ID M4S5C6_9SPHN Unreviewed; 796 AA.
AC M4S5C6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=G432_12110 {ECO:0000313|EMBL:AGH50143.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH50143.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH50143.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH50143.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
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};
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DR EMBL; CP004036; AGH50143.1; -; Genomic_DNA.
DR AlphaFoldDB; M4S5C6; -.
DR STRING; 745310.G432_12110; -.
DR KEGG; sphm:G432_12110; -.
DR PATRIC; fig|745310.14.peg.2514; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_004542_5_1_5; -.
DR Proteomes; UP000011816; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011816};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..796
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004057062"
FT DOMAIN 715..784
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 796 AA; 86035 MW; B994E38F38601D14 CRC64;
MRSSARLAML ACASAITAIG TPLVAPVIAA AQQAPARPIY KDASQPVEAR VEDLLKRMTL
EEKVAQIITV WEGKTAVFDD QLQLDPKKLP AVWPDGIGQF ARPSDARGAV SPRVVPGRDV
RQTIALVNAL QRWATTQTRL GIPILFHEEG LHGYAAVGAT SFPQAMALAS TWDPGLIRQI
NGVIAGEIRA RGVHLALSPV VDVARDPRWG RIEETFGEDP YLVGEMGVAA VQGLQGDTSA
DRLLPAGHVF ATLKHLTGHG QPESGTNVGP APISVRELRE NFFPPFEQVV RRTGIEAVMA
SYNEIDGVPS HANRWLLQDV LRGEWGFKGA IVSDYSAVDQ LMSLHHVSPD LEGAAIRALD
AGVDSDLPEG LSYKTLVKAV REGRVDEARV DVAVRRMLDL KFRAGLFENP YADVRQALAI
TNNDAARALA LKTAQQAITL LKNDGTLPLS LAAKPTIAVI GPNADVARLG GYYGQPPHSV
SILEGIRNRA GNRANILFAP GVKITENDDW WADEVKLADP AANRRMIAEA VEVAKKADRI
VLAIGDTEQT SREAWADNHI GDRPSLDLVG EQQALFDALK ALGKPITVIL INGRPASTVT
IAEQANALIE GWYLGEQGGN AVADVLFGTV NPGGKLPVTI PRNVGQLPMF YNHKPSAHRG
YLFDTTAPLF PFGWGLSYTS FDIGQPRLSA GTIRPDGDVD VLVDVANTGS RAGDETVQVY
VRDKVSSVTR PVKELKGFQR VTLQPGERRT VKIRLTPASF QMWNDRMERV VEPGEFDIMA
GPNSVDLKTV TLTVKP
//