BGLA_THENN
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 25-MAY-2022, entry version 65.
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; Thermotogae; Thermotogales; Thermotogaceae; 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 EnsemblBacteria; ACM22958; ACM22958; CTN_0782.
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 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 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
