ID A0A0R1ZUH3_9LACO Unreviewed; 486 AA.
AC A0A0R1ZUH3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phospho-beta-glucosidase {ECO:0000313|EMBL:KRM55417.1};
GN ORFNames=FC18_GL001312 {ECO:0000313|EMBL:KRM55417.1};
OS Lacticaseibacillus sharpeae JCM 1186 = DSM 20505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM55417.1, ECO:0000313|Proteomes:UP000051679};
RN [1] {ECO:0000313|EMBL:KRM55417.1, ECO:0000313|Proteomes:UP000051679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM55417.1,
RC ECO:0000313|Proteomes:UP000051679};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM55417.1}.
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DR EMBL; AYYO01000022; KRM55417.1; -; Genomic_DNA.
DR RefSeq; WP_054678343.1; NZ_BBAC01000012.1.
DR AlphaFoldDB; A0A0R1ZUH3; -.
DR STRING; 1291052.FC18_GL001312; -.
DR PATRIC; fig|1291052.5.peg.1330; -.
DR OrthoDB; 1688691at2; -.
DR Proteomes; UP000051679; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468};
KW Reference proteome {ECO:0000313|Proteomes:UP000051679}.
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 486 AA; 55606 MW; B4702930BFC7B75B CRC64;
MAKLREDFLW GGAVAAHQLE GGWQEGGKGV SVADVMTAGA NGVERTITDG VLPGYNYPNH
DAIDFYHHYK DDVKLFADLG LKAFRTSIAW TRIFPNGDET EPNEAGLQFY DDLFDELLKN
GIEPVITLSH FEMPYHLVTE YGGWRSRKVI DFFVRFATTV FKRYKNKVRY WMTFNEINNQ
ANVGTEFALF TNSGVKVKPG EDAEKVMYQA AHYEVVASAL AVQIGHQINP DFQIGAMIAM
VPLYPISPRP ADIFKAERAI QTRYWFADVQ ANGEYPAWLT RYQERAGFNL DITLEDRDVL
KQGKVDYIGF SYYMSNTVKA KDDEPDSYKY EEDKDIVRNP TVEASEWGWQ IDPQGLRYAM
NWFNDRYKLP LFIVENGFGA IDKLDADGHV HDDYRVNYMR EHIEQMELAV DVDGVDLIGY
TPWGFIDLVS AGTGQMDKRY GLIYVDKNDK GEGTLARSKK DSFYWFQNVI KTNGEDLTDV
VPDYQV
//