ID   ENO2_CHLTE              Reviewed;         437 AA.
AC   Q8KG25;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 48.
DE   RecName: Full=Enolase 2;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phosphoglycerate dehydratase 2;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase 2;
GN   Name=eno2; Synonyms=eno-2; OrderedLocusNames=CT0145;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE006470; AAM71393.1; -; Genomic_DNA.
DR   RefSeq; NP_661051.1; -.
DR   HSSP; Q9NDH8; 1OEP.
DR   GeneID; 1007040; -.
DR   GenomeReviews; AE006470_GR; CT0145.
DR   KEGG; cte:CT0145; -.
DR   NMPDR; fig|194439.1.peg.145; -.
DR   TIGR; CT0145; -.
DR   HOGENOM; Q8KG25; -.
DR   BioCyc; CTEP194439:CT_0145-MON; -.
DR   GO; GO:0009986; C:cell surface; IEA:HAMAP.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Phosphoprotein; Secreted.
FT   CHAIN         1    437       Enolase 2.
FT                                /FTId=PRO_0000133869.
FT   REGION      376    379       Substrate binding (By similarity).
FT   ACT_SITE    204    204       Proton donor (By similarity).
FT   ACT_SITE    349    349       Proton acceptor (By similarity).
FT   METAL       251    251       Magnesium (By similarity).
FT   METAL       297    297       Magnesium (By similarity).
FT   METAL       324    324       Magnesium (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
FT   BINDING     163    163       Substrate (By similarity).
FT   BINDING     297    297       Substrate (By similarity).
FT   BINDING     324    324       Substrate (By similarity).
FT   BINDING     349    349       Substrate (covalent); in inhibited form
FT                                (By similarity).
FT   BINDING     400    400       Substrate (By similarity).
FT   MOD_RES     291    291       Phosphotyrosine (By similarity).
SQ   SEQUENCE   437 AA;  46946 MW;  7D9969C282B1CD8E CRC64;
     MSVITRIHAR QIMDSRGNPT VEVDVHTESS FGRAAVPSGA STGVHEAVEL RDKDKSVFLG
     KGVLKAVENV NTLINDALLG MDVTEQEAID AKLIELDGTP NKSKLGANAI LGVSLACAKA
     GAEYSALPLY RYIGGTTAKT LPVPMMNVLN GGAHADNTVD FQEFMIMPIG FERYSDALRC
     GAEVFHSLKS LLHDRGLSTA VGDEGGFAPN VESNEQAIEL VIEAIGMAGY KAGAPTDRGG
     LGDGHVMIAL DPASSEFYDA EKKKYVFKKS SGRELSSEEM ASYWADWASR YPIISIEDGM
     AEDDWEGWKM LTDKIGGRVQ LVGDDLFVTN SKRLAEGIEK GVGNSILIKV NQIGTLTETL
     QAIELAKRNG YTSVISHRSG ETEDTTIAQI AVATNAGQIK TGSMSRSDRM AKYNELLRIE
     EELGSTALYP GIGAFRV
//