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Database: UniProt
Entry: A0A0Q9KWX0_9MICO
LinkDB: A0A0Q9KWX0_9MICO
Original site: A0A0Q9KWX0_9MICO 
ID   A0A0Q9KWX0_9MICO        Unreviewed;       456 AA.
AC   A0A0Q9KWX0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=ASG74_06890 {ECO:0000313|EMBL:KRE42175.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE42175.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE42175.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE42175.1,
RC   ECO:0000313|Proteomes:UP000051965};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRE42175.1}.
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DR   EMBL; LMSA01000002; KRE42175.1; -; Genomic_DNA.
DR   RefSeq; WP_056140643.1; NZ_LMSA01000002.1.
DR   AlphaFoldDB; A0A0Q9KWX0; -.
DR   STRING; 1736394.ASG74_06890; -.
DR   Proteomes; UP000051965; Unassembled WGS sequence.
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};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT   ACT_SITE        167
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         416..417
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   456 AA;  50240 MW;  36696D1F69DB0AC1 CRC64;
     MTFETTFPDS FLWGAATASY QIEGAVAEDG RLPSIWDTFC AEPGKVLGGE SGEVACDHYH
     RMPQDVALMK ELGLDAYRFS IAWPRVIPTG TGAVNTKGLD FYSRLVDTLL DRGIRPFVTL
     YHWDLPQALG DQGGWLNRDI KDWFAEYTGA VVGALGDRVK NWTTLNEPWC SSLLSYSLGH
     HAPGHTDRVE GLVSAHHLML AHGTAVPVIR EACPDAEVSI TLNPTQVIGP DDPTDADLDA
     MQRADDVLNG IFFGPLFHGA YPPTLLENTA HLTDHAYIHD GDLEVMSAPL DNLGVNNYFP
     TRVKHTDGAT HPLPGGEGVE ETEPHPPLTA MGWEINADAH HDILMRSSQE SGLPIYVTEN
     GSAWPDVIET GPEGESVHDV DRTAYLHGHL DAVKRAIDDG ADVRGYFAWS LMDNFEWAFG
     YSKRFGIVYV DYDTQERTVK DSGKEYARII AAHRTD
//
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