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   16-JUN-2009, entry version 67.
DE   RecName: Full=Alpha-enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=eno1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88268812; PubMed=3390159;
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: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer.
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.
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DR   EMBL; Y00718; CAA68706.1; -; mRNA.
DR   PIR; S00463; NOXL.
DR   HSSP; P56252; 1PDZ.
DR   SMR; P08734; 2-431.
DR   HOVERGEN; P08734; -.
DR   BRENDA; 4.2.1.11; 648.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   PANTHER; PTHR11902; Enolase; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   ProDom; PD000902; Enolase; 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      1       Removed (By similarity).
FT   CHAIN         2    434       Alpha-enolase.
FT                                /FTId=PRO_0000134106.
FT   REGION      370    373       Substrate binding (By similarity).
FT   ACT_SITE    210    210       Proton donor (By similarity).
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   METAL       245    245       Magnesium (By similarity).
FT   METAL       293    293       Magnesium (By similarity).
FT   METAL       318    318       Magnesium (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     293    293       Substrate (By similarity).
FT   BINDING     318    318       Substrate (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
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
//