BGLA_THEMA
ID BGLA_THEMA Reviewed; 446 AA.
AC Q08638;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 126.
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;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=8277941; DOI=10.1007/bf00277355;
RA Liebl W., Gabelsberger J., Schleifer K.H.;
RT "Comparative amino acid sequence analysis of Thermotoga maritima beta-
RT glucosidase (BglA) deduced from the nucleotide sequence of the gene
RT indicates distant relationship between beta-glucosidases of the BGA family
RT and other families of beta-1,4-glycosyl hydrolases.";
RL Mol. Gen. Genet. 242:111-115(1994).
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 -!- CAUTION: As the DNA coding for this protein is not found in the
CC complete genome of T.maritima. It could have originated from another
CC bacterial species. {ECO:0000305}.
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DR EMBL; X74163; CAA52276.1; -; Genomic_DNA.
DR PIR; S41561; S34570.
DR RefSeq; WP_004082398.1; NZ_CP011107.1.
DR PDB; 1OD0; X-ray; 2.11 A; A/B=2-446.
DR PDB; 1OIF; X-ray; 2.12 A; A/B=2-446.
DR PDB; 1OIM; X-ray; 2.15 A; A/B=2-446.
DR PDB; 1OIN; X-ray; 2.15 A; A/B=2-446.
DR PDB; 1UZ1; X-ray; 2.00 A; A/B=2-446.
DR PDB; 1W3J; X-ray; 2.00 A; A/B=2-446.
DR PDB; 2CBU; X-ray; 1.85 A; A/B=2-446.
DR PDB; 2CBV; X-ray; 1.95 A; A/B=2-446.
DR PDB; 2CES; X-ray; 2.15 A; A/B=2-446.
DR PDB; 2CET; X-ray; 1.97 A; A/B=2-446.
DR PDB; 2J75; X-ray; 1.85 A; A/B=2-446.
DR PDB; 2J77; X-ray; 2.10 A; A/B=2-446.
DR PDB; 2J78; X-ray; 1.65 A; A/B=2-446.
DR PDB; 2J79; X-ray; 1.94 A; A/B=2-446.
DR PDB; 2J7B; X-ray; 1.87 A; A/B=2-446.
DR PDB; 2J7C; X-ray; 2.09 A; A/B=2-446.
DR PDB; 2J7D; X-ray; 2.24 A; A/B=2-446.
DR PDB; 2J7E; X-ray; 2.19 A; A/B=2-446.
DR PDB; 2J7F; X-ray; 2.28 A; A/B=2-446.
DR PDB; 2J7G; X-ray; 1.91 A; A/B=2-446.
DR PDB; 2J7H; X-ray; 1.95 A; A/B=2-446.
DR PDB; 2JAL; X-ray; 1.90 A; A/B=2-446.
DR PDB; 2VRJ; X-ray; 1.90 A; A/B=2-446.
DR PDB; 2WBG; X-ray; 1.85 A; A/B/C/D=2-446.
DR PDB; 2WC3; X-ray; 2.00 A; A/B/C/D=2-446.
DR PDB; 2WC4; X-ray; 1.70 A; A/B/C/D=2-446.
DR PDB; 4GXP; X-ray; 3.00 A; A/B/C=1-160, A/B/C=204-217, A/B/C=352-380, A/B/C=395-446.
DR PDB; 5N6S; X-ray; 2.10 A; A/B/C/D=2-446.
DR PDB; 5N6T; X-ray; 2.10 A; A/B=2-446.
DR PDB; 5OSS; X-ray; 1.70 A; A/B=2-446.
DR PDBsum; 1OD0; -.
DR PDBsum; 1OIF; -.
DR PDBsum; 1OIM; -.
DR PDBsum; 1OIN; -.
DR PDBsum; 1UZ1; -.
DR PDBsum; 1W3J; -.
DR PDBsum; 2CBU; -.
DR PDBsum; 2CBV; -.
DR PDBsum; 2CES; -.
DR PDBsum; 2CET; -.
DR PDBsum; 2J75; -.
DR PDBsum; 2J77; -.
DR PDBsum; 2J78; -.
DR PDBsum; 2J79; -.
DR PDBsum; 2J7B; -.
DR PDBsum; 2J7C; -.
DR PDBsum; 2J7D; -.
DR PDBsum; 2J7E; -.
DR PDBsum; 2J7F; -.
DR PDBsum; 2J7G; -.
DR PDBsum; 2J7H; -.
DR PDBsum; 2JAL; -.
DR PDBsum; 2VRJ; -.
DR PDBsum; 2WBG; -.
DR PDBsum; 2WC3; -.
DR PDBsum; 2WC4; -.
DR PDBsum; 4GXP; -.
DR PDBsum; 5N6S; -.
DR PDBsum; 5N6T; -.
DR PDBsum; 5OSS; -.
DR AlphaFoldDB; Q08638; -.
DR SMR; Q08638; -.
DR STRING; 243274.THEMA_04935; -.
DR DrugBank; DB08260; (1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide.
DR DrugBank; DB08090; (3Z,5S,6R,7S,8R,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol.
DR DrugBank; DB07370; (3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol.
DR DrugBank; DB07367; (3Z,5S,6R,7S,8S,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol.
DR DrugBank; DB04545; Afegostat.
DR DrugBank; DB04658; Calystegine B2.
DR DrugBank; DB03206; Duvoglustat.
DR DrugBank; DB03862; Tetrahydrooxazine.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; tmw:THMA_1897; -.
DR PATRIC; fig|243274.18.peg.955; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 654705at2; -.
DR UniPathway; UPA00696; -.
DR EvolutionaryTrace; Q08638; -.
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.
FT CHAIN 1..446
FT /note="Beta-glucosidase A"
FT /id="PRO_0000063879"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 351
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 95..110
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2J78"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:2J78"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 187..211
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 216..231
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 288..302
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5N6S"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2WC4"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 329..342
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 369..387
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:2J78"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:2J78"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2J78"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:2J78"
SQ SEQUENCE 446 AA; 51548 MW; 2E5B06E72BF84C01 CRC64;
MNVKKFPEGF LWGVATASYQ IEGSPLADGA GMSIWHTFSH TPGNVKNGDT GDVACDHYNR
WKEDIEIIEK LGVKAYRFSI SWPRILPEGT GRVNQKGLDF YNRIIDTLLE KGITPFVTIY
HWDLPFALQL KGGWANREIA DWFAEYSRVL FENFGDRVKN WITLNEPWVV AIVGHLYGVH
APGMRDIYVA FRAVHNLLRA HARAVKVFRE TVKDGKIGIV FNNGYFEPAS EKEEDIRAVR
FMHQFNNYPL FLNPIYRGDY PELVLEFARE YLPENYKDDM SEIQEKIDFV GLNYYSGHLV
KFDPDAPAKV SFVERDLPKT AMGWEIVPEG IYWILKKVKE EYNPPEVYIT ENGAAFDDVV
SEDGRVHDQN RIDYLKAHIG QAWKAIQEGV PLKGYFVWSL LDNFEWAEGY SKRFGIVYVD
YSTQKRIVKD SGYWYSNVVK NNGLED
