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ENO_METS5
ID   ENO_METS5               Reviewed;         416 AA.
AC   A4YHC1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318};
DE            EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318};
DE   AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318};
GN   Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=Msed_1668;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate
CC       into phosphoenolpyruvate. It is essential for the degradation of
CC       carbohydrates via glycolysis. {ECO:0000255|HAMAP-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:0000255|HAMAP-
CC         Rule:MF_00318};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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 the
CC       export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}.
CC       Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface
CC       {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are
CC       present in both the cytoplasm and on the cell surface. The export of
CC       enolase possibly depends on the covalent binding to the substrate; once
CC       secreted, it remains attached to the cell surface. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
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DR   EMBL; CP000682; ABP95823.1; -; Genomic_DNA.
DR   RefSeq; WP_012021610.1; NC_009440.1.
DR   AlphaFoldDB; A4YHC1; -.
DR   SMR; A4YHC1; -.
DR   STRING; 399549.Msed_1668; -.
DR   PRIDE; A4YHC1; -.
DR   EnsemblBacteria; ABP95823; ABP95823; Msed_1668.
DR   GeneID; 5105314; -.
DR   GeneID; 59457214; -.
DR   KEGG; mse:Msed_1668; -.
DR   eggNOG; arCOG01169; Archaea.
DR   HOGENOM; CLU_031223_2_1_2; -.
DR   OMA; EFMIIPV; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000000242; 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; SFLDF00002; enolase; 1.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Reference proteome;
KW   Secreted.
FT   CHAIN           1..416
FT                   /note="Enolase"
FT                   /id="PRO_1000072009"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         360..363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00318"
SQ   SEQUENCE   416 AA;  45751 MW;  D8C0586EBEAF601F CRC64;
     MMNGFSIANV QGYEIIDSRG NLTVRARVTL ESGIRATGDA PSGASKGTRE AVELRDKDGS
     VKGAVDSINY YISPALMGLD VREQGKIDRI MIELDGTENK SRLGANATIA TSIAVAKTAS
     ISMGLEPFMY IGGARTHTLP VPLLNILNGG LHAGNMLKIQ EFMVIPVKFD TLKEALIAST
     KIYKTLKSLV TERYGKIYTA LGDEGGISPP LSVTEDALKL VHEAIKRSGM EGRVFMGMDA
     AASDFYNPEK GVYEIDNTSK SPDEMIEFYV DIASRYPLLY LEDPFEENDF SRYSELQSRI
     KNVIVTGDDL FTTNVRYLRK GIEMKSARGV IVKANQIGTL TETIQFFDLA KDNSIKTVVS
     HRSGETEDSF IADLAVGLNS DFIKTGAPSR GERTSKYNRL LEIENEFGLE YLGRRL
 
 
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