ID A0A1C4YUY6_9ACTN Unreviewed; 458 AA.
AC A0A1C4YUY6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=GA0074696_3724 {ECO:0000313|EMBL:SCF24466.1};
OS Micromonospora purpureochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47872 {ECO:0000313|EMBL:SCF24466.1, ECO:0000313|Proteomes:UP000198228};
RN [1] {ECO:0000313|EMBL:SCF24466.1, ECO:0000313|Proteomes:UP000198228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43821 {ECO:0000313|EMBL:SCF24466.1,
RC ECO:0000313|Proteomes:UP000198228};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|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; LT607410; SCF24466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4YUY6; -.
DR Proteomes; UP000198228; 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: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}.
FT ACT_SITE 167
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 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 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 407..408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 458 AA; 49914 MW; D6623977154F7619 CRC64;
MPDLSKLPPD FRWGVATSAY QIEGAVRADG RAPSIWDTFC EVPGAVDNGD TGAVACDHYH
RWPQDVALMR QLGVGAYRLS VAWPRVRPDG VGRVNPAGLD FYDRLVDAVL AAGIQPVVTL
YHWDLPQALQ DRGGWPERST AEAFADYAAV VAARLGDRVT DWCTVNEPLC VAWIGHLEGR
MAPGERDLTR AVRTAHHVLL GHGLATQAVR AHAARPASIG PVLNLSPCEP ASDRPADVAA
TRRMDGHVNR WWLDPLHGRG YPADMVATYG VEPPVRGDDL AVIATPSDFL GVNYYFRQVV
ADDPDGPPPY ARQVPVPGAT QTGMGWEAYP AGLEDLLVAV TEEYAPARIM VTESGAAWPD
RVTPEGTVED PERTAYLEGH LAACAAARER GVPLDGYFVW SLLDNFEWAY GYDKRFGLVH
VDYATQRRTV KASGLRYAEL IRAHQRLAGS SEAVPARG
//
