ID W7D195_9LIST Unreviewed; 481 AA.
AC W7D195;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative beta-glucosidase {ECO:0000313|EMBL:EUJ45614.1};
GN ORFNames=PRIP_07158 {ECO:0000313|EMBL:EUJ45614.1};
OS Listeria riparia FSL S10-1204.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1265816 {ECO:0000313|EMBL:EUJ45614.1, ECO:0000313|Proteomes:UP000019248};
RN [1] {ECO:0000313|EMBL:EUJ45614.1, ECO:0000313|Proteomes:UP000019248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL S10-1204 {ECO:0000313|EMBL:EUJ45614.1,
RC ECO:0000313|Proteomes:UP000019248};
RX PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L., Fortes E.D.,
RA Nightingale K.K., Kephart D., Wiedmann M.;
RT "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT cornellensis sp. nov., Listeria riparia sp. nov. and Listeria grandensis
RT sp. nov., from agricultural and natural environments.";
RL Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
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:EUJ45614.1}.
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DR EMBL; AODL01000007; EUJ45614.1; -; Genomic_DNA.
DR RefSeq; WP_036084771.1; NZ_AODL01000007.1.
DR AlphaFoldDB; W7D195; -.
DR GeneID; 58716799; -.
DR PATRIC; fig|1265816.5.peg.1417; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000019248; 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:SF136; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLC; 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}.
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 481 AA; 55002 MW; 2E6FF6FD2E8A73EF CRC64;
MQHKTLKPFP KDFLWGSASA AYQVEGAWDT EGKGPSVWDE FVRIPGKTFK GTNGDVAVDH
YHRFKEDVAL MAEQGLKAYR FSIAWSRIFP KGHGEVNEAG LAFYDALVDE LVAHNITPVI
TLYHWDIPQA IQDEYGGWES RRIIQDFTDY AEVCFKRYGD RVKYWVTLNE QNVFISHGYK
LALHPPGLTD DKRMFQANHI ANLSNASAIA KFRELGMDGK IGPSFAYGPN YAIDGKPENA
LAADNSEEFN AHLWMDVYTW GEYPIAVWNW LEDNGFAPDL EPGDTELLKK GKPDFMGVNY
YRTMTNAANP LDGVGVGKMN TTGEKGSTQE SGLPGVYRHV NNPYLEKTNW DWDIDPTGLR
VGLRRIASRY RLPILITENG LGEYDTLEEG NEIHDEYRID YIRAHSIAIQ EAITDGVEML
GYCTWSFTDL LSWLNGYQKR YGFVYVDRDE NDEKELARYK KDSFYWYQKT IKENGANLIN
E
//