ID   BGLA_THENE              Reviewed;         425 AA.
AC   P0C946; O33843; O52505;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=1,4-beta-D-glucan glucohydrolase {ECO:0000250|UniProtKB:B9K7M5};
DE            Short=Glucan glucohydrolase {ECO:0000250|UniProtKB:B9K7M5};
DE            EC=3.2.1.74 {ECO:0000250|UniProtKB:B9K7M5};
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Beta-glucosidase;
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:B9K7M5};
DE   AltName: Full=Glucan 1,4-beta-glucosidase;
DE   Flags: Fragment;
GN   Name=bglA; Synonyms=gghA;
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=2337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Z2706-MC24;
RX   PubMed=8352795; DOI=10.1006/bbrc.1993.1974;
RA   Dakhova O., Kurepina N., Zverlov V., Svetlichnyi V., Velikodvorskaya G.;
RT   "Cloning and expression in Escherichia coli of Thermotoga neapolitana genes
RT   coding for enzymes of carbohydrate substrate degradation.";
RL   Biochem. Biophys. Res. Commun. 194:1359-1364(1993).
CC   -!- FUNCTION: Broad substrate specificity glycosidase. Releases glucose
CC       from soluble glucooligomers, with a preference for longer oligomers;
CC       acts more readily on cellotetraose than on cellobiose. Displays similar
CC       activities towards the disaccharides lactose and cellobiose. Is also
CC       able to hydrolyze various aryl-beta-glycosides in vitro.
CC       {ECO:0000250|UniProtKB:B9K7M5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-linkages in (1->4)-beta-D-glucans, to
CC         remove successive glucose units.; EC=3.2.1.74;
CC         Evidence={ECO:0000250|UniProtKB:B9K7M5};
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         Evidence={ECO:0000250|UniProtKB:B9K7M5};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000250|UniProtKB:B9K7M5}.
CC   -!- PATHWAY: Glycan metabolism; beta-D-glucan degradation.
CC       {ECO:0000250|UniProtKB:B9K7M5}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:B9K7M5}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; Z97212; CAB10165.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C946; -.
DR   SMR; P0C946; -.
DR   UniPathway; UPA00350; -.
DR   UniPathway; UPA00696; -.
DR   GO; GO:0031217; F:glucan 1,4-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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..425
FT                   /note="1,4-beta-D-glucan glucohydrolase"
FT                   /id="PRO_0000063880"
FT   ACT_SITE        164
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   NON_TER         425
SQ   SEQUENCE   425 AA;  49366 MW;  E66E33B75266187B CRC64;
     MKKFPEGFLW GVATASYQIE GSPLADGAGM SIWHTFSHTP GNVKNGDTGD VACDHYNRWK
     EDIEIIEKIG AKAYRFSISW PRILPEGTGK VNQKGLDFYN RIIDTLLEKN ITPFITIYHW
     DLPFSLQLKG GWANRDIADW FAEYSRVLFE NFGDRVKHWI TLNEPWVVAI VGHLYGVHAP
     GMKDIYVAFH TVHNLLRAHA KSVKVFRETV KDGKIGIVFN NGYFEPASER EEDIRAARFM
     HQFNNYPLFL NPIYRGEYPD LVLEFAREYL PRNYEDDMEE IKQEIDFVGL NYYSGHMVKY
     DPNSPARVSF VERNLPKTAM GWEIVPEGIY WILKGVKEEY NPQEVYITEN GAAFDDVVSE
     GGKVHDQNRI DYLRAHIEQV WRAIQDGVPL KGYFVWSLLD NFEWAEGYSK RFGIVYVDYN
     TQKRI