ID   V9V2F3_9PSED            Unreviewed;       763 AA.
AC   V9V2F3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=X970_20545 {ECO:0000313|EMBL:AHC89669.1};
OS   Pseudomonas monteilii SB3101.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC89669.1, ECO:0000313|Proteomes:UP000018660};
RN   [1] {ECO:0000313|EMBL:AHC89669.1, ECO:0000313|Proteomes:UP000018660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3101 {ECO:0000313|EMBL:AHC89669.1,
RC   ECO:0000313|Proteomes:UP000018660};
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA   Nielsen J.L.;
RT   "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT   Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL   Submitted (DEC-2013) 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; CP006979; AHC89669.1; -; Genomic_DNA.
DR   RefSeq; WP_024087685.1; NC_023076.1.
DR   AlphaFoldDB; V9V2F3; -.
DR   KEGG; pmot:X970_20545; -.
DR   PATRIC; fig|1435058.3.peg.3978; -.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   Proteomes; UP000018660; Chromosome.
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..763
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004782523"
FT   DOMAIN          683..752
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   763 AA;  83240 MW;  C1FA47A26BD74222 CRC64;
     MMKLSLLGLA MGLASQAALA APSAPPLQDK QAFIDHLISQ MTEAEKIGQL RLISIGPEMP
     KDKIREEIAA GRIGGTFNSR TAPENRPMQD AAMRSRLKIP MFFAYDTVHG ERTIFPIGLG
     MAATWDMDAV AKVGRTAAIE AAADALDMTF APMVDIARDP RWGRTSEGFG EDTYLTSKIG
     QVMVRSFQGS SPANPDSIMA IVKHFALYGA VEGGRDYNTV DMSLPKMYND YLPPYRAALD
     AGAGGVMVAL NSINGVPATS NTWLMNDLLR KEWSFKGVTI SDHGAIQELI RHGVARDGRE
     AAKLAIKAGI DMSMNDTLYG EELPGLLKSG EVTQAELDQA VREVLGAKYD MGLFKDPYVR
     IGKAETDLKD YYGNDRLHRD AARDVARRSL VLLENHNQTL PLKKAGTIAL VGPLADAPID
     MMGSWAADGK PVHSVTVREG LRRAVEGKAK LVYAKGSNVT GDKAMFDYLN FLNFDAPEIV
     DDPRPPAVLI DEAVKAAKQS DVVVAVVGES RGMSHESSSR TTLEIPASQR ELIKALKATG
     KPLVLVLMNG RPLSIAWERE QADAILETWF AGTEGGNAIA DVLFGDYNPS GKLAITFPRS
     VGQIPMYYNH TRIGRPFTPG KPGNYTSQYF EEPNGPLYPF GYGLSYSSFE LSGLKLSNKD
     LKRGDTLEAK VTVKNTGKVA GETVVQLYLQ DVSASMSRPV KELKNFQKLM LKPGESRTLS
     FRISEEDLKF YNGQLQRVAE PGEFNVQVGL DSQAVQQQSF ELL
//