ID A0A0F0LDI2_9MICO Unreviewed; 771 AA.
AC A0A0F0LDI2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thermostable beta-glucosidase B {ECO:0000313|EMBL:KJL29626.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KJL29626.1};
GN Name=bglB_3 {ECO:0000313|EMBL:KJL29626.1};
GN ORFNames=RS83_01647 {ECO:0000313|EMBL:KJL29626.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL29626.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL29626.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL29626.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL29626.1}.
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DR EMBL; JYIW01000023; KJL29626.1; -; Genomic_DNA.
DR RefSeq; WP_045279015.1; NZ_JYIW01000023.1.
DR AlphaFoldDB; A0A0F0LDI2; -.
DR PATRIC; fig|82380.11.peg.1683; -.
DR OrthoDB; 3187421at2; -.
DR Proteomes; UP000033640; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:KJL29626.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT DOMAIN 599..669
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 771 AA; 80788 MW; C89ACF55FF8BEC3E CRC64;
MTDISASDLT LEEKASLTSG ADFWTTKAIE RAGIPAVMMT DGPHGLRKQA GGTDHLGLAS
SVPATCFPPA VGIGSSWDPE IIERVGAAIG VEAAIEDVAV VLGPGINIKR SPLCGRNFEY
FSEDPIVSGI LGAASVRGVQ SQGVGTSLKH FAANNQEFDR MRASSDVDPR PLREIYLRGF
ERVVKDASPW TVMCSYNKLN GVWTSEDPWL LTSVLRDDWG FDGLVVSDWG AVNDRVAGVA
AGLDLEMPAS GGRTDAQLVA AVRAGELDES VLDTAASRAI DLVRKAGERP AVSGPLDVDA
HHALAREAAG RSIVLLKNEA LRGAQRPDAG REQRAVLPLT ADQKVAVIGA FATEPRFQGA
GSSLINPTRV DTALDELRAI GGDTVSYAPG FAVTGGVVAA SGRSADDLRA EAVEVAAAAD
VAVVLLGLPA AEESEGFDRD HIDLPADQLA LLDAVIDVNP NTVVVLSNGG VVALPFADRV
PAIVEGWLLG QAGGGAVADV LYGVVNPSGK LTETVPVRLE DNPSFGNFPG EFGHVRYGEG
LLVGYRWYDA KGLEVTYPFG HGLSYTTFEY GATTASVRAD GDIAVQVELT NTGDRDGREV
VQVYVAPEAS SVQRAPRELK AFSSVALAAG ESRTVELVVR REDLAYWDVR VDRWVVEGGD
YTIDVAASSR DIRSSVSVAV AGDDVQIALT MNSSVGDVLA HPVAGPIVMG ALGGFMEELS
GADSSAASMI PNDEAMQKMM ASFPIGRLVG FPGVDVTYDQ VEQLIAAANA G
//