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Database: UniProt/TrEMBL
Entry: G8MWU2_GEOTH
LinkDB: G8MWU2_GEOTH
Original site: G8MWU2_GEOTH 
ID   G8MWU2_GEOTH            Unreviewed;       470 AA.
AC   G8MWU2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=6-phospho-beta-glucosidase gmuD {ECO:0000313|EMBL:AEV19475.1};
GN   ORFNames=GTCCBUS3UF5_21670 {ECO:0000313|EMBL:AEV19475.1};
OS   Geobacillus thermoleovorans CCB_US3_UF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV19475.1, ECO:0000313|Proteomes:UP000005636};
RN   [1] {ECO:0000313|EMBL:AEV19475.1, ECO:0000313|Proteomes:UP000005636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV19475.1,
RC   ECO:0000313|Proteomes:UP000005636};
RA   Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT   CCB_US3_UF5.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP003125; AEV19475.1; -; Genomic_DNA.
DR   RefSeq; WP_014195961.1; NC_016593.1.
DR   AlphaFoldDB; G8MWU2; -.
DR   KEGG; gte:GTCCBUS3UF5_21670; -.
DR   PATRIC; fig|1111068.3.peg.2091; -.
DR   HOGENOM; CLU_001859_0_1_9; -.
DR   Proteomes; UP000005636; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF139; 6-PHOSPHO-BETA-GLUCOSIDASE GMUD; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295}.
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   470 AA;  54658 MW;  A4E644FD4AD7FAE1 CRC64;
     MEQRSKQPIT YRFPAGFWWG SATSATQIEG AANEGGKGKN IWDHWYEQEP HRFFQGVGPE
     VTSDFYHRYK EDIALMKEIG HNSFRFSISW SRLIPDGVGE VNSEAVRFYN AVIDELLANG
     IEPFVNLYHF DMPLVMQNIG GWENREVIDA YARYASLCFQ LFGDRVKTWF THNEPIVPVE
     GGYLYDFHYP NVVDFRRAVQ VAYHTMIAHA KAVAAFRRAA IQGGKIGIIL NLTPSYPRSQ
     HPADVKAAHI ADLLFNRSFL DPAVKGEYPQ DLIELLAEHR FLPVMEVGDR ELIKENTIDL
     LGINYYQPRR VKAKEHLPNP DAPFLPERFF DYYAMPGRKM NPYRGWEIYE KGIYDILINI
     KEKYGNIECF ISENGMGVEG EERFRDESGM IHDDYRIEFI QEHLKWVHRA IEEGTNVKGY
     HIWTFMDNWS WTNAYKNRYG LVAVDLENGL KRTIKKSGYW FKSLAENNGF
//
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