ID A0A0G3X6P8_9SPHN Unreviewed; 457 AA.
AC A0A0G3X6P8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN ORFNames=AM2010_217 {ECO:0000313|EMBL:AKM06306.1};
OS Pelagerythrobacter marensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Pelagerythrobacter.
OX NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM06306.1, ECO:0000313|Proteomes:UP000037643};
RN [1] {ECO:0000313|EMBL:AKM06306.1, ECO:0000313|Proteomes:UP000037643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM06306.1,
RC ECO:0000313|Proteomes:UP000037643};
RA Kim K.M.;
RL Submitted (JUN-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 ECO:0000256|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
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DR EMBL; CP011805; AKM06306.1; -; Genomic_DNA.
DR RefSeq; WP_047805506.1; NZ_LMVG01000002.1.
DR AlphaFoldDB; A0A0G3X6P8; -.
DR STRING; 543877.AM2010_217; -.
DR KEGG; amx:AM2010_217; -.
DR PATRIC; fig|543877.4.peg.218; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000037643; Chromosome.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR03356; BGL; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000037643}.
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 406..407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 457 AA; 50774 MW; D05511218E674237 CRC64;
MSGAFPEGFL WGAATAAYQV EGSPLADGAG TSIWHRFTHD PRLMIASGDT GDVACDHYNR
MESDVDLMKR LGLQAYRFSI SWSRILPGGT GRVNQAGLDF YRRLVDRLND AGIMPLPTLY
HWDLPAALDD RGGWLNRDIA EWFGEYAAVM YRALDGEVRR WATLNEPWVV ADGGYLNGVL
APGHRSIFEC AIASRNLMRA HGRAVQVYRE LGRHEVGVVF NIEPKYPASD SAEDLAATAR
ADAYMNRQYA DPALLGTCPP ELREVYGEAW EDWSQDDLAL ACQPVDFVGI NYYTRSVVRA
SDTAWPFYAE PVVQEGAQHT ETDWEVFPEA MTRTLLWFRE RYGDIPLYIM ENGAAFADPA
SSAGALIADD HRCRYLADHI AAVGDAIAAG VDVRGYMVWS LFDNLEWALG YAKRFGIVHV
DYETLERTPK KSADLYRRII ESNGTAVAGA ATEDAAS
//
