ID A0A4R6IFM0_9SPHI Unreviewed; 764 AA.
AC A0A4R6IFM0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 8.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=CLV32_4339 {ECO:0000313|EMBL:TDO19715.1};
OS Pedobacter duraquae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=425511 {ECO:0000313|EMBL:TDO19715.1, ECO:0000313|Proteomes:UP000295499};
RN [1] {ECO:0000313|EMBL:TDO19715.1, ECO:0000313|Proteomes:UP000295499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19034 {ECO:0000313|EMBL:TDO19715.1,
RC ECO:0000313|Proteomes:UP000295499};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2019) 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}.
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:TDO19715.1}.
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DR EMBL; SNWM01000006; TDO19715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6IFM0; -.
DR OrthoDB; 9758670at2; -.
DR Proteomes; UP000295499; 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:SF121; PERIPLASMIC 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:UP000295499};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..764
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020305172"
FT DOMAIN 684..753
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 764 AA; 83182 MW; 5ECFC6B0923DFC11 CRC64;
MRKISSLLSI LLLATLITQA QTRSAVPAAN PKMNAFIKTL MSKMTIDEKI GQLNLVTGGE
ATTGSSVSMD VEGKIKKGQV GGIFSLTTPA RVRKAQEIAV QSRLKIPLIF GQDVIHGYKT
TFPIPLGLAC TWDLNLIERT ARIAATEASA DGINWTFSPM VDISRDPRWG RISEGNGEDT
YLGSQIARAM VKGYQGTDLL SNNTLMACVK HFALYGAAES GRDYNTTDMS LDRMYNEYLP
PYKAAVDAGA GSVMVSFNDI NGVPATANKW LLSDVLRKQW GFNGFVVSDY TGVSELIEHG
LGTLPEVSAL SLKAGTDMDM VSEGFLTTLK KSYTEGKVSL QQIDNSCRLI LEAKYKLGLF
DDPFKYCSEE RAKAEILTPA NLKTARLAAA ESFVLLKNDN NTLPLKKTGK VALIGPLGNT
GSNMPGTWSV NADLKNTLSL LDGLKEVANN KVDISYTVGS NLLADAAYQQ RATMFGRDLP
RDNRSEEDMI KEAITAAKKA DVVVAALGES SEMSGESSSR TDLQLPDVQQ RLLAALLKTG
KPVVLVLFTG RPLTLKWEQE NIPAILNVWF GGTEAAHAIG DVLFGDVNPS GKLTTTFPQN
VGQVPLYYSH KNTGRPLEDG KWFSKFRSNY LDVSNDPLYP FGFGLSYSNF SYGAIKLDKK
TFKPGEAITA SVTVTNTGTV AGKEVVQLYT RDMVGSSTRP VKELKGFQKI SLKPGESREV
SFRIQESDLK FYNANLKYVA EPGAFKVFIG TNSRDVQTAD FTLL
//