ID   ENO_AERHH               Reviewed;         433 AA.
AC   A0KGH3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
GN   Name=eno; OrderedLocusNames=AHA_0821;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-
CC       phosphoglycerate into phosphoenolpyruvate. It is essential for the
CC       degradation of carbohydrates via glycolysis (By similarity).
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   -!- ENZYME REGULATION: The covalent binding to the substrate causes
CC       inactivation of the enzyme, and possibly serves as a signal for
CC       the export of the protein (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface.
CC       Note=Fractions of enolase are present in both the cytoplasm and on
CC       the cell surface. The export of enolase possibly depends on the
CC       covalent binding to the substrate; once secreted, it remains
CC       attached to the bacterial cell surface (By similarity).
CC   -!- SIMILARITY: Belongs to the enolase family.
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DR   EMBL; CP000462; ABK35864.1; -; Genomic_DNA.
DR   RefSeq; YP_855364.1; -.
DR   SMR; A0KGH3; 2-433.
DR   GeneID; 4489301; -.
DR   GenomeReviews; CP000462_GR; AHA_0821.
DR   KEGG; aha:AHA_0821; -.
DR   TIGR; AHA_0821; -.
DR   OMA; A0KGH3; DIAVGTN.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_00318; -; 1.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Secreted.
FT   CHAIN         1    433       Enolase.
FT                                /FTId=PRO_0000280832.
FT   REGION      370    373       Substrate binding (By similarity).
FT   ACT_SITE    209    209       Proton donor (By similarity).
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   METAL       246    246       Magnesium (By similarity).
FT   METAL       291    291       Magnesium (By similarity).
FT   METAL       318    318       Magnesium (By similarity).
FT   BINDING     159    159       Substrate (By similarity).
FT   BINDING     168    168       Substrate (By similarity).
FT   BINDING     291    291       Substrate (By similarity).
FT   BINDING     318    318       Substrate (By similarity).
FT   BINDING     343    343       Substrate (covalent); in inhibited form
FT                                (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
SQ   SEQUENCE   433 AA;  45720 MW;  C311B54F0EFFB3D5 CRC64;
     MSKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL
     GKGVLKALEA VNGPIAQALL GKDAKDQATV DQIMIDLDGT ENKSKFGANA ILAVSLANAK
     AAAAAKGMPL YAHIAELNGT PGVYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLK
     EAVRMGAEVF HNLAKVLKSK GYNTAVGDEG GFAPNLKSNA EALEVIAEAV AAAGYKLGTD
     ITLAMDCAAS EFYDAEKKEY NLKGEGRVFT SNGFSDFLAD LTTKFPIVSI EDGLDESDWD
     GFAYQTAELG KKIQIVGDDL FVTNTKILKR GIDNGIANSI LIKFNQIGSL TETLAAIKMA
     KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRVAKYNQL IRIEEALGAK
     APFRGLKEVK NQA
//