(data stored in SCRATCH zone)

SWISSPROT: C7QJ14_CATAD

ID   C7QJ14_CATAD            Unreviewed;       428 AA.
AC   C7QJ14;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=Caci_0201 {ECO:0000313|EMBL:ACU69156.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69156.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69156.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00318};
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. {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; CP001700; ACU69156.1; -; Genomic_DNA.
DR   RefSeq; WP_012784451.1; NC_013131.1.
DR   ProteinModelPortal; C7QJ14; -.
DR   STRING; 479433.Caci_0201; -.
DR   PRIDE; C7QJ14; -.
DR   EnsemblBacteria; ACU69156; ACU69156; Caci_0201.
DR   KEGG; cai:Caci_0201; -.
DR   eggNOG; ENOG4105C70; Bacteria.
DR   eggNOG; COG0148; LUCA.
DR   HOGENOM; HOG000072174; -.
DR   KO; K01689; -.
DR   OMA; EFMIIPV; -.
DR   OrthoDB; POG091H02DK; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000000851; 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-HAMAP.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
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; IPR034390; Enolase-like_superfamily.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   InterPro; IPR029017; Enolase_N-like.
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   SFLD; SFLDS00001; 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;
DR   PRODOM; C7QJ14.
DR   SWISS-2DPAGE; C7QJ14.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
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:ACU69156.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Secreted {ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN        4    134       Enolase_N. {ECO:0000259|SMART:SM01193}.
FT   DOMAIN      139    423       Enolase_C. {ECO:0000259|SMART:SM01192}.
FT   REGION      362    365       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    335    335       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       283    283       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318}.
FT   METAL       310    310       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     283    283       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     310    310       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
FT   BINDING     335    335       Substrate (covalent); in inhibited form.
FT                                {ECO:0000256|HAMAP-Rule:MF_00318}.
FT   BINDING     386    386       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00318, ECO:0000256|PIRSR:PIRSR001400-
FT                                2}.
SQ   SEQUENCE   428 AA;  45818 MW;  87B51871B42F1F55 CRC64;
     MASIEAINAR EILDSRGNPT VEVEVLLEDG SFARAAVPSG ASTGAFEAVE LRDGDAARYG
     GKGVERAVQG VLDEIYPAVV GEDASDQRLI DQAMIDLDAT PNKARLGANA LLGVSLAVAK
     AAAESAELPL FRYLGGPNAH TLPVPMMNIL NGGAHADSNV DIQEFMIAPI GAGSFREALR
     WGAEVYHALK SVLKERGLNT GLGDEGGFAP SLPSNRDALD LILVAIEKAG YTPGRDIALA
     LDVAASEFYK DGAYQFEGKS RTASEMTDYY AELVDAYPLV SIEDPLFEDD WDGWKILTDR
     LGTQVQIVGD DLFVTNPERL ARGIAGGQAN ALLVKVNQIG TLTETFDAVQ LAHRNGYRCM
     MSHRSGETED TTIADLAVAV DCGQIKTGAP ARSDRVAKYN QLLRIEEELD DAARYAGRSA
     FPRFTHEG
//

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