ID I3ZLC5_TERRK Unreviewed; 484 AA.
AC I3ZLC5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Terro_3834 {ECO:0000313|EMBL:AFL90043.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL90043.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL90043.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) 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; CP003379; AFL90043.1; -; Genomic_DNA.
DR RefSeq; WP_014787303.1; NC_018014.1.
DR AlphaFoldDB; I3ZLC5; -.
DR STRING; 926566.Terro_3834; -.
DR KEGG; trs:Terro_3834; -.
DR PATRIC; fig|926566.3.peg.3773; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_3_0; -.
DR OrthoDB; 2339329at2; -.
DR Proteomes; UP000006056; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361175};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..484
FT /note="Beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003684121"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 445..446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 484 AA; 53521 MW; 8DBD908B30918D43 CRC64;
MPYRISRRTF GQLAGSLVTA AALPFRMFAA PSVSRATATG DRRFPAGFLW GSATASYQVE
GAVNEDGRGK TVWDTFSHTA GKTHNGDTGD VSTDSYHRYA EDIALMKDLG LKTCRFSVAW
SRIFPDGAGQ PNPKGIDHYR KFCQALRAAG IEPWCTLYHW DLPQALEDKG GWQNRETAKL
FADYAGYTAG KLADVCSHFM TMNEISTFVE LGYGNGIHAP GLKLSRGKLA QVRHHAVLAH
GLAVQAIRAA APHVKVGSAE NLTAVVPVFD SPEHVAAAKK ATVEENAGYL TVMRTGRYTD
QYLQTLGADA PEFTQEEMKA IGSPLDFQGL NIYTATYARA VKNAKGYDIV GNPASYPHME
SPWLTVGPDA LYWAPRLANE CWDLKEIYIT ENGCSSADVV AGDGHIYDTD RVMYLRNYLT
HLQRATSEGV PVKGYFLWSL LDNFEWADGY DKRFGITYVD FKTQKRTPKL SSEFYRNLIA
RNSL
//
