ID A0A1G8C673_9PSED Unreviewed; 766 AA.
AC A0A1G8C673;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SAMN05216272_101392 {ECO:0000313|EMBL:SDH40420.1};
OS Pseudomonas panipatensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=428992 {ECO:0000313|EMBL:SDH40420.1, ECO:0000313|Proteomes:UP000199636};
RN [1] {ECO:0000313|EMBL:SDH40420.1, ECO:0000313|Proteomes:UP000199636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7469 {ECO:0000313|EMBL:SDH40420.1,
RC ECO:0000313|Proteomes:UP000199636};
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; FNDS01000001; SDH40420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8C673; -.
DR STRING; 428992.SAMN05216272_101392; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000199636; 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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..766
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011489561"
FT DOMAIN 686..755
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 766 AA; 83823 MW; E29D15D00257C19C CRC64;
MKRNAISQIC WFSLLLGLNS PYLLAAEGPA VPAPGQSKDA FIRELMQRMT LDEKIGQLRL
VSVGPDHPKP VLLEEIAAGT TGAVFNTVVR PGIRDLQDAA MRSRLKIPLF FAYDVVHGHR
TVFPIGLGLA ASWDMAAITE SARISALEAS ADGLNLTYSP TVDIARDPRW GRVSEGFGED
AWLTSKVAAA VVKGYQGKGL DQPQTIMAGV KHFALYGAGE GGRDYNTVDM SPQRMYQDYL
PPYRAAIDAG AGAVMVSLNS INGVPATANK WLLQDLLRGQ WGYRGMTLSD HGAVKELIKH
GVAADERQAV KLSIKAGVDM NMNDDLYGKH LPELLKAGEI SQSDIDNACR DVLAAKWDMG
LFKDPYRYLQ GADPVDTDAE SRLHRDAARE VARKGMVLLK NKDDVLPLKR EGTIALIGPL
ADSKRDVMGS WSAAGKAFQA VTLLEGMRHA TRGKAQLLYA KGANVTNNPD IIKYLNEYNT
DVDIDPRDPK VVIAEALEVA KKADVIVAAV GEAQGMAHEA SSKTNLHISF SQIELLKALK
ATGKPLVLVL MNGRPLDLSW EDGIADAILE TWFSGTEGGN AIADVLFGDY NPSGKLTMTF
PRSVGQVPIY YNHLNTGRPF DHEHPNKYTS RYFDSANGPQ YPFGYGLSYT RFSVSDIQLS
SAKLRKGDSL TAKVTVKNTG KRAGETVVQL YLHDVAASIS RPVKELKGYR KLMLKPGESK
VVEFPIREED LRFYDSSLRY ASEPGDFKVY IGLDSDDVKE QQFTLL
//