ID   A0A3N1MMU3_9MICO        Unreviewed;       489 AA.
AC   A0A3N1MMU3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ROQ04277.1};
GN   ORFNames=EDF54_2480 {ECO:0000313|EMBL:ROQ04277.1};
OS   Rathayibacter sp. PhB93.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=2485103 {ECO:0000313|EMBL:ROQ04277.1, ECO:0000313|Proteomes:UP000270764};
RN   [1] {ECO:0000313|EMBL:ROQ04277.1, ECO:0000313|Proteomes:UP000270764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PhB93 {ECO:0000313|EMBL:ROQ04277.1,
RC   ECO:0000313|Proteomes:UP000270764};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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:ROQ04277.1}.
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DR   EMBL; RJLA01000015; ROQ04277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1MMU3; -.
DR   Proteomes; UP000270764; Unassembled WGS sequence.
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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF122; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLH; 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|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468}.
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   489 AA;  55234 MW;  5254DB384623247C CRC64;
     MALPEGFRWG GALAANQVEG AWREGGRGPA VSDVASYKPK ADPKEYAIHH QNTVASITAA
     MADDDTEYYP KRRGIDFYHR YPGDLALFAE MGFTTLRVSI AWTRLYPTGE EAEPLEEGVA
     YYLALFTEMR RLGIEPLVTL SHYDPPLALA LKHNAWVERR TIELFERFAR TCFERFGHLV
     DMWLSFNEID GIIRHPFTSG GIIEETVEGS VEQACYTALH HQFVASASVT RILHELWPEA
     RMGCMLTMLT TYPNTCHPDD VAATQAKERM LYLCTDVQAG GAYPRLALRA LAARGVEIPF
     AEGDAELLRE HPVDFISFSY YMSMTESVRP DAERTPGNTV LGVKNPFLES SEWGWQIDPV
     GLRISLIDLY DRYGKPLFIV ENGLGMRDEL VASDNEGEDP RIHDPYRIDY FRAHFEQMIQ
     AVDEGVELLG YVSWAPIDLI SASSSQISKR YGFVYVDMDD LGHGSTNRYR KDSFFWYQRV
     IASNGADLG
//