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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   26-NOV-2014, entry version 88.
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:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC       Note=Binds 1 NAD(+) per subunit.;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) 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}.
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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; 18093432; -.
DR   GeneID; 898202; -.
DR   KEGG; tma:TM1281; -.
DR   PATRIC; 23937500; VBITheMar51294_1296.
DR   eggNOG; COG1486; -.
DR   InParanoid; Q9X108; -.
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       {ECO:0000244|PDB:1UP7}.
FT   HELIX        13     23       {ECO:0000244|PDB:1UP7}.
FT   TURN         24     26       {ECO:0000244|PDB:1UP7}.
FT   STRAND       31     35       {ECO:0000244|PDB:1UP7}.
FT   HELIX        39     53       {ECO:0000244|PDB:1UP7}.
FT   STRAND       56     61       {ECO:0000244|PDB:1UP7}.
FT   HELIX        65     69       {ECO:0000244|PDB:1UP7}.
FT   STRAND       73     77       {ECO:0000244|PDB:1UP7}.
FT   HELIX        83     92       {ECO:0000244|PDB:1UP7}.
FT   HELIX        93     97       {ECO:0000244|PDB:1UP7}.
FT   STRAND      103    105       {ECO:0000244|PDB:1UP7}.
FT   HELIX       107    129       {ECO:0000244|PDB:1UP7}.
FT   STRAND      134    137       {ECO:0000244|PDB:1UP7}.
FT   STRAND      139    141       {ECO:0000244|PDB:1UP7}.
FT   HELIX       142    151       {ECO:0000244|PDB:1UP7}.
FT   STRAND      156    160       {ECO:0000244|PDB:1UP7}.
FT   HELIX       164    175       {ECO:0000244|PDB:1UP7}.
FT   HELIX       180    182       {ECO:0000244|PDB:1UP7}.
FT   STRAND      183    190       {ECO:0000244|PDB:1UP7}.
FT   STRAND      193    201       {ECO:0000244|PDB:1UP7}.
FT   HELIX       207    214       {ECO:0000244|PDB:1UP7}.
FT   HELIX       228    234       {ECO:0000244|PDB:1UP7}.
FT   STRAND      236    238       {ECO:0000244|PDB:1UP7}.
FT   HELIX       240    242       {ECO:0000244|PDB:1UP7}.
FT   HELIX       243    246       {ECO:0000244|PDB:1UP7}.
FT   HELIX       248    256       {ECO:0000244|PDB:1UP7}.
FT   HELIX       261    276       {ECO:0000244|PDB:1UP7}.
FT   HELIX       284    288       {ECO:0000244|PDB:1UP7}.
FT   TURN        290    293       {ECO:0000244|PDB:1UP7}.
FT   HELIX       294    306       {ECO:0000244|PDB:1UP7}.
FT   STRAND      307    309       {ECO:0000244|PDB:1UP7}.
FT   STRAND      311    318       {ECO:0000244|PDB:1UP7}.
FT   STRAND      331    339       {ECO:0000244|PDB:1UP7}.
FT   STRAND      342    346       {ECO:0000244|PDB:1UP7}.
FT   HELIX       353    374       {ECO:0000244|PDB:1UP7}.
FT   HELIX       378    387       {ECO:0000244|PDB:1UP7}.
FT   HELIX       394    407       {ECO:0000244|PDB:1UP7}.
FT   TURN        408    411       {ECO:0000244|PDB:1UP7}.
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
//
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