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Database: UniProt
Entry: C7QYM5_JONDD
LinkDB: C7QYM5_JONDD
Original site: C7QYM5_JONDD 
ID   C7QYM5_JONDD            Unreviewed;       749 AA.
AC   C7QYM5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   OrderedLocusNames=Jden_0198 {ECO:0000313|EMBL:ACV07872.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV07872.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV07872.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
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; CP001706; ACV07872.1; -; Genomic_DNA.
DR   RefSeq; WP_015770501.1; NC_013174.1.
DR   AlphaFoldDB; C7QYM5; -.
DR   STRING; 471856.Jden_0198; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   KEGG; jde:Jden_0198; -.
DR   eggNOG; COG1472; Bacteria.
DR   HOGENOM; CLU_004542_5_1_11; -.
DR   OrthoDB; 3187421at2; -.
DR   Proteomes; UP000000628; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACV07872.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000628}.
FT   DOMAIN          667..736
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   749 AA;  81330 MW;  D2039AF885E2DD19 CRC64;
     MTTPLPYRDP TLPIQQRVTD LLSRMSREEK VGQMMQLDAR DNLDHLINTV HVGSILHTSP
     DALREAHTLV ERTPLGIPLL VGEDCIHGHS FFEGTTIFPT QLGMAASWNA PLIEQAARVT
     AVEASATGIH WTFSPVLCIA RDLRWGRVNE TFGEDPHLIG ELASAMVRGY QGDGLTDHTA
     ILATAKHFAA YSETQGGRDA SEADVSQRKM RSWFLPPFER VAREGCRTFM LGYQTTDGVP
     ITINSWLLDD VLRGEWGYTG MLITDWDNVG RMVWEQQVMP DHTHAAAAAV KAGNDMVMTT
     PQFFDGALRA LDQGLLTDAD VDAAVSRILT VKFELGLFEN PRRPNPERIA TALATPDHTA
     INRDLTRRSL VLLANDGTLP LDATLEVSKK IAVIGPNAND HQYQLGDWAG NSGQAGWMPD
     GHLTNQITTV YEGLRDIVPD TWTVTHARGA NIVDLVDDPA GTHFPDGQPR PRIAQPAPID
     EALHNEALAA ANNADYIVAV VGDAIPLVGE GRSTATLNLL GGQEQLLNDL AATGKPLIVV
     LLASKPLVLP PSALNANAII WAANPGMRGG QALAELITGA IEPAGRLPIS FARHVGQQPT
     YYNQIRGQHG DRYADLTQDP QWAFGFGLSY TTVEYSELVL DRTVLGAGDT VTAHITVTNT
     GQRPAVETVQ AYVSDLVTSV SWADKELKAF TQVEVQPGQS VTATVQVPVA DCTIVDARGR
     RVVEPGEFEL LVGPSSRDED LHRAKFIVQ
//
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