ID A0A0B8T902_9SPHI Unreviewed; 446 AA.
AC A0A0B8T902;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=DI53_1489 {ECO:0000313|EMBL:KGE14460.1};
OS Sphingobacterium deserti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE14460.1, ECO:0000313|Proteomes:UP000031802};
RN [1] {ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA Zhang W.;
RT "Whole-Genome optical mapping and complete genome sequence of
RT Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT west of China.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGE14460.1, ECO:0000313|Proteomes:UP000031802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX PubMed=25830331;
RA Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA Zhang W., Lin M.;
RT "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT Desert of China.";
RL PLoS ONE 10:E0122254-E0122254(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGE14460.1}.
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DR EMBL; JJMU01000024; KGE14460.1; -; Genomic_DNA.
DR RefSeq; WP_037497212.1; NZ_JJMU01000024.1.
DR AlphaFoldDB; A0A0B8T902; -.
DR STRING; 1229276.DI53_1489; -.
DR PATRIC; fig|1229276.3.peg.1541; -.
DR eggNOG; COG2723; Bacteria.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000031802; Unassembled WGS sequence.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU361175};
KW Reference proteome {ECO:0000313|Proteomes:UP000031802}.
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 356
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 22
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 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 409..410
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 446 AA; 51634 MW; C7F2EA1E5282D46B CRC64;
MQLTKEAFGN DFVWGVSTAA YQIEGAHQHE GKGSSIWDVF VQKKNKIFQN HKGDIACDFY
NRYVEDLHLM HRMHIKNYRF SIGWSRIIPD GTGEINKKGI DFYNRLIDLS LELGITPWIT
LYHWDLPYAL ELRGGWVNRE VKDWFGDYVG ICVKHFGDRV KNWMVLNEPT VFSAAGYFFG
VHAPGKTGLE NFLATAHHAS LAQAYGGKII KSLQQDSRVG TTFSCSYVEP FSARDKDVRA
AKKADVLLNR LFIEPLLGLG YPTTEIKALK RIERYMQQHD EADLRFDMDF IGLQNYTREV
IRYSMFVPYL QAKIVTAKER KVPMTAMNWE VYPESIYHIL KKFSAYKNIP PLMITENGAA
FPDQVLGGEV HDPQRLSYLQ DALQQVHRAK QEGVQVDGYF VWTFLDNFEW AEGYYPRFGL
VHVDFQSQER IVKSSGHWYA DFLQDE
//
