ID A0A1M7J7D5_9GAMM Unreviewed; 847 AA.
AC A0A1M7J7D5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SHM48905.1};
GN ORFNames=SAMN05428972_3763 {ECO:0000313|EMBL:SHM48905.1};
OS Rhodanobacter sp. OK091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1881037 {ECO:0000313|EMBL:SHM48905.1, ECO:0000313|Proteomes:UP000184078};
RN [1] {ECO:0000313|EMBL:SHM48905.1, ECO:0000313|Proteomes:UP000184078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK091 {ECO:0000313|EMBL:SHM48905.1,
RC ECO:0000313|Proteomes:UP000184078};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; FRCH01000006; SHM48905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7J7D5; -.
DR STRING; 1881037.SAMN05428972_3763; -.
DR Proteomes; UP000184078; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
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 Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000184078};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..847
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013223711"
FT DOMAIN 431..574
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 847 AA; 91970 MW; 4E25D23E5923BA00 CRC64;
MRMKPLSRIL PALLLTCLGP IFAHAAVPAA SGPVVDSPAV EQRVNAMLGK LTLEQKVDLI
GGVDNMFIRA EPAAGLPRMQ MSDGPFGVRS VGPSTAYMAG VGLAASWDPQ LAQQVGEAMG
RDARARGVHF FLGPGANIHR APQNGRNMEY YSEDPFLAGS MGVGFIDGIQ SQGVVATIKH
FVANNSEYDR RHLDTLIDER TLREIYLPAF EMAVKDAHVG AVMSSYNLVN GDHLSENRAI
SHDILKQEWG FDGIFMSDWQ ATHDGIKAFN AGLDLEMPSA EAMTPQRLLP QLKDGKLSPD
VLNDKVCRIL RTAVRFGFLD RSQKDLSLPL LSLDNDAVAL QSAREGLVLL KNELNVLPLD
AGKLKTIAVI GPNAFPAISS AGGSSHVDTF EAQSVLSGIT HQLGDKVRVL YSRGLPSADD
VFKQSVFVSP DGGKGLQRQT FANSDFQGKP AESGVDAHVD QWKPELWTTS ATERQSIRWS
GRFVPTHSGK YLFLTAAASL DTYQLFVDGR NVIEQPQREG QAPLYVTLDL VAGKPVTIRL
DYKPDVSYSR MGLGVIALDE LISPDARKMA AMADAAVVAV GFDPTSESEA FDRTFQLPWG
QEALIEAVAA ANKKTVVTVN SGDAYATDSW LAKVPALLQS WYPGQQGGRA IAEVLFGAHT
PEGKLPISFG REWKDNPTRD FYDAPPHPAG SNPTVKYGEG VFLGYRWYTS YPEKAQPLFA
FGYGLSYTTF TFANLQLSPA AAKAGDTVSV SFDVTNTGQR VGAEVAQVYV GDPSAKVARP
ARELKAFRKV RLQPGQTEHV TLVLDRRSFA YYDVKQHAWQ VDPGRFKVYV GDASNHTPLS
ADLTLGD
//