ID A0A0Q5TB67_9SPHI Unreviewed; 740 AA.
AC A0A0Q5TB67;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ASG14_17505 {ECO:0000313|EMBL:KQS32335.1};
OS Pedobacter sp. Leaf194.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS32335.1, ECO:0000313|Proteomes:UP000051708};
RN [1] {ECO:0000313|EMBL:KQS32335.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS32335.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS32335.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS32335.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS32335.1}.
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DR EMBL; LMPU01000013; KQS32335.1; -; Genomic_DNA.
DR RefSeq; WP_056872596.1; NZ_LMPU01000013.1.
DR AlphaFoldDB; A0A0Q5TB67; -.
DR STRING; 1736297.ASG14_17505; -.
DR OrthoDB; 9758670at2; -.
DR Proteomes; UP000051708; 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..740
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006262810"
FT DOMAIN 658..727
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 740 AA; 81614 MW; 021C3AF847C1514B CRC64;
MKNYLASALI IAASFSSASA QDKRIEKKID SVLKLMTLDE KIGQLNQYTG DRDATGPITN
NPNKLKDIRD GKLGSMLNVR GAAETRAVQE VAMQSRMKIP LIFGLDVIHG YRVTFPIPLA
EAASWDLNEM ENAARVAGRE TAASGIHWTF APMVDIARDP RWGRVMEGAG EDTYLGSQIA
RARVKGFQGK GLGNLDAIMA CAKHFAAYGA AIAGRDYNSV DMSEHTLWET YLPPFKAAVD
AGAATFMNSF NTLNGIPATG NAYLQRDILK GQWKYTGFVV SDWGSIGEMI AHGYAKDKAQ
AAELAIKAGS DMDMESRSYL PSLAKLVTDK KVSLALIDDA VRRILRKKFE LGLFDDPYRF
SNPTRQEQEL NSPQNRAASL KMAEKSIVLL KNEKQILPLS KNLKKIAVIG PLAKSEKDMQ
GFWSVAWEND KLVSLYEGLK NKVGNNTELL YAKGCSITDS SKTGFAEAIE TAKQADVVII
AAGETLDMTG EAKSKTNIHI PGVQEDLIKA IQATGKPVVV LLMAGRPLIF NWTADNVPAI
MYTWWLGSEA GNAMANVLFG DYNPAGKLPM TFPRDEGQIP LYYNYLSTGR PSKSDKDRNY
KSAYLDSPNS PKFAFGYGLS YTTFDYSNLN LSKTQMAIGE KITVNITLKN TGKYDGEEVV
QLYLQDKFAS VVRPVKELKD FRKVMLKAGE TKNISFVIDK EKLSFYNQQL KWGAEPGDFK
LMIGTASDNI KLEKDFTLTN
//
