ID A0A086YZL4_9BIFI Unreviewed; 757 AA.
AC A0A086YZL4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KFI39714.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFI39714.1};
GN ORFNames=BACT_0414 {ECO:0000313|EMBL:KFI39714.1};
OS Bifidobacterium actinocoloniiforme DSM 22766.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI39714.1, ECO:0000313|Proteomes:UP000029015};
RN [1] {ECO:0000313|EMBL:KFI39714.1, ECO:0000313|Proteomes:UP000029015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI39714.1,
RC ECO:0000313|Proteomes:UP000029015};
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, 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:KFI39714.1}.
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DR EMBL; JGYK01000001; KFI39714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086YZL4; -.
DR STRING; 1437605.AB656_00685; -.
DR KEGG; bact:AB656_00685; -.
DR PATRIC; fig|1437605.7.peg.138; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 3187421at2; -.
DR Proteomes; UP000029015; 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; IPR048100; Alph_arabinopyran.
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 NCBIfam; NF041610; alph_arabinopyran; 1.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161, ECO:0000313|EMBL:KFI39714.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000029015}.
FT DOMAIN 588..658
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 81744 MW; 2CE16D9DF39CFE2E CRC64;
MTDTNASRPQ PAFPKASDLS LEEKASLTSG GDAWHLQGIE SKGVPGYMIT DGPHGLRKTE
EKTGAVDLNE SVPATCFPPA AGMASSWNPQ LVEEVGRAMG QECIQEQVAV ILGPGVNIKR
NPLGGRCFEF WSEDPFLAGH EAVGIVSGVQ SQGVGTSLKH FAVNNQETDR LRISARVSQR
ALREIYLPAF EYIVKTAQPW TVMCAYNQIN GVHASQDHWL LTDVLRKEWG FTGIVMSDWG
ADHDRVASLN AGLNLEMPPS YTDDRVVSAA RDGSLPVDQL DSMAQGMIDL AAKAAPAMSR
TDYRYSVDEH RDVARRAARE SAVLLKNEGA LLPLDPNGTV AVIGEFARTP RYQGGGSSHI
TPTAVSSFLD AAGERGAKVD FAPGFTLDDE PQDESLTSQA VESARKAKSV LLFLGLPEQE
ESEGADRTNL DLPAKQLDLL KAVSAVNPHV AVVLSNGSVV SIAPWRDQAQ AILEGWLLGQ
DGGRALADLI YGDYSPSGKL AQTIPMDLAD DPTMLNWPGE EGHVDYGEGV YVGYRYYDSF
HKPVAYPFGF GLSYASFELS DVHVTARQGN TATVSVRVTN TSDRDAAETV QVYVAPGKAK
VARPSHELKA FRKVFLKAGE SQEISIDLDE RAFAYWSETH AGWRIEAGDY GVEVGTSSRD
IAATVTISLP GDGKRLPLTE WSTMDEWRED PVGGPIMERM EALGRSGELP ELPIDNASAA
IFLASMPINS LFVLMGGNGS KLTNYLLDNY AQATHAA
//