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Database: UniProt
Entry: D7UX19_LISGR
LinkDB: D7UX19_LISGR
Original site: D7UX19_LISGR 
ID   D7UX19_LISGR            Unreviewed;       743 AA.
AC   D7UX19;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX {ECO:0000313|EMBL:EFI84227.1};
GN   ORFNames=HMPREF0556_10780 {ECO:0000313|EMBL:EFI84227.1};
OS   Listeria grayi DSM 20601.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI84227.1, ECO:0000313|Proteomes:UP000010119};
RN   [1] {ECO:0000313|EMBL:EFI84227.1, ECO:0000313|Proteomes:UP000010119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI84227.1,
RC   ECO:0000313|Proteomes:UP000010119};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EFI84227.1}.
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DR   EMBL; ACCR02000003; EFI84227.1; -; Genomic_DNA.
DR   RefSeq; WP_003757821.1; NZ_GL538353.1.
DR   AlphaFoldDB; D7UX19; -.
DR   STRING; 525367.HMPREF0556_10780; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_9; -.
DR   Proteomes; UP000010119; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:EFI84227.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010119}.
FT   DOMAIN          662..731
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   743 AA;  82428 MW;  A33C0C2328140164 CRC64;
     MKKEKLEALF QTLTLEEKIG QVVQVSGNVY MEDKQTIDTG PLQDIGFHSD FQLDLIGSVY
     NVNDWRQIKK IQTEYLHKHP KKIPLLIMAD VIYGFRTINP IPLAQAGSFD FELIQKGATE
     TAKESYRNGL HVLFSPMLDL VRDPRWGRVM ESPGEDVYVA SQYANSIVTG YQGELNEEKT
     IEEDHVAAGI KHFAAYGAPE AGREYNSVDM SLLKLRQTYL PPYEAALKAN AKLVMTAFNL
     LNGIPATANK FLNRKILREE NNFDGVLISD FAAIEELVDH GYAKDKQTAA QKALEAGVDI
     DMMTSCYANE LQSLIESDQL PMELLDEAVR RILVLKNELG LFENPYRGLE AETAGEILTA
     TAKQTAIELV EKSSVLLKND QQLPLEKPEK LAVIGPYGTS KLTLGFWASV TGSPLDTISL
     AEGLQQHFPN QQLLLSKGYN LFDDYEAFGP LKEAVIQLNG PIDAENELVQ EAVEKAKQAD
     KILFTFGENF MESGEGASKA HLDLPEKQLH LLRELKKTGK PIVGILYTGR PLVLTEVATL
     FDSLLLVWYP GTMGGIGISN LLTGKANPSG RLAMTFPRAE GQIPIYYAHH STGRPMGTSN
     QQPRFTSRYT DEANEPLYPF GYGLSYSSFQ ITTDSAAVHC RAGDTFSFKL AIQNTSQVDG
     EEVIQFYIQA AASEIVRPVQ ELVGSKRIFV RAKSVEEVEI EVDSNSLGYV NESGEHVLEK
     GSYRYLIATS SDNVHKSISI VIE
//
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