BGLT_THEMA
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 03-AUG-2022, entry version 123.
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 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA 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 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
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 WITH
RP 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-phosphate
CC (Glc6P) and glucose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
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 homodimer/homotetramer
CC equilibrium state in solution.
CC -!- MISCELLANEOUS: Is a retaining glucosidase as it hydrolyzes glycosidic
CC bond with retention of anomeric configuration. Reaction mechanism
CC includes redox steps involving NAD and stabilization of intermediates
CC by Mn(2+).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {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; NZ_CP011107.1.
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 AlphaFoldDB; Q9X108; -.
DR SMR; Q9X108; -.
DR STRING; 243274.THEMA_07930; -.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; AAD36356; AAD36356; TM_1281.
DR KEGG; tma:TM1281; -.
DR eggNOG; COG1486; Bacteria.
DR InParanoid; Q9X108; -.
DR OMA; NEHASHI; -.
DR OrthoDB; 277080at2; -.
DR BRENDA; 3.2.1.86; 6331.
DR SABIO-RK; Q9X108; -.
DR EvolutionaryTrace; Q9X108; -.
DR Proteomes; UP000008183; Chromosome.
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:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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; 3.90.110.10; -; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese;
KW Metal-binding; NAD; Reference proteome.
FT CHAIN 1..415
FT /note="6-phospho-beta-glucosidase BglT"
FT /id="PRO_0000169857"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT BINDING 1..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 87
FT /ligand="substrate"
FT BINDING 140
FT /ligand="substrate"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 163
FT /ligand="substrate"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 261
FT /ligand="substrate"
FT SITE 103
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1UP7"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 107..129
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:1UP7"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 331..339
FT /evidence="ECO:0007829|PDB:1UP7"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 353..374
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:1UP7"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:1UP7"
FT TURN 408..411
FT /evidence="ECO:0007829|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
