BGLA_ACET2
ID BGLA_ACET2 Reviewed; 448 AA.
AC P26208; A3DBX4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Beta-glucosidase A;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase;
DE AltName: Full=Cellobiase;
DE AltName: Full=Gentiobiase;
GN Name=bglA; OrderedLocusNames=Cthe_0212;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1909624; DOI=10.1111/j.1432-1033.1991.tb16186.x;
RA Graebnitz F., Seiss M., Ruecknagel K.P., Staudenbauer W.L.;
RT "Structure of the beta-glucosidase gene bglA of Clostridium thermocellum.
RT Sequence analysis reveals a superfamily of cellulases and beta-glycosidases
RT including human lactase/phlorizin hydrolase.";
RL Eur. J. Biochem. 200:301-309(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 3-448.
RA Salama-Alber O., Bayer E.;
RT "Crystal structure of Ruminiclostridium Thermocellum beta-Glucosidase A.";
RL Submitted (JUL-2017) to the PDB data bank.
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN51453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X60268; CAA42814.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN51453.1; ALT_INIT; Genomic_DNA.
DR PIR; S17215; S17215.
DR PDB; 5OGZ; X-ray; 1.60 A; A/B=3-448.
DR PDBsum; 5OGZ; -.
DR AlphaFoldDB; P26208; -.
DR SMR; P26208; -.
DR STRING; 203119.Cthe_0212; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR DNASU; 4808630; -.
DR EnsemblBacteria; ABN51453; ABN51453; Cthe_0212.
DR KEGG; cth:Cthe_0212; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_9; -.
DR OMA; VEQWITL; -.
DR BRENDA; 3.2.1.21; 1530.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002145; Chromosome.
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-UniPathway.
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; Reference proteome.
FT CHAIN 1..448
FT /note="Beta-glucosidase A"
FT /id="PRO_0000063876"
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:5OGZ"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5OGZ"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 138..154
FT /evidence="ECO:0007829|PDB:5OGZ"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 187..210
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 373..391
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:5OGZ"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:5OGZ"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5OGZ"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:5OGZ"
SQ SEQUENCE 448 AA; 51482 MW; D59B9EB7BEE67621 CRC64;
MSKITFPKDF IWGSATAAYQ IEGAYNEDGK GESIWDRFSH TPGNIADGHT GDVACDHYHR
YEEDIKIMKE IGIKSYRFSI SWPRIFPEGT GKLNQKGLDF YKRLTNLLLE NGIMPAITLY
HWDLPQKLQD KGGWKNRDTT DYFTEYSEVI FKNLGDIVPI WFTHNEPGVV SLLGHFLGIH
APGIKDLRTS LEVSHNLLLS HGKAVKLFRE MNIDAQIGIA LNLSYHYPAS EKAEDIEAAE
LSFSLAGRWY LDPVLKGRYP ENALKLYKKK GIELSFPEDD LKLISQPIDF IAFNNYSSEF
IKYDPSSESG FSPANSILEK FEKTDMGWII YPEGLYDLLM LLDRDYGKPN IVISENGAAF
KDEIGSNGKI EDTKRIQYLK DYLTQAHRAI QDGVNLKAYY LWSLLDNFEW AYGYNKRFGI
VHVNFDTLER KIKDSGYWYK EVIKNNGF
