GenomeNet

Database: UniProt
Entry: Q9X108
LinkDB: Q9X108
Original site: Q9X108 
ID   BGLT_THEMA              Reviewed;         415 AA.
AC   Q9X108;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   01-OCT-2014, entry version 86.
DE   RecName: Full=6-phospho-beta-glucosidase BglT;
DE            EC=3.2.1.86;
GN   Name=bglT; OrderedLocusNames=TM_1281;
OS   Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA   Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA   McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA   Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA   Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA   Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   CHARACTERIZATION, AND REACTION MECHANISM.
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX   PubMed=15237973; DOI=10.1021/ja047632w;
RA   Yip V.L.Y., Varrot A., Davies G.J., Rajan S.S., Yang X., Thompson J.,
RA   Anderson W.F., Withers S.G.;
RT   "An unusual mechanism of glycoside hydrolysis involving redox and
RT   elimination steps by a family 4 beta-glycosidase from Thermotoga
RT   maritima.";
RL   J. Am. Chem. Soc. 126:8354-8355(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX
RP   WITH NAD(+) AND GLUCOSE-6-PHOSPHATE.
RX   PubMed=15670594; DOI=10.1016/j.jmb.2004.11.058;
RA   Varrot A., Yip V.L.Y., Li Y., Rajan S.S., Yang X., Anderson W.F.,
RA   Thompson J., Withers S.G., Davies G.J.;
RT   "NAD(+) and metal-ion dependent hydrolysis by family 4 glycosidases:
RT   structural insight into specificity for phospho-beta-D-glucosides.";
RL   J. Mol. Biol. 346:423-435(2005).
CC   -!- FUNCTION: Hydrolyzes cellobiose 6'-phosphate into glucose 6-
CC       phosphate (Glc6P) and glucose.
CC   -!- CATALYTIC ACTIVITY: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose +
CC       H(2)O = D-glucose + D-glucose 6-phosphate.
CC   -!- COFACTOR: Binds 1 NAD per subunit.
CC   -!- COFACTOR: Binds 1 manganese ion per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=41 uM for p-nitrophenyl-beta-D-glucopyranoside 6-phosphate;
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 6.5 to 10.;
CC   -!- SUBUNIT: Homodimer or homotetramer. Exists in a
CC       homodimer/homotetramer equilibrium state in solution.
CC   -!- MISCELLANEOUS: Is a retaining glucosidase as it hydrolyzes
CC       glycosidic bond with retention of anomeric configuration. Reaction
CC       mechanism includes redox steps involving NAD and stabilization of
CC       intermediates by Mn(2+).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC       {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE000512; AAD36356.1; -; Genomic_DNA.
DR   PIR; E72273; E72273.
DR   RefSeq; NP_229086.1; NC_000853.1.
DR   RefSeq; WP_004079953.1; NC_023151.1.
DR   RefSeq; YP_007977635.1; NC_021214.1.
DR   RefSeq; YP_008991622.1; NC_023151.1.
DR   PDB; 1UP4; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-415.
DR   PDB; 1UP6; X-ray; 2.55 A; A/B/C/D/E/F/G/H=1-415.
DR   PDB; 1UP7; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-415.
DR   PDBsum; 1UP4; -.
DR   PDBsum; 1UP6; -.
DR   PDBsum; 1UP7; -.
DR   ProteinModelPortal; Q9X108; -.
DR   SMR; Q9X108; 1-415.
DR   STRING; 243274.TM1281; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   EnsemblBacteria; AAD36356; AAD36356; TM_1281.
DR   GeneID; 898202; -.
DR   KEGG; tma:TM1281; -.
DR   KEGG; tmi:THEMA_07930; -.
DR   KEGG; tmm:Tmari_1286; -.
DR   PATRIC; 23937500; VBITheMar51294_1296.
DR   eggNOG; COG1486; -.
DR   KO; K01222; -.
DR   OMA; PSGHITE; -.
DR   OrthoDB; EOG6CP3SG; -.
DR   SABIO-RK; Q9X108; -.
DR   EvolutionaryTrace; Q9X108; -.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR019802; GlycHydrolase_4_CS.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Complete proteome; Glycosidase;
KW   Hydrolase; Manganese; Metal-binding; NAD; Reference proteome.
FT   CHAIN         1    415       6-phospho-beta-glucosidase BglT.
FT                                /FTId=PRO_0000169857.
FT   NP_BIND       1     64       NAD.
FT   ACT_SITE    241    241       Proton acceptor.
FT   METAL       162    162       Manganese.
FT   METAL       192    192       Manganese.
FT   BINDING      87     87       Substrate.
FT   BINDING     140    140       Substrate.
FT   BINDING     163    163       Substrate.
FT   BINDING     261    261       Substrate.
FT   SITE        103    103       Increases basicity of active site Tyr.
FT                                {ECO:0000250}.
FT   STRAND        2      7
FT   HELIX        13     23
FT   TURN         24     26
FT   STRAND       31     35
FT   HELIX        39     53
FT   STRAND       56     61
FT   HELIX        65     69
FT   STRAND       73     77
FT   HELIX        83     92
FT   HELIX        93     97
FT   STRAND      103    105
FT   HELIX       107    129
FT   STRAND      134    137
FT   STRAND      139    141
FT   HELIX       142    151
FT   STRAND      156    160
FT   HELIX       164    175
FT   HELIX       180    182
FT   STRAND      183    190
FT   STRAND      193    201
FT   HELIX       207    214
FT   HELIX       228    234
FT   STRAND      236    238
FT   HELIX       240    242
FT   HELIX       243    246
FT   HELIX       248    256
FT   HELIX       261    276
FT   HELIX       284    288
FT   TURN        290    293
FT   HELIX       294    306
FT   STRAND      307    309
FT   STRAND      311    318
FT   STRAND      331    339
FT   STRAND      342    346
FT   HELIX       353    374
FT   HELIX       378    387
FT   HELIX       394    407
FT   TURN        408    411
SQ   SEQUENCE   415 AA;  47627 MW;  FB4E3B358245BFEE CRC64;
     MRIAVIGGGS SYTPELVKGL LDISEDVRID EVIFYDIDEE KQKIVVDFVK RLVKDRFKVL
     ISDTFEGAVV DAKYVIFQFR PGGLKGREND EGIPLKYGLI GQETTGVGGF SAALRAFPIV
     EEYVDTVRKT SNATIVNFTN PSGHITEFVR NYLEYEKFIG LCNVPINFIR EIAEMFSARL
     EDVFLKYYGL NHLSFIEKVF VKGEDVTEKV FENLKLKLSN IPDEDFPTWF YDSVRLIVNP
     YLRYYLMEKK MFKKISTHEL RAREVMKIEK ELFEKYRTAV EIPEELTKRG GSMYSTAAAH
     LIRDLETDEG KIHIVNTRNN GSIENLPDDY VLEIPCYVRS GRVHTLSQGK GDHFALSFIH
     AVKMYERLTI EAYLKRSKKL ALKALLSHPL GPDVEDAKDL LEEILEANRE YVKLG
//
DBGET integrated database retrieval system