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Database: UniProt/TrEMBL
Entry: B7MMZ6_ECO45
LinkDB: B7MMZ6_ECO45
Original site: B7MMZ6_ECO45 
ID   B7MMZ6_ECO45            Unreviewed;       489 AA.
AC   B7MMZ6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:CAR02924.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:CAR02924.1};
GN   OrderedLocusNames=ECS88_1609 {ECO:0000313|EMBL:CAR02924.1};
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR02924.1, ECO:0000313|Proteomes:UP000000747};
RN   [1] {ECO:0000313|Proteomes:UP000000747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CU928161; CAR02924.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7MMZ6; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; ecz:ECS88_1609; -.
DR   HOGENOM; CLU_001859_0_2_6; -.
DR   OMA; DPSWPIC; -.
DR   Proteomes; UP000000747; 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|RuleBase:RU004468, ECO:0000313|EMBL:CAR02924.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAR02924.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   489 AA;  56387 MW;  D6B855C83DFE9B82 CRC64;
     MVIYLVKELC MSGFKEDFLW GGAVAAHQLE GGWNEGGKGI SIADVMTAGA HGVPREVTEG
     VIDGLNYPNH EAIDFYHRYK TDIQLFAGMG FKCFRTSIAW TRIFPQGDEQ EPNEEGLQFY
     DDLFDECLKQ GMEPVVTLSH FEMPYHLVTK YGGWRNRKLI DFFIHFASTV FTRYKAKVKY
     WMTFNEINNQ VNFSESLCPF TNSGILYSPE EDLNEREQIM YQAVHYELVA SALAVQTGKL
     INPEFNIGCM IAMCPIYPLT CAPNDMMMAT KAMHRRYWFT DVHARGYYPQ HMLNYFARKG
     FNLDITPDDN AILARGCVDF IGFSYYMSFT TQFSPDNPQL DYVEPRDLVS NPYIDTSEWG
     WQIDPAGLRY SLNWFWDHFQ LPLFIVENGF GAVDQRQADG TVNDHYRIDY FSSHIREMKK
     AVVEDGVDLI GYTPWGCIDL VSAGTGEMKK RYGMIYVDKD NEGKGTLERI RKASFYWYRD
     LIANNGENI
//
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