(data stored in ACNUC7421 zone)

SWISSPROT: ENO_THEFY

ID   ENO_THEFY               Reviewed;         427 AA.
AC   Q47SV1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 105.
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};
GN   OrderedLocusNames=Tfu_0428;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-
CC       phosphoglycerate into phosphoenolpyruvate. It is essential for the
CC       degradation of carbohydrates via glycolysis. {ECO:0000255|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: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
CC       the 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
CC       of enolase possibly depends on the covalent binding to the
CC       substrate; once secreted, it remains attached to the cell surface.
CC       {ECO:0000255|HAMAP-Rule:MF_00318}.
CC   -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00318}.
DR   EMBL; CP000088; AAZ54466.1; -; Genomic_DNA.
DR   RefSeq; WP_011290875.1; NC_007333.1.
DR   SMR; Q47SV1; -.
DR   STRING; 269800.Tfu_0428; -.
DR   PRIDE; Q47SV1; -.
DR   EnsemblBacteria; AAZ54466; AAZ54466; Tfu_0428.
DR   KEGG; tfu:Tfu_0428; -.
DR   eggNOG; ENOG4105C70; Bacteria.
DR   eggNOG; COG0148; LUCA.
DR   HOGENOM; HOG000072173; -.
DR   KO; K01689; -.
DR   OMA; EFMIIPV; -.
DR   OrthoDB; 533698at2; -.
DR   BioCyc; TFUS269800:G1G4Q-434-MONOMER; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000000434; 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; Q47SV1.
DR   SWISS-2DPAGE; Q47SV1.
KW   Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium;
KW   Metal-binding; Reference proteome; Secreted.
FT   CHAIN         1    427       Enolase.
FT                                /FTId=PRO_0000267129.
FT   REGION      361    364       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   ACT_SITE    204    204       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   ACT_SITE    334    334       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   METAL       241    241       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   METAL       282    282       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   METAL       309    309       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   BINDING     154    154       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   BINDING     163    163       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   BINDING     282    282       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   BINDING     309    309       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
FT   BINDING     334    334       Substrate (covalent); in inhibited form.
FT                                {ECO:0000255|HAMAP-Rule:MF_00318}.
FT   BINDING     385    385       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00318}.
SQ   SEQUENCE   427 AA;  45297 MW;  227AED4E04A413AA CRC64;
     MASIEAVHAR EILDSRGNPT VEVEVALDDG TIARAAVPSG ASTGQFEAVE LRDGGDRYGG
     KGVEKAVAAV NEEISEQIVG YEAEEQRLVD SALITLDGTP DKSRLGANAI LGVSLAVAKA
     AAESADLPLF RYLGGPNAHV LPVPMMNILN GGAHADTNVD IQEFMIAPIG AESFREALRW
     GAEVYHSLKA VLKAHGLATG VGDEGGFAPN LDSNRAALDL ISEAITKAGF TLGQDIALAL
     DVAATEFYAD GAYQFEGSSR SAEEMAAYYT ELVESYPLVS IEDPLSEEDW AGWKALTESL
     GDRLQLVGDD LFVTNPERLQ RGIDEGAANS LLVKVNQIGT LSETLDAVSL AQRNRYTAMI
     SHRSGETEDT TIADIAVATN SGQIKTGAPA RSERVAKYNQ LLRIEEELDD AAVYAGANAF
     PRFARQG
//

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