ID G7USD3_PSEUP Unreviewed; 761 AA.
AC G7USD3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN OrderedLocusNames=DSC_06770 {ECO:0000313|EMBL:AER56005.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56005.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER56005.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER56005.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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; CP003093; AER56005.1; -; Genomic_DNA.
DR RefSeq; WP_014160181.1; NC_016147.2.
DR AlphaFoldDB; G7USD3; -.
DR STRING; 1045855.DSC_06770; -.
DR KEGG; psd:DSC_06770; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_6; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000005870; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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 Reference proteome {ECO:0000313|Proteomes:UP000005870}.
FT DOMAIN 679..748
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 761 AA; 80848 MW; 88F001038A232480 CRC64;
MTPGGITRRQ LLVATGAATL LSQLPMGLAL GRDAGKVPAF IDTLIGKMTL QEKAGQLTLF
SSASQNGAAA AANPVTFTGA VSVQIAAAIA GQLTGVFNSS NVLWHERLQK AAMQSRLKIP
MIFAADVIHG FTTVFPVPLG ESASFEPELA RRTARAAAME AASVGIDWTF APMVDIARDA
RWGRGVEGSG EDVLLGRRMA AARVQGFQGE RGLADPEAVA ACPKHFCAYG AAEGGLDYNT
TDVSERVLRQ TYFPPFQAGF EAGALTTMAA FNEISGIPAT ANKWLLDDVL RGQWDFRGVV
VSDYTGDEEL IAHGFARDGR DAARLAILAG VDMSMQSGLY LKHLPDLVES GEVPLAVVDA
SVRRVLQLKA QLGLFDDPFR RIRPSAPSRQ RLPETLALAR EAARKSVVLL KNDNQVLPLR
AGGQRIALIG PLAQDWDSTK GPWTLFGGDD SSSDLASGLK QAMADPTQLS VVAGCGYQGP
LPGGIEDAVN AANAADVVIM AIGESRDHSG EARSRTSITV PQPQLDLLDA VAATGKPVVV
VLGNGRALAL GELLPKAQAV LVGWYLGSAS GLGLADVLFG AYGPSARLPV SFPRESGQVP
YYYDHKITGR PDPHPEKLSA FKTRYMTTPN AALFPFGFGL TYGRIEYGGL DIGDGRLTVE
GTLAIRATVH NRGTRAAEEV VQLYIHDRAA SITRPVQELK DFRKVALAPG ASTQVHFTLR
RADLLFIGQD LKPTVEPGTF DLWVAPSAEV DGLHATFELL A
//