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Database: UniProt
Entry: A0A0U5MJM8_9PROT
LinkDB: A0A0U5MJM8_9PROT
Original site: A0A0U5MJM8_9PROT 
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
//
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