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Database: UniProt
Entry: A0A1G8C673_9PSED
LinkDB: A0A1G8C673_9PSED
Original site: A0A1G8C673_9PSED 
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
//
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