ID L0K850_HALHC Unreviewed; 1031 AA.
AC L0K850;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=Halha_0267 {ECO:0000313|EMBL:AGB40278.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB40278.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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};
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DR EMBL; CP003359; AGB40278.1; -; Genomic_DNA.
DR RefSeq; WP_015326004.1; NC_019978.1.
DR AlphaFoldDB; L0K850; -.
DR STRING; 748449.Halha_0267; -.
DR KEGG; hhl:Halha_0267; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_294204_0_0_9; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000010880; Chromosome.
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; 2.60.120.260; Galactose-binding domain-like; 2.
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 InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF02018; CBM_4_9; 2.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGB40278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010880};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1031
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003944397"
FT DOMAIN 108..246
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 281..407
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 451..791
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 829..1026
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 1031 AA; 113972 MW; FA7F8E6487A71D90 CRC64;
MKKLWIISFL LLSVLVLGGC KAPVDQSQIT NLAIKVRDTN NQQVAANIKV LHAGEKVASK
QGSEVKFELL KNKNYKLEVD KEGYLAKTVN LPLEEDSNLT VKLIKVANLV GNGDFTTPIS
NANPKANGEL DSGDSWVYHQ NSNGQGSVTI EGGEAKVKVN NPGNNPWSVQ LLQGPITLEK
SAYYKISFEA HADQKAKLHL KLGANGNRGW VGYEERDVNL TTTPQTYQFK FVMEEETDQQ
ARFELWFLNQ TDYTIDNIKL IKIKSGTATE QKDEVKIESG EIITNGSFAN KTVGWGSDGN
IELTNQAGKL KAKIESIGDN SYTPQVNQKG IKMVKDVTYT VSFTARANKA RKMNVAIGKP
LNQAPWYIDY IGEVKTFDLT TEMKNYKFRF TMKEESYDDA KLTFELGQIT DGSAATTVYL
DNVRITPDLG FYTDSSLTID KRVSRIISLM TLDEKIGQMT QGERRHVSPK QVRKYHLGSI
LSGGGSTPGN NTPQDWIDMY NNFQEEALSG RLELPLIYGV DAVHGHNNLK GATIFPHNIG
LGAMGKGLME VNKSKQAQKW IEKIARISAQ ETAATGMDWD FAPAVSVVRD ERWGRSYESF
GETAELQKLL AGPYVKGLQG TKDILSKERG HVVATAKHFI GDGATKWETG DAGYQIDRGN
VNIDLNKLKK LHGQGYLEAI DENVGTIMIS YNSYQGTKMH AHQELIQNYL KAPQKEGGLG
FDGFVISDWA AIHEIDAPTH YAKVVKSVNA GIDMFMEPSD WHKFMIDLKT AVKNGDVKES
RINDAVKRIL KIKFKAGLFK KALTDNDSID TIGSQEHRAV AREAVRKSLV LLKNQNQILP
LSKDNKFYIT GSNADNLGHQ CGGWTIKWQG FSGNQATTGT TIKEGIANLL QGQKGQIVND
LNQADVAIAV VGEKAYAEGK GDDADLELSV SDKRELQRIE ESGKPMVVIL VSGRPMIVSP
RIENWDVFVA AWLPGTAGGG VADVIFGDYN FTGKLPVSWP RSVEQLPLNV GDKNYNPLFN
YGYGLKMNLE N
//
