ID   BGLA_THENN              Reviewed;         444 AA.
AC   B9K7M5; O33843; O52505;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=1,4-beta-D-glucan glucohydrolase {ECO:0000303|PubMed:10960102};
DE            Short=Glucan glucohydrolase {ECO:0000303|PubMed:10960102};
DE            EC=3.2.1.74 {ECO:0000269|PubMed:10960102};
DE   AltName: Full=Beta-D-glucoside glucohydrolase;
DE   AltName: Full=Beta-glucosidase;
DE            EC=3.2.1.21 {ECO:0000269|PubMed:10960102};
DE   AltName: Full=Glucan 1,4-beta-glucosidase;
GN   Name=gghA {ECO:0000303|PubMed:10960102}; OrderedLocusNames=CTN_0782;
OS   Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=309803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RX   PubMed=10960102; DOI=10.1128/jb.182.18.5172-5179.2000;
RA   Yernool D.A., McCarthy J.K., Eveleigh D.E., Bok J.-D.;
RT   "Cloning and characterization of the glucooligosaccharide catabolic pathway
RT   beta-glucan glucohydrolase and cellobiose phosphorylase in the marine
RT   hyperthermophile Thermotoga neapolitana.";
RL   J. Bacteriol. 182:5172-5179(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA   Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA   Kim J.J., Park K.J., Lee S.Y.;
RT   "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT   neapolitana.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:10960102}.
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:0000269|PubMed:10960102};
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:0000269|PubMed:10960102};
CC   -!- ACTIVITY REGULATION: Activated by glucose up to 200 mM when p-
CC       nitrophenyl-beta-glucoside is used as the substrate. This activation by
CC       end product concentrations may be due to a transglycosylation activity
CC       of the enzyme. {ECO:0000269|PubMed:10960102}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=28.6 mM for cellobiose {ECO:0000269|PubMed:10960102};
CC         KM=4.55 mM for cellotriose {ECO:0000269|PubMed:10960102};
CC         KM=2.15 mM for cellotetraose {ECO:0000269|PubMed:10960102};
CC         Note=kcat is 285.0, 345.7 and 333.7 sec(-1) for the hydrolysis of
CC         cellobiose, cellotriose and cellotetraose, respectively.;
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:10960102};
CC       Temperature dependence:
CC         Optimum temperature is 95 degrees Celsius. Is highly thermostable,
CC         retaining 85% activity after incubation for 9 hours at 90 degrees
CC         Celsius and 88% activity after 1 hour at 95 degrees Celsius.
CC         {ECO:0000269|PubMed:10960102};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000303|PubMed:10960102}.
CC   -!- PATHWAY: Glycan metabolism; beta-D-glucan degradation.
CC       {ECO:0000303|PubMed:10960102}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10960102}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACM22958.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF039487; AAB95492.2; -; Genomic_DNA.
DR   EMBL; CP000916; ACM22958.1; ALT_INIT; Genomic_DNA.
DR   PDB; 5IDI; X-ray; 1.90 A; A/B=1-444.
DR   PDBsum; 5IDI; -.
DR   AlphaFoldDB; B9K7M5; -.
DR   SMR; B9K7M5; -.
DR   STRING; 309803.CTN_0782; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; tna:CTN_0782; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_0; -.
DR   BRENDA; 3.2.1.21; 6332.
DR   SABIO-RK; B9K7M5; -.
DR   UniPathway; UPA00350; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000445; Chromosome.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
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   NCBIfam; TIGR03356; BGL; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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   CHAIN           1..444
FT                   /note="1,4-beta-D-glucan glucohydrolase"
FT                   /id="PRO_0000372089"
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   CONFLICT        436
FT                   /note="V -> G (in Ref. 1; AAB95492)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..13
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           32..37
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   TURN            49..53
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           55..69
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           93..108
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           124..128
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           137..152
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           185..209
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          223..230
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           231..244
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           247..255
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           260..266
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           278..281
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          286..291
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           305..307
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          308..311
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           327..340
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          345..350
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   TURN            360..362
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           367..385
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          390..396
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           404..409
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          414..417
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   TURN            419..421
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:5IDI"
FT   HELIX           428..439
FT                   /evidence="ECO:0007829|PDB:5IDI"
SQ   SEQUENCE   444 AA;  51535 MW;  56A2D49A20A8CE01 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
     TQKRIIKDSG YWYSNVIKNN GLTD
//