ID   S3JZV6_9ENTR            Unreviewed;       753 AA.
AC   S3JZV6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF0201_01163 {ECO:0000313|EMBL:EPF18559.1};
OS   Cedecea davisae DSM 4568.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cedecea.
OX   NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF18559.1, ECO:0000313|Proteomes:UP000014585};
RN   [1] {ECO:0000313|EMBL:EPF18559.1, ECO:0000313|Proteomes:UP000014585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF18559.1,
RC   ECO:0000313|Proteomes:UP000014585};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2013) 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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EPF18559.1}.
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DR   EMBL; ATDT01000006; EPF18559.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3JZV6; -.
DR   STRING; 566551.HMPREF0201_01163; -.
DR   PATRIC; fig|566551.4.peg.1069; -.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   Proteomes; UP000014585; 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; IPR019800; Glyco_hydro_3_AS.
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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT   DOMAIN          673..742
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   753 AA;  82200 MW;  AACDA5ABAA476133 CRC64;
     MALQPALADE MFGPHPLTPE ARDAFVTGLL KKMTTDEKIG QLRLISVGPD NPKEAIREMI
     KDGQVGAIFN TVTRQDIRAM QDQVMQLSHL KIPLFFAYDV VHGQRTVFPI SLGLASSFNL
     DAVKTVGRIS AYEAADDGLN MTWAPMVDVS RDPRWGRVSE GFGEDTYLTA TMGRTMVEAM
     QGKSPADRYS VMTSVKHFAA YGAVEGGKEY NTVDMSPQRL FNDYMPPYKA ALDAGSGGVM
     VALNSLNGTP ASADSWLLKD LLRDEWKFKG ITISDHGAIK ELIKHGVASD PKDAVRIALN
     SGINMSMSDE YYSKYLPELV KSGAVPMKEL DDATRHVLNV KYDMGLFNDP YSHLGPKDSD
     PQDTNAESRL HRKEAREVAR ESMVLLKNRL QTLPLKKSAT VAVIGPLADS KRDAMGSWSA
     AGVAAQSVTP LEGIRNAVGQ QGKVVFAKGA NVTDEKDIVA FLNQYEPAVT VDPRTPKEMI
     DEAVNTAKSA DVVVAVVGEA QGMAHEASSR TDLTLPQSQR DLIAALKATG KPLVLVLMNG
     RPLALVKEDQ QADALLEAWY GGTEGGNAIA DVLFGDYNPS GKLPMSFPRS VGQIPTYYSH
     LNTGRPYNPE KPNKYTSRYF DEANGPLYPF GYGLSYTTFN VSDVKLSSPV MKRDGKVEAS
     VTVTNSGDRE GATVVQMYLQ DVTASMSRPV KELKGFKKVT LKAGESQTVS FPIDVNALKF
     WNAKMKYEAE PGKFNVFIGL DSARVKQGEF ELK
//