ENOA_PYTRG
ID ENOA_PYTRG Reviewed; 434 AA.
AC Q9W7L0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Phosphopyruvate hydratase;
OS Python regius (Ball python) (Boa regia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Henophidia; Pythonidae; Python.
OX NCBI_TaxID=51751;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=10508547; DOI=10.1006/mpev.1999.0640;
RA Mannen H., Li S.S.-L.;
RT "Molecular evidence for a clade of turtles.";
RL Mol. Phylogenet. Evol. 13:144-148(1999).
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=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {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; AF072589; AAD41646.1; -; mRNA.
DR AlphaFoldDB; Q9W7L0; -.
DR SMR; Q9W7L0; -.
DR PRIDE; Q9W7L0; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..434
FT /note="Alpha-enolase"
FT /id="PRO_0000134103"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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 /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 47570 MW; F242F93E6D467033 CRC64;
MSILKIQARE IFDSRGNPTI EVDLYTKKGL FRAAVPSGAS TGIYEALELR DNDKTRFLGK
GVSKAVEHVN KTIAPALVNK NVSVVEQEKI DKLMIEMDGS ENKSKFGANA ILGVSLAVCK
AGAAEKDIPL YRHIADLAGN KEVILPVPAF NVINGGSHAG NKLAMQEFMI LPIGAECFKE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA ISKAGYADKI
VIGMDVAASE FYRDGKYDLD FKSPDDRSRY ITPDQLADLY KGFVKNYPVV SIEDPFDQDD
WPAWKKFTAE SGIQVVGDDL TVTNPKRIAK AVQEKSCNCL LLKVNQIGSV TESLQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK
ARFAGRNFRN PRVN
