ID   ENOA_ALLMI              Reviewed;         434 AA.
AC   Q9PVK2;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 48.
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   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Crocodylidae; Alligatorinae; Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=99439677; 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: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the enolase family.
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DR   EMBL; AF072586; AAD41643.1; -; mRNA.
DR   HSSP; P56252; 1PDZ.
DR   SMR; Q9PVK2; 2-433.
DR   HOVERGEN; Q9PVK2; -.
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:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
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_0000134102.
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;  47322 MW;  DFD23524BECF5ECA CRC64;
     MSILKIHARE IFDSRGNPTV EVDLYTSKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK
     GVSKAVAHVN KTIAPALISK NISVVEQEKI DRLMLEMDGS ENKSKFGANA ILGVSLAVCK
     AGAAEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFKE
     AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKNA INKAGYSDKI
     VIGMDVAASE FYRDGKYDLD FKSPDDPSRY ITPDQLADLY KSFVKNYPVV SIEDPFDQDD
     WAAWKKFTAS VGIQVVGDDL TVTNPKRIAK AVDDKACNCL LLKVNQIGSV TESLQACKLA
     QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK
     ARFAGRNFRN PRIN
//