ID W5WHJ9_9PSEU Unreviewed; 460 AA.
AC W5WHJ9;
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_6985 {ECO:0000313|EMBL:AHI00343.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00343.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00343.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00343.1};
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; AHI00343.1; -; Genomic_DNA.
DR RefSeq; WP_025360198.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WHJ9; -.
DR STRING; 1449976.KALB_6985; -.
DR KEGG; kal:KALB_6985; -.
DR PATRIC; fig|1449976.3.peg.7014; -.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
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 365
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 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 419..420
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 460 AA; 50689 MW; A1DB2CA9822E1F90 CRC64;
MTTGTALRFP AGFLWGVATS SFQIEGATHE DGRGASIWDT FSATRGKVDG GGTGDPACDH
YHRYGEDVEL LADLGLAAYR FSVAWPRVQP DGRGPVERRG LDFYDRLLDR LLDKGIEPVA
TLYHWDLPQA LEDAGGWPNR DTAHRFAEYA ALVHARFADR VRMWTTLNEP WCSAFLGYCS
GIHAPGRQDP VAALKAAHHL LLGHGLAMRA LRAQAPSDHQ LSIVLNLSPV LAEDPSAGEA
VRKVDGLQNR FFLDPVFGRG YPADVLADTA WLGDWQRVVA DGDLDLIATP LDWYGINYYS
PVRVSLADEP LAVTPGNLPG LRGVRMLEPR GQLTGFGWEQ NADAFHTLLR RLGRDYPGVP
MIVTENGSAF PDLISPQGTV EDPERSGYLV DHLRAVHRAV DAGVDVRGYL AWSLLDNFEW
AAGYGQRFGL VHVDFETQRR TIKDSGRLFA RIAAENELPV
//
