNQILR IEEEL