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Database: UniProt
Entry: A0A085AG48_9ENTR
LinkDB: A0A085AG48_9ENTR
Original site: A0A085AG48_9ENTR 
ID   A0A085AG48_9ENTR        Unreviewed;       765 AA.
AC   A0A085AG48;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX {ECO:0000313|EMBL:KFC09193.1};
GN   ORFNames=GTGU_01132 {ECO:0000313|EMBL:KFC09193.1};
OS   Trabulsiella guamensis ATCC 49490.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Trabulsiella.
OX   NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC09193.1, ECO:0000313|Proteomes:UP000028630};
RN   [1] {ECO:0000313|EMBL:KFC09193.1, ECO:0000313|Proteomes:UP000028630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC09193.1,
RC   ECO:0000313|Proteomes:UP000028630};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) 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:KFC09193.1}.
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DR   EMBL; JMTB01000043; KFC09193.1; -; Genomic_DNA.
DR   RefSeq; WP_038154775.1; NZ_JMTB01000043.1.
DR   AlphaFoldDB; A0A085AG48; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000028630; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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_5001786437"
FT   DOMAIN          685..754
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   765 AA;  83553 MW;  54462C1078C40763 CRC64;
     MKWLCSVGVA VSLALQPALA DDLFGNHPLT PEARDAFVTE LLKKMTVDEK IGQLRLISVG
     PDNPKEAIRE MIKAGQVGAI FNTVTRPDIR TMQDQVMELS RLKIPLFFAY DVIHGQRTVF
     PNSLGLASSF NLDAVKTVGR VSAFEAADDG LNMTWAPMVD VSRDPRWGRV SEGFGEDTYL
     TAIMGKTMVE SMQGKSPADR YSVMTSVKHF AAYGAVEGGK EYNTVDMSPQ RLFNDYMPPY
     KAALDAGSGG VMVALNSLNG TPASSDSWLL KDLLRNEWGF KGITISDHGA IKELIKHGTA
     SDPEDAVRVA LKSGINMSMS DEYYSKYLPG LVKSGKVTMA ELDDATRHVL NVKYDMGLFN
     DPYSHLGPKE SDPKDTNAES RLHRKEAREV ARESLVLLKN RLDTLPLKKT ATIAVVGPLA
     DSKRDMMGSW SAAGVADQSV TLLTGIRNSV GTQGKVIYAK GANVTSDKGI VDFLNQYEPA
     VVVDPRSPQA MIDEAVTAAK QSDVVVAVVG EAQGMAHEAS SRTDITIPQS QRDIIAALKA
     TGKPLVLVLM NGRPLALVKE DQQADAILET WFAGTEGGNA IADVLFGDYN PSGKLPMSFP
     RSVGQIPVYY SHLNTGRPYN PEKPNKYTSR YFDEANGPLY PFGYGLSYTT FTVSDVKMSA
     PTMKRNGNVT ASVDVTNTGK REGATVIQMY LQDVTASMSR PVKQLRGFEK VNLKPGETRT
     VSFPIDVDAL KFWNQRMKYD VEPGKFNVFI GVDSARVKQG EFELK
//
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