BGLA_PAEPO
ID BGLA_PAEPO Reviewed; 448 AA.
AC P22073;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Beta-glucosidase A;
DE Short=BGA;
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=bglA;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC STRAIN=ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343
RC / NRRL B-4317 / VKM B-514;
RX PubMed=9466926; DOI=10.1006/jmbi.1997.1467;
RA Sanz-Aparicio J., Hermoso J.A., Martinez-Ripoll M., Lequerica J.L.,
RA Polaina J.;
RT "Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights
RT into the catalytic activity in family 1 glycosyl hydrolases.";
RL J. Mol. Biol. 275:491-502(1998).
CC -!- FUNCTION: BglA is intracellular and cleaves cellobiose probably through
CC inorganic phosphate mediated hydrolysis.
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 -!- SUBUNIT: Homooctamer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; M60210; AAA22263.1; -; Genomic_DNA.
DR PIR; JW0037; JW0037.
DR RefSeq; WP_019688628.1; NZ_UGSC01000001.1.
DR PDB; 1BGA; X-ray; 2.40 A; A/B/C/D=2-448.
DR PDB; 1BGG; X-ray; 2.30 A; A/B/C/D=1-448.
DR PDB; 1E4I; X-ray; 2.00 A; A=2-448.
DR PDB; 1TR1; X-ray; 2.20 A; A/B/C/D=2-448.
DR PDB; 1UYQ; X-ray; 2.20 A; A=2-448.
DR PDB; 6QWI; X-ray; 2.85 A; A/B=1-448.
DR PDB; 6R4K; X-ray; 2.13 A; A/B=1-448.
DR PDBsum; 1BGA; -.
DR PDBsum; 1BGG; -.
DR PDBsum; 1E4I; -.
DR PDBsum; 1TR1; -.
DR PDBsum; 1UYQ; -.
DR PDBsum; 6QWI; -.
DR PDBsum; 6R4K; -.
DR AlphaFoldDB; P22073; -.
DR SMR; P22073; -.
DR STRING; 1052684.PPM_4291; -.
DR DrugBank; DB02658; 2,4-Dinitrophenyl 2-Deoxy-2-Fluoro-Beta-D-Allopyranoside.
DR DrugBank; DB04282; 2-deoxy-2-fluoro-Alpha-D-glucose.
DR DrugBank; DB04304; L-Gluconic Acid.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR eggNOG; COG2723; Bacteria.
DR BRENDA; 3.2.1.21; 683.
DR EvolutionaryTrace; P22073; -.
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 A"
FT /id="PRO_0000063871"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:1E4I"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1BGG"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1E4I"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1TR1"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 187..211
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1E4I"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 369..387
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:1E4I"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1E4I"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:1E4I"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:1E4I"
SQ SEQUENCE 448 AA; 51649 MW; D971D2E61B6627C1 CRC64;
MTIFQFPQDF MWGTATAAYQ IEGAYQEDGR GLSIWDTFAH TPGKVFNGDN GNVACDSYHR
YEEDIRLMKE LGIRTYRFSV SWPRIFPNGD GEVNQEGLDY YHRVVDLLND NGIEPFCTLY
HWDLPQALQD AGGWGNRRTI QAFVQFAETM FREFHGKIQH WLTFNEPWCI AFLSNMLGVH
APGLTNLQTA IDVGHHLLVA HGLSVRRFRE LGTSGQIGIA PNVSWAVPYS TSEEDKAACA
RTISLHSDWF LQPIYQGSYP QFLVDWFAEQ GATVPIQDGD MDIIGEPIDM IGINYYSMSV
NRFNPEAGFL QSEEINMGLP VTDIGWPVES RGLYEVLHYL QKYGNIDIYI TENGACINDE
VVNGKVQDDR RISYMQQHLV QVHRTIHDGL HVKGYMAWSL LDNFEWAEGY NMRFGMIHVD
FRTQVRTPKE SYYWYRNVVS NNWLETRR
