ID   G9ZA23_9ENTR            Unreviewed;       765 AA.
AC   G9ZA23;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF0880_04382 {ECO:0000313|EMBL:EHM45033.1};
OS   Yokenella regensburgei ATCC 43003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Yokenella.
OX   NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM45033.1, ECO:0000313|Proteomes:UP000003044};
RN   [1] {ECO:0000313|EMBL:EHM45033.1, ECO:0000313|Proteomes:UP000003044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM45033.1,
RC   ECO:0000313|Proteomes:UP000003044};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:EHM45033.1}.
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DR   EMBL; AGCL01000046; EHM45033.1; -; Genomic_DNA.
DR   RefSeq; WP_006820830.1; NZ_JH417874.1.
DR   AlphaFoldDB; G9ZA23; -.
DR   STRING; 1002368.HMPREF0880_04382; -.
DR   PATRIC; fig|1002368.3.peg.4003; -.
DR   HOGENOM; CLU_004542_5_1_6; -.
DR   Proteomes; UP000003044; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..765
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003529205"
FT   DOMAIN          685..754
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   765 AA;  83477 MW;  5AA449448D15B178 CRC64;
     MKWLCSVGVA VSLAIQPALA DSLFGNHPLT PEARDAFVTE LLKKMTVDEK IGQLRLISVG
     PDNPKDAIRE MIKDGQVGAI FNTVTRQDIR TMQDQVMQLS RLKIPLFFAY DVIHGQRTVF
     PNSLGLASSF NLDAVKTVGR VSAYEAADDG LNMTWAPMVD VSRDPRWGRV SEGFGEDTYL
     TAIMGKTMVE SMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSPQ RLFNDYLPPY
     KAALDAGSGG VMVALNSLNG TPASSDSWLL KDILRDDWGF KGITISDHGA IKELIKHGTA
     SDPEDAVRIA LTSGINMSMS DEYYSKYLPG LVKSGKVTMA ELDDATRHVL NVKYDMGLFN
     DPYSHLGAKE TDPQDTNAES RLHRKEAREV ARESLVLLKN RLETLPLKKN AIIAVVGPLA
     DSQRDMMGSW SAAGVASQSV TLLTGIQNAV GTEGKVLYAK GANVTNDKGI VEFLNQYEPA
     VVVDPRSPQA MIDEAVKAAK QSDVVVAVVG EAQGMAHEAS SRTDITIPQS QRDLISALKA
     TGKPLVLVLM NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPMSFP
     RSVGQIPVYY SHLNTGRPYN PEKPNKYTSH YFDEANGPLY PFGYGLSYTT FTVSDVKMSS
     PVMKRDGKVT ASVEVTNTGK REGATVIQMY VQDVTASMSR PVKQLRGFEK VTLKPGETQT
     VSFPIDVNAL KFWNQRMKFA AEPGKFNVFI GVDSARVKQG EFELQ
//