ID H6CIT2_9BACL Unreviewed; 707 AA.
AC H6CIT2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:EHS57667.1};
GN ORFNames=WG8_2623 {ECO:0000313|EMBL:EHS57667.1};
OS Paenibacillus sp. Aloe-11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1050222 {ECO:0000313|EMBL:EHS57667.1, ECO:0000313|Proteomes:UP000005078};
RN [1] {ECO:0000313|Proteomes:UP000005078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aloe-11 {ECO:0000313|Proteomes:UP000005078};
RX PubMed=22461553; DOI=10.1128/jb.00087-12;
RA Li N.Z., Xia T., Xu Y.L., Qiu R.R., Xiang H., He D., Peng Y.Y.;
RT "Genome Sequence of Paenibacillus sp. Strain Aloe-11, an Endophytic
RT Bacterium with Broad Antimicrobial Activity and Intestinal Colonization
RT Ability.";
RL J. Bacteriol. 194:2117-2118(2012).
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; JH601054; EHS57667.1; -; Genomic_DNA.
DR RefSeq; WP_007430612.1; NZ_JH601054.1.
DR AlphaFoldDB; H6CIT2; -.
DR HOGENOM; CLU_004542_5_1_9; -.
DR Proteomes; UP000005078; 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; 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.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:EHS57667.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHS57667.1}.
FT DOMAIN 629..698
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 707 AA; 79336 MW; 9F19A7633E691722 CRC64;
MDNKKIIELL QKMTLAEKIG QLSQTTGEHY VGKIDIEMVE TGPDFPDHML EGDTLYTMGS
IIGVSSARIT NLIQSKYLQK SRLKIPLLFM HDAIHGYRTI FPIPLGLSCT WDEGIVQQAA
ADTASELRAA GIHVNFSPMV DLVRDSRWGR VMESFGEDHL LSGNLGRSMI RGYQKDEDGE
FAESGVAACL KHFAAYGAGI GGKDYNAVDM SWREFYAYYG KPYEIALQEK PKFVMSSFNT
FNGVPVSASE QMMKEILRGT YQFDNIVISD WGAVAELQNH RVAGNDKEAA EMALKAGIDI
EMVSTLYLEH YEQILEENPA LIQDIDAAVL KILQLKNEMG LFENPFVNEA RENEVLMNPR
FLEHAKDIAK RTCVLLKNEQ MLPISKEYKK IIIVGPFAGS NQLLGNWRCK GSFDDVVTLA
EGMKRVDDSF DLQVYESLKD CPQAELEQSD YIVVAVGEHW ELSGEGHSSV NIDLEASQQQ
LIREVKQTNK PYACICFSGR PLALQNIIDD IPALLWCWYP GTQAGSAIAE LITGQDTPSG
KLTMSFPRHS AQAPIYYNEY STGRPANESS YSSRYQDCEI GPLFPFGHGL TYTGAQYSDF
KISRHHLTAG EELTISFQVS NPSGYDYSEI TILYIEDLVS KAVRPVREMK KYQVVGVPAH
QTVNVQMTLA LDDLQYLDTS LQQTVETGKF NIYINDLDHP VFTIEYR
//
