ID   Q0GC07_THENN            Unreviewed;       721 AA.
AC   Q0GC07;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:ABI29899.1};
DE            EC=3.2.1.21 {ECO:0000313|EMBL:ABI29899.1};
GN   Name=bgl3B {ECO:0000313|EMBL:ABI29899.1};
OS   Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=309803 {ECO:0000313|EMBL:ABI29899.1};
RN   [1] {ECO:0000313|EMBL:ABI29899.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 4359 {ECO:0000313|EMBL:ABI29899.1};
RX   PubMed=17448557; DOI=10.1016/j.jbiotec.2007.02.016;
RA   Turner P., Svensson D., Adlercreutz P., Nordberg Karlsson E.;
RT   "A novel variant of Thermotoga neapolitana beta-glucosidase B is an
RT   efficient catalyst for the synthesis of alkyl glucosides by
RT   transglycosylation.";
RL   J. Biotechnol. 130:67-74(2007).
RN   [2] {ECO:0007829|PDB:2X40, ECO:0007829|PDB:2X41}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GLUCOSE.
RX   PubMed=20138890; DOI=10.1016/j.jmb.2010.01.072;
RA   Pozzo T., Pasten J.L., Karlsson E.N., Logan D.T.;
RT   "Structural and functional analyses of beta-glucosidase 3B from Thermotoga
RT   neapolitana: a thermostable three-domain representative of glycoside
RT   hydrolase 3.";
RL   J. Mol. Biol. 397:724-739(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; DQ873691; ABI29899.1; -; Genomic_DNA.
DR   RefSeq; WP_038066943.1; NC_011978.1.
DR   PDB; 2X40; X-ray; 2.31 A; A=1-721.
DR   PDB; 2X41; X-ray; 2.05 A; A=1-721.
DR   PDB; 2X42; X-ray; 2.10 A; A=1-721.
DR   PDBsum; 2X40; -.
DR   PDBsum; 2X41; -.
DR   PDBsum; 2X42; -.
DR   AlphaFoldDB; Q0GC07; -.
DR   SMR; Q0GC07; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   BRENDA; 3.2.1.21; 6332.
DR   EvolutionaryTrace; Q0GC07; -.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2X40, ECO:0007829|PDB:2X41};
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:ABI29899.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT   DOMAIN          633..702
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
FT   CARBOHYD        58
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:2X42"
FT   CARBOHYD        130
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:2X42"
FT   CARBOHYD        163
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:2X42"
FT   CARBOHYD        243
FT                   /note="Glucose"
FT                   /evidence="ECO:0007829|PDB:2X42"
SQ   SEQUENCE   721 AA;  81160 MW;  78D048F6F9F3AFEA CRC64;
     MEKVNEILSQ LTLEEKVKLV VGVGLPGLFG NPHSRVAGAA GETHPVPRVG LPAFVLADGP
     AGLRINPTRE NDENTYYTTA FPVEIMLAST WNRELLEEVG KAMGEEVREY GVDVLLAPAM
     NIHRNPLCGR NFEYYSEDPV LSGEMASSFV KGVQSQGVGA CIKHFVANNQ ETNRMVVDTI
     VSERALREIY LRGFEIAVKK SKPWSVMSAY NKLNGKYCSQ NEWLLKKVLR EEWGFEGFVM
     SDWYAGDNPV EQLKAGNDLI MPGKAYQVNT ERRDEIEEIM EALKEGKLSE EVLDECVRNI
     LKVLVNAPSF KNYRYSNKPD LEKHAKVAYE AGAEGVVLLR NEEALPLSEN SKIALFGTGQ
     IETIKGGTGS GDTHPRYAIS ILEGIKERGL NFDEELAKTY EDYIKKMRET EEYKPRRDSW
     GTIIKPKLPE NFLSEKEIHK LAKKNDVAVI VISRISGEGY DRKPVKGDFY LSDDETDLIK
     TVSREFHEQG KKVIVLLNIG SPVEVVSWRD LVDGILLVWQ AGQETGRIVA DVLTGRINPS
     GKLPTTFPRD YSDVPSWTFP GEPKDNPQKV VYEEDIYVGY RYYDTFGVEP AYEFGYGLSY
     TTFEYSDLNV SFDGETLRVQ YRIENTGGRA GKEVSQVYIK APKGKIDKPF QELKAFHKTR
     LLNPGESEEV VLEIPVRDLA SFNGEEWVVE AGEYEVRVGA SSRNIKLKGT FSVGEERRFK
     P
//