ID A0A1I1E654_9BACT Unreviewed; 773 AA.
AC A0A1I1E654;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SAMN05421780_101657 {ECO:0000313|EMBL:SFB82705.1};
OS Flexibacter flexilis DSM 6793.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flexibacteraceae;
OC Flexibacter.
OX NCBI_TaxID=927664 {ECO:0000313|EMBL:SFB82705.1, ECO:0000313|Proteomes:UP000199514};
RN [1] {ECO:0000313|EMBL:SFB82705.1, ECO:0000313|Proteomes:UP000199514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6793 {ECO:0000313|EMBL:SFB82705.1,
RC ECO:0000313|Proteomes:UP000199514};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR EMBL; FOLE01000001; SFB82705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1E654; -.
DR STRING; 927664.SAMN05421780_101657; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000199514; Unassembled WGS sequence.
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; 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; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000199514};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..773
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011532002"
FT DOMAIN 698..767
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 773 AA; 85400 MW; 1ACCC1C043DD5CCB CRC64;
MNLQSFNIKA TAQALALGML CLSQTAFAQN AQDAQIEKLI SQMTLQEKVG QMAQITLDVI
GKGKDRYSSF EPLALDTAEL NKAILKYHVG SVLNTANNRA RTPQVWHELI NQMQAVATKK
ARLKIPIIYG IDAIHGTTYT AGATFFPQQI GQAATFNRNL VREGAEIAAY ETRASGIRWN
FSPVLDLGAD PRFSRQWEGY GEDPYLGTAL GLEAVKGYQG QLGQNGEIDA KHVAACLKHF
LAYSAPASGK DRTPAYMSEQ MLREYHLPAF KAAIEAGAAT IMINSGLINN IPTHANYQIL
TKLLKEELNF KGLVVSDWGD IENLYRRDHI AANDKEAIML AVNAGIDMSM IAYQYEVFCD
NLVALVKEGK VKQERIDDAV RRVLRTKQQL GLFKNAVEKQ KDYPKFADKT FQQAAYNTAA
ESITLLKNQN GVLPLAKNKK VFVTGPNANS MRTLNGGWSY SWQGEKVEDF AGQYNTILEA
IQNEVGKANV QYAAGVSYKM TGSYYEEFAD KLEEAVAQAA QSDVIVVCVG ENSYTEKPGD
LNDLYLSDLQ TTLVQRLAAT GKPVVVVLNE GRPRVISRFE QSVPAIVQAY LPGNFGGDAI
ADILFGDVNP SGKLPYNYPR YPNSVSTYYH KPSEEQKKAE GMYNYEADYN PQYEFGTGLS
YTTFKYSNLQ LSKNKLKVGE SLSVSVDVTN TGTREGKETV LLYLSDKVAS ITPDVKRLKG
FDKISLKPNE TRKLTFTLSP AEMAFIGLDL KPTVEAGDFE VQVADQKAVF VCE
//