ID A0A080N1T5_9BIFI Unreviewed; 816 AA.
AC A0A080N1T5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative beta-glucosidase {ECO:0000313|EMBL:KFF30797.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFF30797.1};
GN ORFNames=BBOMB_0108 {ECO:0000313|EMBL:KFF30797.1};
OS Bifidobacterium bombi DSM 19703.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF30797.1, ECO:0000313|Proteomes:UP000028730};
RN [1] {ECO:0000313|EMBL:KFF30797.1, ECO:0000313|Proteomes:UP000028730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF30797.1,
RC ECO:0000313|Proteomes:UP000028730};
RX PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL Appl. Environ. Microbiol. 80:6290-6302(2014).
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:KFF30797.1}.
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DR EMBL; ATLK01000001; KFF30797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080N1T5; -.
DR STRING; 1341695.BBOMB_0108; -.
DR eggNOG; COG1472; Bacteria.
DR Proteomes; UP000028730; 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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-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 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:KFF30797.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFF30797.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT DOMAIN 584..654
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 816 AA; 87745 MW; 243EB35CC9AE8AAD CRC64;
MGDEKTMRLE DLSVAQKAAL LSGASEWDSR GSKKADIPSF VMSDGPHGVR RQLGSGDHLG
LGSSKPATCF PTAGTVANSW DPALAEAMGE ALGREAHDLD VNVLLGPGMN IKRNPLCGRN
FEYYSEDPQV AGHMAAGLIK GVQSNGVASC PKHFAVNSQE LRRQASNSVV DERTLRELYL
TAFEIAVRTA RPWAIMSSYN EVNGVYAHEN KKLLTEILRD EWGFDGAVIS DWGGSNSAVA
AVKAGASLEM PSPGYTSVRE LVAAVQSGDL SEADLTARAA EVAKVAKRAH VDGVGRDDLL
SDDIIKKHHD VARRVAEESI VLLKNDHDVL PLASGTRVAV VGDMARTARY QGSGSSKINA
TKVENLLDEL DKADSGVEVS GFAQGYDRQG ATDQGLIDEA VALVSSAATD VAVAVVGLDE
RSESEGLDRT TMAIPKPQND LVNALAATGK PIVVVLVAGA PVELPWFDGI DAMLYIGLSG
QAGASATSRV LCGKVNPSGH LAETWPLKYE DCPSSQWYPA SGRDSIYREG PFVGYRYYET
VGVPVRFPFG FGLSYSDFSL ADLALDRQGA AFVVTNESDT PGSAVVQLYV HGPRNGVLRP
ERELKGFIKV ALAAHESKKV RIDFDETTFR HFDIDEGRWG IQSGDWTVLV GTDVEHLPLN
GQISIDGDDI SRPVDPAFGH YLKGDVKHVT DAEVAQLFGH TVTAAVEPTV FGANDPISSW
VRSPGWTART VARFLKKREL KVREKTGSPD LNTLFILNMP PRAMCKMTQG MVDQDMVKAV
VAIANGHTFR GIVSLIAGFF RGRGAERRMA KELADM
//