ID A0A0H3MNI7_ECO7I Unreviewed; 474 AA.
AC A0A0H3MNI7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cryptic 6-phospho-beta-glucosidase {ECO:0000313|EMBL:CAR19023.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CAR19023.1};
GN Name=ascB {ECO:0000313|EMBL:CAR19023.1};
GN OrderedLocusNames=ECIAI39_2902 {ECO:0000313|EMBL:CAR19023.1};
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057 {ECO:0000313|EMBL:CAR19023.1, ECO:0000313|Proteomes:UP000000749};
RN [1] {ECO:0000313|Proteomes:UP000000749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC {ECO:0000313|Proteomes:UP000000749};
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; CU928164; CAR19023.1; -; Genomic_DNA.
DR RefSeq; WP_000110378.1; NC_011750.1.
DR RefSeq; YP_002408835.1; NC_011750.1.
DR AlphaFoldDB; A0A0H3MNI7; -.
DR STRING; 585057.ECIAI39_2902; -.
DR KEGG; ect:ECIAI39_2902; -.
DR PATRIC; fig|585057.6.peg.3011; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR Proteomes; UP000000749; 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:CAR19023.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CAR19023.1}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 474 AA; 53833 MW; 2078EBD2842C402C CRC64;
MSVFPQGFLW GGALAANQSE GAYREGGKGL TTVDMIPHGE HRMAVKLGLE KRFQLRDDEF
YPSHEATDFY HRYKEDIALM AEMGFKVFRT SIAWSRLFPQ GDELTPNQQG IAFYRSVFEE
CKKYGIEPLV TLCHFDVPMH LVTEYGSWRN RKLVEFFSRY ARTCFEAFDG LVKYWLTFNE
INIMLHSPFS GAGLVFEEGE NQDQVKYQAA HHQLIASALA TKIAHEVNPQ NQVGCMLAGG
NFYPYSCKPE DVWAALEKDR ENLFFIDVQA RGAYPAYSAR VFREKGVTID KAPGDDEILK
NTVDFVSFSY YASRCASAEM NANNSSAANV VKSLRNPYLQ VSDWGWGIDP LGLRITMNMM
YDRYQKPLFL VENGLGAKDE FAANGEINDD YRISYLREHI RAMGEAIADG IPLMGYTTWG
CIDLVSASTG EMSKRYGFVY VDRDDAGNGT LARTRKKSFW WYKKVIASNG EDLE
//
