BGLA_NIACI
ID BGLA_NIACI Reviewed; 450 AA.
AC Q03506;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Beta-glucosidase;
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 Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29.
RC STRAIN=ATCC 21783 / subsp. Alkalophilus;
RX PubMed=8481013; DOI=10.1128/aem.59.3.927-932.1993;
RA Paavilainen S.K., Hellman J., Korpela T.;
RT "Purification, characterization, gene cloning, and sequencing of a new
RT beta-glucosidase from Bacillus circulans subsp. alkalophilus.";
RL Appl. Environ. Microbiol. 59:927-932(1993).
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; M96979; AAA22266.1; -; Genomic_DNA.
DR PIR; A48969; A48969.
DR PDB; 1QOX; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-450.
DR PDBsum; 1QOX; -.
DR AlphaFoldDB; Q03506; -.
DR SMR; Q03506; -.
DR MINT; Q03506; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR EvolutionaryTrace; Q03506; -.
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;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8481013"
FT CHAIN 2..450
FT /note="Beta-glucosidase"
FT /id="PRO_0000063870"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 187..210
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 373..391
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:1QOX"
FT TURN 425..428
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1QOX"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:1QOX"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:1QOX"
SQ SEQUENCE 450 AA; 51303 MW; C52C1DB233B72790 CRC64;
MSIHMFPSDF KWGVATAAYQ IEGAYNEDGR GMSIWDTFAH TPGKVKNGDN GNVACDSYHR
VEEDVQLLKD LGVKVYRFSI SWPRVLPQGT GEVNRAGLDY YHRLVDELLA NGIEPFCTLY
HWDLPQALQD QGGWGSRITI DAFAEYAELM FKELGGKIKQ WITFNEPWCM AFLSNYLGVH
APGNKDLQLA IDVSHHLLVA HGRAVTLFRE LGISGEIGIA PNTSWAVPYR RTKEDMEACL
RVNGWSGDWY LDPIYFGEYP KFMLDWYENL GYKPPIVDGD MELIHQPIDF IGINYYTSSM
NRYNPGEAGG MLSSEAISMG APKTDIGWEI YAEGLYDLLR YTADKYGNPT LYITENGACY
NDGLSLDGRI HDQRRIDYLA MHLIQASRAI EDGINLKGYM EWSLMDNFEW AEGYGMRFGL
VHVDYDTLVR TPKDSFYWYK GVISRGWLDL
