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
//