ID E4N3R8_KITSK Unreviewed; 492 AA.
AC E4N3R8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=KSE_57760 {ECO:0000313|EMBL:BAJ31549.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ31549.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ31549.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
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|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU361175}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP010968; BAJ31549.1; -; Genomic_DNA.
DR RefSeq; WP_014138846.1; NC_016109.1.
DR AlphaFoldDB; E4N3R8; -.
DR STRING; 452652.KSE_57760; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ksk:KSE_57760; -.
DR PATRIC; fig|452652.3.peg.5786; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_11; -.
DR Proteomes; UP000007076; 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; 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:BAJ31549.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:BAJ31549.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000007076}.
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 397
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 451..452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 492 AA; 53429 MW; 94A923962088D548 CRC64;
MTTASSADQP VVASAAESES AVGTAAQPAR FPAGFVWGAA TAAYQIEGAA DQDGRTPSIW
DTFARRPGAV RNGDTGDIAA DHYHRYRDDV ALMSELGLRA YRFSLSWPRV RPGGRGPANE
AGLDFYDRLV DELLGAGITP VATLYHWDLP QELEDEGGWT NRDTAYRFAE YASLAAGRLG
DRVPTWTTLN EPWCSAFLGY GNGVHAPGRT DHAAALAAHH HLLLAHGLGT AALRAELPDT
AQVSLTLNLA AVRPLSTDAA DLDAARRIDG LANRIFLDPV FRGSYPEDVL ADTAHVTDWS
FVRDGDLAEI SRPIDSLGIN YYTPTVVAAE RPEADGTAPR GDGHQGDSPW PADHGIRFLP
APGTRTAMGW PVDADGLYEL LTRLRDDLPG VPLLVTENGA AYEDYTDPSG AVHDPERIDY
LHTHLAAVHR AIADGAPVRG YFLWSLLDNY EWAYGYSKRF GIVHVDFASQ RRTPKDSAHW
YARVIRDGAL PQ
//
