ID   B2VKZ2_ERWT9            Unreviewed;       478 AA.
AC   B2VKZ2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=BglA protein, 6-phospho-beta-glucosidase (Involved in beta-glucoside utilization) {ECO:0000313|EMBL:CAO95525.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:CAO95525.1};
GN   Name=bglA {ECO:0000313|EMBL:CAO95525.1};
GN   OrderedLocusNames=ETA_04790 {ECO:0000313|EMBL:CAO95525.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO95525.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO95525.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CU468135; CAO95525.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2VKZ2; -.
DR   STRING; 465817.ETA_04790; -.
DR   KEGG; eta:ETA_04790; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_6; -.
DR   Proteomes; UP000001726; 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:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 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, ECO:0000313|EMBL:CAO95525.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAO95525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001726}.
FT   ACT_SITE        376
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   478 AA;  55280 MW;  77B28863470C1676 CRC64;
     MMSLPNDFLW GGAVAAHQVE GGWNQGGKGP SIVDVLSGGS HGVNRVITDG IDAQHQYPNH
     LAVDFYHRYK EDIALFAEMG FKCFRTSIAW TRIFPQGDEL EPNEAGLQFY DDLFDELLKY
     NIEPVITLSH FEMPLHLVKE YGGWLNRKVV DFFVRYSEAV LKRYQHKVKY WMTFNEINNQ
     RNWRYPLFGY CNSGVIFTDH EKPEQAMYQV LHHQFVASAQ VVKLGHQINP NMKIGCMLAI
     VPLYPWSCHP DDVMFAQEAM RERHLFGDVH LRGYYPSYIV KEWQRKGYQI EMQPGDEQTL
     REGCADYLGF SYYMSNAVQY SEKDNSDGRH IEGFPGSRPN PHVKASDWGW QIDPVGLRYT
     LNAFWERYQK PMFIVENGFG AYDKVEADGQ INDDYRIAYL QAHIEQMKIA VLEDGVDLMG
     YTPWGCIDCV SFTTGQYDKR YGFIHVNKND DGNGDLARSK KKSFNWYKQV IASNGEDV
//