(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIK8_GEOS0

ID   A0A0F6BIK8_GEOS0        Unreviewed;       430 AA.
AC   A0A0F6BIK8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318};
DE            EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318};
GN   Name=eno {ECO:0000256|HAMAP-Rule:MF_00318};
GN   OrderedLocusNames=GY4MC1_0418 {ECO:0000313|EMBL:ADP73259.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73259.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73259.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73259.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-
CC       phosphoglycerate into phosphoenolpyruvate. It is essential for the
CC       degradation of carbohydrates via glycolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_00318}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC         ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00318};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00318};
CC   -!- ACTIVITY 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. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}.
CC       Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface
CC       {ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC       present in both the cytoplasm and on the cell surface. The export
CC       of enolase possibly depends on the covalent binding to the
CC       substrate; once secreted, it remains attached to the cell surface.
CC       {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00318}.
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DR   EMBL; CP002293; ADP73259.1; -; Genomic_DNA.
DR   RefSeq; WP_013400009.1; NC_014650.1.
DR   EnsemblBacteria; ADP73259; ADP73259; GY4MC1_0418.
DR   KEGG; gmc:GY4MC1_0418; -.
DR   KO; K01689; -.
DR   OMA; EFMIIPV; -.
DR   OrthoDB; 533698at2; -.
DR   BioCyc; GSP581103:G1GOQ-465-MONOMER; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000002034; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   HAMAP; MF_00318; Enolase; 1.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   PANTHER; PTHR11902; PTHR11902; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   SFLD; SFLDG00178; enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIK8.
DR   SWISS-2DPAGE; A0A0F6BIK8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000313|EMBL:ADP73259.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN        4    134       Enolase_N. {ECO:0000259|SMART:SM01193}.
FT   DOMAIN      139    427       Enolase_C. {ECO:0000259|SMART:SM01192}.
FT   REGION      366    369       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00318, ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                1}.
FT   ACT_SITE    339    339       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                1}.
FT   METAL       242    242       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318}.
FT   METAL       287    287       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318}.
FT   METAL       314    314       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318}.
FT   BINDING     155    155       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     287    287       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     314    314       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     339    339       Substrate (covalent); in inhibited form.
FT                                {ECO:0000256|HAMAP-Rule:MF_00318}.
FT   BINDING     390    390       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
SQ   SEQUENCE   430 AA;  46461 MW;  9258AE220A6916CF CRC64;
     MSAILDVYAR EVLDSRGNPT VEVEIYTEDG GFGRALVPSG ASTGEYEAVE LRDGDKSRYL
     GKGVLKAVEN VNEVIAPAII GLEVTDQVGI DKTLIELDGT ENKSKLGANA ILGVSLAVAR
     AAADELGMPL YQYLGGFNAK TLPVPMMNIL NGGAHADNNV DIQEFMIMPV GAKSFREALR
     MGAEIFHSLK AVLKAKGYNT AVGDEGGFAP NLKSNEEALQ TIIEAIEKAG YKPGEEVMLA
     MDVASSELYN KEDGKYHLEG EGVVRTSEEM VAWYEELVSK YPIISIEDGL DENDWEGHKL
     LTERLGKKVQ LVGDDLFVTN TKKLAEGIEK GVGNSILIKV NQIGTLTETF DAIEMAKRAG
     YTAVVSHRSG ETEDSTIADI AVATNAGQIK TGAPSRTDRV AKYNQLLRIE DQLGDTAIYN
     GIKSFYNLKK
//

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