ID Q1AUD7_RUBXD Unreviewed; 457 AA.
AC Q1AUD7;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=Rxyl_2046 {ECO:0000313|EMBL:ABG04991.1};
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04991.1, ECO:0000313|Proteomes:UP000006637};
RN [1] {ECO:0000313|EMBL:ABG04991.1, ECO:0000313|Proteomes:UP000006637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC {ECO:0000313|Proteomes:UP000006637};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG04991.1; -; Genomic_DNA.
DR RefSeq; WP_011565006.1; NC_008148.1.
DR AlphaFoldDB; Q1AUD7; -.
DR STRING; 266117.Rxyl_2046; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; rxy:Rxyl_2046; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_11; -.
DR OrthoDB; 9765195at2; -.
DR PhylomeDB; Q1AUD7; -.
DR Proteomes; UP000006637; 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:ABG04991.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ABG04991.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 362
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 416..417
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 457 AA; 50374 MW; 5C601E2882B5B49F CRC64;
MRFPEGFLWG AATAAYQVEG AVGEGGRGPS IWDTFSHTPG RVYRGDTGDV ACDHYHRLEE
DLDLMARFGL GAYRFSVAWP RIQPEGRGPA NRSGLDFYRR LVEGLGERGI EPVLTLYHWD
LPQALEDQGG WTSRQTSERF AEYAALVYEA LGGSVRFWIT LNEPWVSAWM GYGLGVHAPG
RRSTADALAA THHLLLGHGL ALEALRALGG GGRLGITLNL SPVRAASAEP ADAEAARRVD
GNANRLYLDP LFRGSYPQDM LEHYRGASDF SFVRDGDLQR ISAPVDFLGV NYYMRHTVRA
APGGGVRGPS TGMRFGELGA ETVLPEGVGT TAMGWPVEPD GLAEILVRVK EEYRDLPVFV
TENGCAVHDY IDPEGEVNDV ERVAYLDAHL RAAHAALERG VDLRGYMVWS LLDNFEWAEG
YSKRFGLVYV EYGSQRRVPK RSARWYAAVI RRGGPEG
//
