ID   B3DRK8_BIFLD            Unreviewed;       757 AA.
AC   B3DRK8;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Beta-glucosidase-related glycosidase {ECO:0000313|EMBL:ACD99390.1};
GN   Name=bglX {ECO:0000313|EMBL:ACD99390.1};
GN   OrderedLocusNames=BLD_1945 {ECO:0000313|EMBL:ACD99390.1};
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD99390.1, ECO:0000313|Proteomes:UP000002419};
RN   [1] {ECO:0000313|EMBL:ACD99390.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD99390.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA   Lee J.H., O'Sullivan D.J.;
RT   "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT   DJO10A and construction of a shuttle cloning vector.";
RL   Appl. Environ. Microbiol. 72:527-535(2006).
RN   [2] {ECO:0000313|EMBL:ACD99390.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD99390.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; CP000605; ACD99390.1; -; Genomic_DNA.
DR   RefSeq; WP_008782746.1; NZ_AABM02000004.1.
DR   AlphaFoldDB; B3DRK8; -.
DR   KEGG; blj:BLD_1945; -.
DR   HOGENOM; CLU_004542_4_1_11; -.
DR   Proteomes; UP000002419; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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:ACD99390.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT   DOMAIN          591..661
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   757 AA;  81617 MW;  82EBB1D1C72503C9 CRC64;
     MSESTYPSVK DLTLEEKASL TSGGDAWHLQ GVESKGIPGY MITDGPHGLR KSLASSAGET
     DLDDSVPATC FPPAAGLSSS WNPELIHKVG EAMAEECIQE KVAVILGPGV NIKRNPLGGR
     CFEYWSEDPY LAGHEAIGIV EGVQSKGVGT SLKHFAANNQ ESDRLRVDAR ISPRALREIY
     FPAFEHIVKK AQPWTIMCSY NRINGVHSAQ NHWLLTDVLR DEWGFEGIVM SDWGADHDRG
     ASLNAGLNLE MPPSYTDDQI VYAVRDGRIT PAQLDRMAQG MIDLVNKTRA AMSIDNYRFD
     VDAHDEVAHQ AAIESIVMLK NDDAILPLNA GPVANPSAMP QKIAVIGEFA RTPRYQGGGS
     SHITPTKMTS FLDTLAERGI KADFAPGFTL DLEPVDPALE SEAVETAKNA DVVLMFLGLP
     EAAESEGFDR DTLDMPAKQI TLLEQVAAAN QNVVVVLSNG SVITVAPWAK NAKGILESWL
     LGQSGGPALA DVIFGQVSPS GKLAQSIPLD INDDPSMLNW PGEEGHVDYG EGVFVGYRYY
     DTYGKAVDYP FGYGLSYATF EITGVAVAKT GANTATVNAT VTNTSDVDAA ETVQVYVVPG
     KADVARPKHE LKGFTKVFLK AGESKTVTID LDERAFAYWS EKYNDWHVEA GEYAIEVGVS
     SRDIADTVAV ALDGDGKTQP LTEWSTYGEW EADPFGAKIV AAVAAAGEAG ELPKLPDNAM
     MRMFLNSMPI NSLPTLLGEG GKKIAQFMVD EYAKLSK
//