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Database: UniProt
Entry: D1A1R2_THECD
LinkDB: D1A1R2_THECD
Original site: D1A1R2_THECD 
ID   D1A1R2_THECD            Unreviewed;       471 AA.
AC   D1A1R2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN   OrderedLocusNames=Tcur_2184 {ECO:0000313|EMBL:ACY97750.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY97750.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY97750.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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:0000256|ARBA:ARBA00000448,
CC         ECO:0000256|RuleBase:RU361175};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU361175}.
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DR   EMBL; CP001738; ACY97750.1; -; Genomic_DNA.
DR   RefSeq; WP_012852534.1; NC_013510.1.
DR   AlphaFoldDB; D1A1R2; -.
DR   STRING; 471852.Tcur_2184; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; tcu:Tcur_2184; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_1_3_11; -.
DR   OrthoDB; 5166882at2; -.
DR   Proteomes; UP000001918; 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-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
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; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ACY97750.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ACY97750.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918}.
FT   ACT_SITE        168
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        371
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         425..426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   471 AA;  51869 MW;  926241624C94294B CRC64;
     MTDHDLPTGF PPGFLWGAAT SAYQIEGGVD ADGRVPSIWD TYSHTPGRVR DGDTGDVACD
     HYHRWAEDVA IMAELGLNAY RFSIAWPRIM PGGRFNPKGA DFYSRLVDAL LERGIAPVAT
     LYHWDLPQEL EDAGGWPARQ TAFRFAEYAE AIGRVLGDRV HIWTTLNEPW CSAFLGYCSG
     SHAPGRTDPA AALAAAHHLN LAHGLAVRAL RRAAPGARCS VTLNLHHARG ASAADADAVR
     RVDAVANRIF LGPMLTGRYP ADLIDDTASI TDWAFVHPGD EQTIAAPLDV LGVNYYAPVL
     VRRWDGSAPR QSADGHRPGS RSAFPGCEEV EFLPMPGPRT AMGWPIDPAG LTELLMRLHR
     DHPGVPLMIT ENGAAFEEEA DADGRVHDAR RIGYLRDHLA AAKAAMDAGA DLRGYFVWSL
     MDNFEWARGY SKRFGIVRVD YRTQRRTWKD SAHWYRRVIA ANARSHQAPR P
//
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