ID   G4NZ12_BACS4            Unreviewed;       479 AA.
AC   G4NZ12;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:AEP88975.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:AEP88975.1};
GN   OrderedLocusNames=GYO_4418 {ECO:0000313|EMBL:AEP88975.1};
OS   Bacillus spizizenii (strain DSM 15029 / JCM 12233 / NBRC 101239 / NRRL
OS   B-23049 / TU-B-10) (Bacillus subtilis subsp. spizizenii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1052585 {ECO:0000313|EMBL:AEP88975.1, ECO:0000313|Proteomes:UP000002651};
RN   [1] {ECO:0000313|EMBL:AEP88975.1, ECO:0000313|Proteomes:UP000002651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15029 / JCM 12233 / NBRC 101239 / NRRL B-23049 / TU-B-10
RC   {ECO:0000313|Proteomes:UP000002651};
RX   PubMed=22493193; DOI=10.1128/JB.05675-11;
RA   Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A.,
RA   Daugherty S., Losick R., Kolter R., Ravel J.;
RT   "Whole-genome sequences of Bacillus subtilis and close relatives.";
RL   J. Bacteriol. 194:2378-2379(2012).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP002905; AEP88975.1; -; Genomic_DNA.
DR   RefSeq; WP_014115811.1; NC_016047.1.
DR   AlphaFoldDB; G4NZ12; -.
DR   STRING; 1052585.GYO_4418; -.
DR   KEGG; bst:GYO_4418; -.
DR   HOGENOM; CLU_001859_1_3_9; -.
DR   Proteomes; UP000002651; Chromosome.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF85; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLA; 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.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:AEP88975.1}.
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   479 AA;  54899 MW;  AEA2EB69DDEE8B6C CRC64;
     MGNMTKDFLW GGALAAHQFE GGWNQGGKGP SVVDVMTAGA HGVPRKITDT IEENEFYPNH
     EAIDFYHRYK EDIALFAEMG LKCLRTSIGW SRIFPKGDEA EPNEAGLQFY DDVFDELLKH
     GIEPVITLSH FEMPLHLARE YGGFRNRKVV DFFVNFAEAC FNRYKDKVKY WMTFNEINNQ
     MDVNNPLFLW TNSGVVVGEN ENAKEVMYQT AHHELVASAL AVAKGKDINP DFQIGAMVSH
     VPIYPFSSNP EDVMLAEEEM RQRYFFPDVQ VRGYYPSYAL KEFEREGYHI TFEDGDDEIL
     RNGTVDYLGF SYYMSTTVKS DVENDNTGDI VNGGLPNGVE NPYITSSDWG WAIDPTGLRY
     TLNRFYDRYQ IPLFIVENGF GAVDTLEEDG KIHDLERIQY LKSHIEALEK AVTYDGVDLI
     GYTPWGIIDI VSFTTGEMKK RYGMIYVDRD NEGNGSMKRY KKDSFEWYKN VIQTNGEEL
//