ID A0A0U5MJM8_9PROT Unreviewed; 450 AA.
AC A0A0U5MJM8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=bglA3 {ECO:0000313|EMBL:CUW40112.1};
GN ORFNames=XM1_3051 {ECO:0000313|EMBL:CUW40112.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW40112.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-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|RuleBase:RU361175};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU361175}.
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DR EMBL; LN997848; CUW40112.1; -; Genomic_DNA.
DR RefSeq; WP_068434413.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5MJM8; -.
DR STRING; 1663591.XM1_3051; -.
DR KEGG; magx:XM1_3051; -.
DR PATRIC; fig|1663591.3.peg.3011; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000063191; Chromosome I.
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:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
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; LACTASE-LIKE PROTEIN; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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, ECO:0000313|EMBL:CUW40112.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:CUW40112.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 353
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 410..411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 450 AA; 50308 MW; EC9F8EC13D25B936 CRC64;
MGAGKKKQTS LRPDFVWGVS TSAFQVEGAT KEDGRGPSIW DTRCRLQGGV WTGANADVAC
DHYHRWPEDV GLIKDLGVDA YRFSIAWPRL LPKGKGQVNR KGLDFYDRLI DGVLEAGITP
WVCLYHWDLP QALDDLGGWT NRDCAGWFAD YAVLAAKRYG DRVKHFATFN EFSVFTMFGY
AIDWAAPGVT DRAAHMKAIH HVNLAHGMGV DVLRDHVPGV SIGAIHNRQI VRPEGGLAEN
QAAADLLDAH WNGVFCDPQH LGHYPEIMAR DVEPYVQAGD LARICRPTDW MGLNHYGPIY
AKADPATTWG YGWGAPPESA NHPEVGWPIF PEVFKDELLT LTRRYKLPVY VTENGCGGGA
GSDTPDENGV VNDTHRLAYF REYQQAMLDA VAEGADVRGY FVWALLDNFE WGSGYGPRFG
LYHVDFDSQK RTIKNSGKWY RDMIKGWRKG
//