ID A0A0H3MLB7_ECO7I Unreviewed; 481 AA.
AC A0A0H3MLB7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Putative 6-phospho-beta-glucosidase {ECO:0000313|EMBL:CAR17960.1};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CAR17960.1};
GN OrderedLocusNames=ECIAI39_1829 {ECO:0000313|EMBL:CAR17960.1};
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057 {ECO:0000313|EMBL:CAR17960.1, 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; CAR17960.1; -; Genomic_DNA.
DR RefSeq; YP_002407809.1; NC_011750.1.
DR AlphaFoldDB; A0A0H3MLB7; -.
DR STRING; 585057.ECIAI39_1829; -.
DR KEGG; ect:ECIAI39_1829; -.
DR PATRIC; fig|585057.6.peg.1903; -.
DR HOGENOM; CLU_001859_0_2_6; -.
DR OMA; DPSWPIC; -.
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; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:CAR17960.1};
KW Hydrolase {ECO:0000313|EMBL:CAR17960.1}.
FT ACT_SITE 379
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 481 AA; 55601 MW; 04BFA983EDE3994B CRC64;
MCMSGFKKGF LWDGAVAAHQ LEGGWNEGGK GISIADVMTA GAHGVPREVT EGIIDGLNYP
NHEAIDFYHR YKTDIQLFAE MGFKCFRTSI AWTRIFPQGD EQEPNEEGLQ FYDDLFDECL
KQGMEPVVTL SHFEMPYHLV TKYGGWRHRK LIDFFIRFAS TVFTRYKEKV KYWMTFNEIN
NQVNFSESLC LFTNSGILYS PEEDINEREQ IMYQAVHYEL VASALAVQTG KSINPEFNIG
CMIAMCPIYP LTCAPNDMMM ATKAMHRRYW FTDVHARGYY PQHMLNYFAR KGFNLDITPE
DNAILARGCV DFIGFSYYMS FTTQFSPDNP QLNYVEPRDL VSNPYIDTSE WGWQIDPAGL
RYSLNWFWDH FQLPLFIVEN GFGAVDQRQA DGTVNDHYRI DYFASHIREM KKAVVEDGVD
LIGYTPWGCI DLVSAGTGEM KKRYGMIYVD KDNEGKGTLE RIRKASFYWY RDLIANNGEN
I
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