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Database: UniProt
Entry: A0A196NEE4_9SPHN
LinkDB: A0A196NEE4_9SPHN
Original site: A0A196NEE4_9SPHN 
ID   A0A196NEE4_9SPHN        Unreviewed;       744 AA.
AC   A0A196NEE4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=A7X12_15015 {ECO:0000313|EMBL:OAN65733.1};
OS   Sphingomonas sp. TDK1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN65733.1, ECO:0000313|Proteomes:UP000078445};
RN   [1] {ECO:0000313|EMBL:OAN65733.1, ECO:0000313|Proteomes:UP000078445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TDK1 {ECO:0000313|EMBL:OAN65733.1,
RC   ECO:0000313|Proteomes:UP000078445};
RA   Takahashi S.;
RT   "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT   strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT   Bacteria.";
RL   Submitted (MAY-2016) 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   -!- 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:OAN65733.1}.
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DR   EMBL; LXVY01000006; OAN65733.1; -; Genomic_DNA.
DR   RefSeq; WP_064311052.1; NZ_LXVY01000006.1.
DR   AlphaFoldDB; A0A196NEE4; -.
DR   STRING; 453247.A7X12_15015; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000078445; Unassembled WGS sequence.
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:SF121; PERIPLASMIC 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..744
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008272824"
FT   DOMAIN          645..713
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   744 AA;  78448 MW;  539B32CFFAB1933F CRC64;
     MNRRNVLAAG AMLAASAWTP LARAARPLGA DTRARIQALL GQMTLAEKVG QMNQIAGGRQ
     KSLNSKLDAA MLDRVRKGEM GSFLHVAGAE PLRDLQRVAV EESRLKIPLL FAMDVIHGYR
     TILPVPLALA ASWDAQVAEQ AARIAAEEAW AAGLHWTFTP MVDVARDPRW GRVVEGAGED
     AYLGSRIAEA QVAGFQGADL GKGMRMMACA KHFVGYGAAE GGRDYDSAEV GPRTLNEVYL
     PPFHAAARAG AGSFMTAFNA LDGVPMTANA DLVRGFLRAR WHYQGLVVSD WNAIRELVNH
     GIAADAREAA VLALKAGVDM DMASGSYATY LAEAATADAR LVPLIDEAVG RILAAKARLG
     LFDNPYGFGD PARDKAPLRR TEARDLAKRS VVLLRNDGAV LPLKPGARLA LIGALADDAS
     SAIGSWRARG QATDAVTLKA ALAGADYQPG TDVPAAVEAA KRADVVLVAL GEDFNRTGEA
     RSYAEIGLPE GQAALLEALK AAGKPIVAIL MGGRPLALER ELAGVPAVLQ TWLLGIESGP
     AIAEILTGKA APGGRLPIGM PRRTGQSPQS YAHLPTGRPA NPDLAVDSAR YHDTEIGPLF
     AFGHGLTYGE IAYGPLTLSA ETLAPGGRIT ASVQVTHRGA MAVEDVVQLY ANDPVASVSR
     PVAELRGFAR VALKPGQSRI VRFTLTPEQF AFWRDGKWIV EPGDIRLMVG ASAADLKSEA
     KFRITAGGEG QMPAAAIATK VEIA
//
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