ID E6XES3_CELAD Unreviewed; 454 AA.
AC E6XES3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=Celal_0791 {ECO:0000313|EMBL:ADV48125.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV48125.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV48125.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(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}.
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DR EMBL; CP002453; ADV48125.1; -; Genomic_DNA.
DR RefSeq; WP_013549615.1; NC_014934.1.
DR AlphaFoldDB; E6XES3; -.
DR STRING; 688270.Celal_0791; -.
DR KEGG; cao:Celal_0791; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_1_0_10; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000008634; 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:ADV48125.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361175, ECO:0000313|EMBL:ADV48125.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001}.
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 365
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1,
FT ECO:0000256|PROSITE-ProRule:PRU10055"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 418..419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 454 AA; 52036 MW; 9D9F0116A7E1C18C CRC64;
MPKNKTSKKT KFTSKKFGED FVWGVSVAAY QIEGAHEKHD KSPSIWDTFT SKPGVIHKNE
TGDTACDFYH SYKEDILLMK AMNISNFRFS LSWSRILPKG IGDVSARGIQ FYNEVIDFCM
EHNIIPWVTL YHWDLPQVLQ DKGGWTNREI VSWFEYFTTV CATNFGDRVK HWMVLNEPMV
FTGAGHFLGV HAPGLKGLKN FLPAIHHAVL CQAAGGRILR ERVSGATIGT TFSCSYITPV
NKKKKNILAA EKADALLNRL FIEPSLGLGY PVAAAPILKK LKKYIQPGDL EDAVFDFDFI
GIQNYTREVV KHSYFIPYLS AKIVDAKNRN VQTTVMNWEV YPKSIYKMIK KFNAYEGVKK
IIITENGAAF EDNVANGFVN DIERRKFFKQ YLKQVYKAKE KGLKIDGYFV WTLMDNFEWA
EGYKPRFGLI HVNFETQERI VKSSGKWFAK FLKP
//
