(data stored in ACNUC10043 zone)

HOGENOM: IGNH4_1_PE1002

ID   IGNH4_1_PE1002                       STANDARD;      PRT;   414 AA.
AC   IGNH4_1_PE1002; A8AB84;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Enolase; EC=4.2.1 11;AltName: Full=2-phospho-D-glycerate
DE   hydro-lyase;AltName: Full=2-phosphoglycerate dehydratase;
DE   (IGNH4_1.PE1002).
GN   Name=eno; OrderedLocusNames=Igni_1007;
OS   IGNICOCCUS HOSPITALIS KIN4/I.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS IGNH4_1.PE1002.
CC       Ignicoccus hospitalis KIN4/I chromosome, complete genome.
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:A8AB84_IGNH4
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 cell surface (By similarity).
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -!- GENE_FAMILY: HOG000072173 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8AB84; -.
DR   EMBL; CP000816; ABU82186.1; -; Genomic_DNA.
DR   RefSeq; YP_001435593.1; NC_009776.1.
DR   ProteinModelPortal; A8AB84; -.
DR   SMR; A8AB84; 2-410.
DR   STRING; A8AB84; -.
DR   GeneID; 5563023; -.
DR   GenomeReviews; CP000816_GR; Igni_1007.
DR   KEGG; iho:Igni_1007; -.
DR   eggNOG; arNOG04113; -.
DR   OMA; GELYKNF; -.
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; Enolase; 1; -.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   TIGRFAMs; TIGR01060; Eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
DR   HOGENOMDNA; IGNH4_1.PE1002; -.
KW   enolase;
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Phosphoprotein; Secreted.
SQ   SEQUENCE   414 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRGRWILDSR GNPTVEVDVY TEGGFGRAAA PAGASKGSKE ALELRDGGNA FMGKGVLKAV
     RNVNEVIGPS LVGMDSLDQK EIDMKMIELD GTENKSKLGA NAIVATSMAV AKAAADSLSV
     PLYYHLGGAL AQTLPTPLLN VINGGAHAGN ELAIQEFMIV PWDFSSFSEA LQAASEIYHY
     LKSYLKEKYG KSAINVGDEG GFAPPMRQTR EALDALVNAI KKAGYEGRVA LALDAAATHF
     YDQEKGVYRI DGKELDREGL LELYEELIRD YPIVSIEDPL HEEDWEGFKE AVKRLKIRVV
     GDDLLVTNPK LVKKAIEEGV ANAVLVKVNQ VGTVTEAYEV VDMAKRASWA AIVSHRSGET
     EDTFISHFAV GSGAPAIKAG APARGERTAK YNELLRIEEE LGRPKFARDA YFRT
//

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