ID A0A0C1D711_9SPHI Unreviewed; 765 AA.
AC A0A0C1D711;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=OC25_14640 {ECO:0000313|EMBL:KIA92941.1};
OS Pedobacter kyungheensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1069985 {ECO:0000313|EMBL:KIA92941.1, ECO:0000313|Proteomes:UP000031246};
RN [1] {ECO:0000313|EMBL:KIA92941.1, ECO:0000313|Proteomes:UP000031246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 16221 {ECO:0000313|EMBL:KIA92941.1,
RC ECO:0000313|Proteomes:UP000031246};
RA Anderson B.M., Newman J.D.;
RT "Pedobacter Kyungheensis.";
RL Submitted (OCT-2014) 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:KIA92941.1}.
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DR EMBL; JSYN01000017; KIA92941.1; -; Genomic_DNA.
DR RefSeq; WP_039477389.1; NZ_JSYN01000017.1.
DR AlphaFoldDB; A0A0C1D711; -.
DR OrthoDB; 9758670at2; -.
DR Proteomes; UP000031246; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..765
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002130647"
FT DOMAIN 685..754
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 765 AA; 83334 MW; B3E8FA607FB88F72 CRC64;
MKRAKILAVF FTAFVLNASA QTKKPVSAEE AKMNTFINNL MAKMTVDEKI GQLNLPSSGD
ITTGQANSSD IGKKIKDGQV GGLFNIKGVE KIRAVQKVAV ENSRMKIPLL FGMDVIHGYN
TVFPIPLGMS ATWNMDAVQK SARVAAIEAS ASGINWTFSP MVDISRDPRW GRISEGNGED
PYLGSQIAKA MVKGYQGKLQ ANNEILACVK HYALYGAAEA GRDYNTTDMS KVKMYNEYLP
PYKAAVDAGA ASIMASFNEV DGIPATGSKW LMTEVLRNQW GFKGFVVTDY TGIPEMIAHG
MGDLQTVSAL ALNAGVDMDM VGEGFLGTLK KSLAEKKVNI DQINRACRLI LQAKYKLGLF
ADPYKFCDAN RAEKEVFSPE NRSIARQIAA ESFVLLKNKN NILPLKKSGT IGLVGPLADN
TANMYGTWSV AALFDKSVTV LQGLKNALGN NAKILTARGA NFLADSALEH RYVNIHNPTY
KHDSRSEAEM IKEALAVAEK SDVIVATVGE GSEFSGESSS VTDIQIPETQ KNLLKALVKT
GKPVVMVLFT GRPLALKWED ENIPAILNVW FPGSEAGSAI ADVLFGDANP SGKLSATFPQ
NVGQVPLYYA HKNTGRPLAD GKWFEKFRSN YLDVSNDPLY PFGYGLSYTT FNYSDIKLSS
NTLTKGKSIT ASVTLTNTGK YDGQEVVQLY IRDLVGSITR PVKELKGFQK VGLKAGESKN
ITFTLTENDL KFYNSDLKFV AEPGDFKVFI GTNSRDVKEA SFTLK
//