ID A0A087CPE9_9BIFI Unreviewed; 978 AA.
AC A0A087CPE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative beta-glucosidase {ECO:0000313|EMBL:KFI85149.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFI85149.1};
GN ORFNames=BREU_1971 {ECO:0000313|EMBL:KFI85149.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI85149.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI85149.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI85149.1,
RC ECO:0000313|Proteomes:UP000028984};
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:KFI85149.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JGZK01000010; KFI85149.1; -; Genomic_DNA.
DR RefSeq; WP_044089283.1; NZ_JGZK01000010.1.
DR AlphaFoldDB; A0A087CPE9; -.
DR STRING; 1437610.BREU_1971; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 3187562at2; -.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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:KFI85149.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 444..518
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 978 AA; 106364 MW; E7577D6C75EE7A00 CRC64;
MLSINWSDVW NVIASIAPQL IAIAVVFVLA LALTIGVNKK TVKNVGTRKL IHSESWLVFL
VAVVVAVSMM LFGPLASLLN SATATKYELS QTTISNANKL AKEIQAEAIT MLKNEDGNLP
LANKKVNVFG WGSTNPVYGG TGSGSMNQNY KTTSLLDGLK EAGIETNADL SKLYTDYRAD
RPVVAMAEQD WTLPEVPADQ YSDSLISKAK SFSDEAVVVI TRVGGEGADL PTNMKAKGIT
YTNNSKDYED FKDGESFLEL SQTEKNMIDL VTKNFDKVTV VYNGANAFEL GFVDQYPQIK
SVLWCPPAGQ TGFSALGDVL SGETNPSGKT SDTFIKDLTQ QPSYNNFGDF KYDNMSEFPT
ENFEEGETSP AFVNYAEGIY VGYKYWETAA DEGAINYDDY VQYPFGYGLS YTTFDQKMGD
VTYSGGKVSF DVTVTNTGDV AGKDVVETYY NPPYTNGGIE KASANLVAFE KTKELAPGES
ETVKISFDDD DMASYDSKNA KAYVLEKGDY DISIQSDSHT TIAEQTITVG DTITYDSDSN
THNGDKTVAT NVFDDASGDE LGVTYLSRAD HFANYAKATA APTNYTLPED LKADFRNNSN
YKASETNNDS DEMPTTGAKN GVRLADLTGK DYDDPLWDQL LDQLTFDEMD NLIAFGGYGT
QAVNSIGKIA LTDVDGPASL NNNFTGVGSI GFPSSTSVAC TWNKDLAKQF GDGIGNMAHD
MHVAGWYAPA MNIHRNAFAG RNFEYFSEDA LLSGTMASQQ VAGAQAKGVY AFMKHFALND
QETNRLSELN TWASEQSIRE IYLKPFEMSV KEGGAGAVMS SFNYIGIEWA GSHSGLLNTV
LRDEWGFRGM VLTDYFGGYG YQNADRAIRG GNDVMLATTD VTNHITDKSA TSIKAMRTAS
HNILYTAANS WLYENGEPDV PTPIWKTITY VVWGVTAVLV IGLEFLTIQK YLKRRKQATV
SIAAPAADGG SEAPASEA
//