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-MAY-2013, entry version 76.
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.
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DR EMBL; AE000512; AAD36356.1; -; Genomic_DNA.
DR PIR; E72273; E72273.
DR RefSeq; NP_229086.1; NC_000853.1.
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 PATRIC; 23937500; VBITheMar51294_1296.
DR eggNOG; COG1486; -.
DR KO; K01222; -.
DR OMA; PSGHITE; -.
DR ProtClustDB; CLSK875676; -.
DR SABIO-RK; Q9X108; -.
DR EvolutionaryTrace; Q9X108; -.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; Lactate_DH/Glyco_hydro_4_C; 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 (By
FT similarity).
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
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