ID W5VYM2_9PSEU Unreviewed; 437 AA.
AC W5VYM2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=KALB_34 {ECO:0000313|EMBL:AHH93411.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93411.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH93411.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93411.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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|RuleBase:RU361175}.
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DR EMBL; CP007155; AHH93411.1; -; Genomic_DNA.
DR RefSeq; WP_025353702.1; NZ_CP007155.1.
DR AlphaFoldDB; W5VYM2; -.
DR STRING; 1449976.KALB_34; -.
DR KEGG; kal:KALB_34; -.
DR PATRIC; fig|1449976.3.peg.36; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_11; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000019225; 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; 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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:AHH93411.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:AHH93411.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225}.
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 399..400
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 437 AA; 47764 MW; A6AFEF7681E39DE4 CRC64;
MTEPALPSFP DGFLWGVSTS AYQVEGAVSE GGRGRSTWDT FCATPDRVYS GHTGEVACDH
YHRYPEDIAL MSQLGVDAYR FSIAWPRIQP EGTGPANAEG LGFYDRLVDA LCEAGIAPAA
TLYHWDTPQP VEDAGGWLSR DTAKHFADYA ALVGERLADR VAMWIPLNEP MVTTVYGYGI
GQYAPGQFLL LDSVPTAHHQ NLAHGLAVQA LRAAGARQIG TANNHGPIWS ATDSAADRAA
ADYASDLLNW LFADPVLAGS YPEQLHPLLP TGFAEDLPTI AAPLDLYGVN YYEPTQVSAP
SEGNPLPFDL GAVEGYPMTT NGSPVVPDGF RQFLLELRDR HGSALPPVYI TENGCSYDGV
DDQQRIEFLD GHLRALHAAM QQGVDVRGYF VWSLLDNFEW SKGYQPRFGL VDVDYTTQCR
TPKSSFHWYR ALIGGTR
//
