ID A0A087CPF2_9BIFI Unreviewed; 974 AA.
AC A0A087CPF2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glycosyl hydrolase family 3, N-terminal domain protein {ECO:0000313|EMBL:KFI85152.1};
DE EC=3.2.1.21 {ECO:0000313|EMBL:KFI85152.1};
GN ORFNames=BREU_1974 {ECO:0000313|EMBL:KFI85152.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI85152.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI85152.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI85152.1,
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:KFI85152.1}.
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DR EMBL; JGZK01000010; KFI85152.1; -; Genomic_DNA.
DR RefSeq; WP_044089284.1; NZ_JGZK01000010.1.
DR AlphaFoldDB; A0A087CPF2; -.
DR STRING; 1437610.BREU_1974; -.
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:KFI85152.1};
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 16..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..522
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 599..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 106202 MW; 3F430F7084F2B3D6 CRC64;
MLDINMSDVI AVLSSLVPYL VVLGVVLVAA IIITFAVNKK TVKDVSVRKL IHSESWLVVL
VAATVAIALM LTGPMATLLN NATAKKYKLS DETIATANAQ AQELYGEAVT MLQNNDGNLP
LTGTNKLNVF GWGSTQPILG GSGSGSMSNE HPMASILSGL KQAGFETNSA LTDLYTKYRA
ERPVLNMFQQ DWTLPEVPAD QYSDSLISDA KSFSDEAMVV ITRFGGENAD LPRDMKAEGV
TYVNNSKDYE DYKQGESILQ LSQTERNMLD LVTKNFDKVT LVYNGSNPLQ FDFLANYPQI
KSVLWCPPAG QTGFNALGDI LAGKVNPSGK TSDTFLKDVR STPTLNNIGN FPYDNVEDMS
AKVSFAGSEY MSSPTFVNYV EGIYVGYKFY ETAADEGAID YDELVQYPFG YGLSYTTFDQ
KMGDVTYADG KVSFDVTVTN TGDVAGKDVV EAYYNPPYTD GGIEKASVNL VAFEKTKELA
PGESETVSIE FDDDDMASYD SKGAKAYVLE QGDYEVSIQS DSHTVIDSAT VNVPETVTYD
SEDNTHDGDK TVATNQFDNA EGYVTYLSRA NHFENLEEAI AAPASMSMSD ETKKEFTNND
IYKPSEHDDA SDEMPTTGAK NGVRLAELRG KDYDDPQWDK LLDQLTFDDM ENMIAMAGYG
TAAIDSIGKI KLTDLDGPAA LINNFTGVSS IAFPSAVGIA NTWNKDLATE FGKTLGKMAR
EMHVDGWYAP GMNIHRSPFS GRNFEYFSED ALLSGVMAAG EVAGARSQGV YSFIKHFALN
DQETNRTAML VTWANEQSIR EIYLKPFEMA VKDGGAQAVM TAYNYIGPTY AGANPALLNT
VLRDEWGFRG FTLTDYFAGF GYQNADQEIR NGGDAMLATM DVTNHVTSKS ATSVKAMRTA
SHNILYTAVN SWQYENGEPK VAMPVWKTGM WIGVAIVAVL VIGLEFLTIQ KYLKRRKQAT
VSIAAPAADA PAEA
//
