ID A0A087C760_9BIFI Unreviewed; 710 AA.
AC A0A087C760;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KFI79110.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFI79110.1};
GN ORFNames=BMON_0306 {ECO:0000313|EMBL:KFI79110.1};
OS Bifidobacterium mongoliense DSM 21395.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437603 {ECO:0000313|EMBL:KFI79110.1, ECO:0000313|Proteomes:UP000029082};
RN [1] {ECO:0000313|EMBL:KFI79110.1, ECO:0000313|Proteomes:UP000029082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21395 {ECO:0000313|EMBL:KFI79110.1,
RC ECO:0000313|Proteomes:UP000029082};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KFI79110.1}.
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DR EMBL; JGZE01000002; KFI79110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087C760; -.
DR STRING; 1437603.GCA_000771525_01416; -.
DR eggNOG; COG1472; Bacteria.
DR Proteomes; UP000029082; 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; 2.
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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 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 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:KFI79110.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI79110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029082}.
FT DOMAIN 543..613
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 77574 MW; 1D555BF3D96DBDC5 CRC64;
MNETSMDDAA RKATEAPRAR DLSVEEQASL TSGADAWHLQ GIESKGIGGY MITDGPHGLR
KTAGDTGAID LNHTVPTTCF PPAAGLSSSW NPELIRNVGE AMAEECIQEK VAVILGPGVN
IKRNPLRISA NVSARALREI YLPAFEHIVK TAQPWTMMCS YNRINGEHSA QNHWLLTPTC
CVGSGATTHR DERLGADHDR VASLNAGLNL EMSPSFTDEQ IVNGVRDGRV EPKQLETMAQ
GMIDLSAKTR KAMEIEGYRF DVDAHHEIAR RAADESIVML KNDANVLPAD RGDSLAVIGE
FARTPRYQGG GSSHITPTRM TGFLDALRED DVDARFAPGF TFDDAPQDPR LTDEALAAAK
ASDRMLMFLG LPNQAESEGF DRTTLDLPAK QLELLDQVTQ VNDHVVVVLS NGSVVSVAPW
RDKVQGILEA WLLGQAGGRA LADVIFGDVS PSGKLAQSIP MRIEDDPSLV NWPGEEGHVD
YGEGVFVGYR YYDTFDREVA YPFGYGLSYG SFELHDVTVR CTGDAAASVA VIVTNTSEVT
AAQTVQVYVA PPKARVARPR HELKAFAKVA LEPGESKRVE MALDERSFAY WSERFGDWRV
EAGRYVIEVG TSSRDIADTV TVELEGDGKS MPLDEWSTFE EWRTDPVGGP IVEQMKRDAD
AGLLPALPEH NAGVELFLDG MPINSMTVLL GKGGKEITRY LLEQYARRIK
//