ID A0A1W2AH24_9SPHI Unreviewed; 452 AA.
AC A0A1W2AH24;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN ORFNames=SAMN04488524_1412 {ECO:0000313|EMBL:SMC59986.1};
OS Pedobacter africanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=151894 {ECO:0000313|EMBL:SMC59986.1, ECO:0000313|Proteomes:UP000192756};
RN [1] {ECO:0000313|Proteomes:UP000192756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12126 {ECO:0000313|Proteomes:UP000192756};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FWXT01000001; SMC59986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2AH24; -.
DR STRING; 151894.SAMN04488524_1412; -.
DR Proteomes; UP000192756; 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: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; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000192756}.
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 363
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 303
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 452 AA; 51596 MW; DD5895A8A81BA12E CRC64;
MPAIEKNMIK ASDFGSDFIW GVATAAAQVE GAAEAYGKGL SIWDTFSKRQ GKIKKGHLPT
TACDFYHSYK ADVELVKLLG FKVFRFSISW PRILPDGKGR VNKEGILFYH QLIDECLRQG
IVPYVTLYHW DLPHALEEEG GWTAFSINNS FNHFVSVCAK EYGDKVKNWI VLNEPFGFTS
LGYMLGVHAP GKTGLTNFFS AVHHTAIAQA DGGRILRAEV KEANIGTSFS CSEIIPHTHS
EADLLAAKRV DCLMNRLFIE PALGMGYPTA GWEVMERFSI QHSTWRHTER LTFDFDFIGI
QNYFPLTIKY NAFIPVVQAW EVKAKNRKKP HTAMGWEINP DSFYNIIRQF ATYPNIPQLM
ITENGAAYHD KLNNYQVHDQ ERIAYFQQYL AALLKAKREG LNIAGYMAWT LMDNFEWAEG
YNARFGLVYT DFKTQQRTVK DSGLWFQDFL NH
//
