ID   ENOA_XENLA              Reviewed;         434 AA.
AC   P08734;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Alpha-enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
GN   Name=eno1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3390159; DOI=10.1042/bj2510031;
RA   Segil N., Shrutkowski A., Dworkin M.B., Dworkin-Rastl E.;
RT   "Enolase isoenzymes in adult and developing Xenopus laevis and
RT   characterization of a cloned enolase sequence.";
RL   Biochem. J. 251:31-39(1988).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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DR   EMBL; Y00718; CAA68706.1; -; mRNA.
DR   PIR; S00463; NOXL.
DR   RefSeq; XP_018082300.1; XM_018226811.1.
DR   AlphaFoldDB; P08734; -.
DR   SMR; P08734; -.
DR   PRIDE; P08734; -.
DR   DNASU; 380298; -.
DR   GeneID; 380298; -.
DR   CTD; 380298; -.
DR   Xenbase; XB-GENE-6256554; eno1.S.
DR   SABIO-RK; P08734; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 380298; Expressed in ovary and 19 other tissues.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..434
FT                   /note="Alpha-enolase"
FT                   /id="PRO_0000134106"
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;  47504 MW;  9126C2F39477E3A4 CRC64;
     MSIKNIRARE IFDSRGNPTV EVDLYTCKGL FRAAVPSGAS TGIYEALELR DNDKTRYLGK
     GVGRAVKYVN EFLGPALCTQ NLNVVEQEKI DKLMIEMDGT ENKSKFGANA LLGVSLAVCK
     AGAAEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGADSFKE
     AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA INKAGYPDKI
     VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ISPDKLAELY MSFVKNYPVV SIEDPFDQDH
     WEAWTKFTAA SGIQVVGDDL TVTNPKRIAK AVEEKACNCL LLKVNQIGTV TESLEACKLA
     QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK
     ARFAGKNFRK PVFN