BGLB_PAEPO
ID BGLB_PAEPO Reviewed; 448 AA.
AC P22505;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Beta-glucosidase B;
DE EC=3.2.1.21;
DE AltName: Full=Amygdalase;
DE AltName: Full=Beta-D-glucoside glucohydrolase;
DE AltName: Full=Cellobiase;
DE AltName: Full=Gentiobiase;
GN Name=bglB;
OS Paenibacillus polymyxa (Bacillus polymyxa).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2123813; DOI=10.1016/0378-1119(90)90410-s;
RA Gonzalez-Candelas L., Ramon D., Polaina J.;
RT "Sequences and homology analysis of two genes encoding beta-glucosidases
RT from Bacillus polymyxa.";
RL Gene 95:31-38(1990).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; M60211; AAA22264.1; -; Genomic_DNA.
DR PIR; JW0038; JW0038.
DR PDB; 2JIE; X-ray; 2.30 A; A=2-448.
DR PDB; 2O9P; X-ray; 2.10 A; A=2-448.
DR PDB; 2O9R; X-ray; 2.30 A; A=4-448.
DR PDB; 2O9T; X-ray; 2.15 A; A=2-448.
DR PDB; 2Z1S; X-ray; 2.46 A; A=2-448.
DR PDBsum; 2JIE; -.
DR PDBsum; 2O9P; -.
DR PDBsum; 2O9R; -.
DR PDBsum; 2O9T; -.
DR PDBsum; 2Z1S; -.
DR AlphaFoldDB; P22505; -.
DR SMR; P22505; -.
DR STRING; 1052684.PPM_3914; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR eggNOG; COG2723; Bacteria.
DR EvolutionaryTrace; P22505; -.
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 InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR03356; BGL; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation.
FT CHAIN 1..448
FT /note="Beta-glucosidase B"
FT /id="PRO_0000063872"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:2O9P"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 96..112
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 188..211
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:2O9P"
FT TURN 345..349
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:2O9P"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2O9P"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2O9P"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2O9P"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:2O9P"
SQ SEQUENCE 448 AA; 51573 MW; 628F44507C21EF1F CRC64;
MSENTFIFPA TFMWGTSTSS YQIEGGTDEG GRTPSIWDTF CQIPGKVIGG DCGDVACDHF
HHFKEDVQLM KQLGFLHYRF SVAWPRIMPA AGIINEEGLL FYEHLLDEIE LAGLIPMLTL
YHWDLPQWIE DEGGWTQRET IQHFKTYASV IMDRFGERIN WWNTINEPYC ASILGYGTGE
HAPGHENWRE AFTAAHHILM CHGIASNLHK EKGLTGKIGI TLNMEHVDAA SERPEDVAAA
IRRDGFINRW FAEPLFNGKY PEDMVEWYGT YLNGLDFVQP GDMELIQQPG DFLGINYYTR
SIIRSTNDAS LLQVEQVHME EPVTDMGWEI HPESFYKLLT RIEKDFSKGL PILITENGAA
MRDELVNGQI EDTGRHGYIE EHLKACHRFI EEGGQLKGYF VWSFLDNFEW AWGYSKRFGI
VHINYETQER TPKQSALWFK QMMAKNGF
