ID   BGLX_DICCH              Reviewed;         654 AA.
AC   Q46684;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Periplasmic beta-glucosidase/beta-xylosidase;
DE   Includes:
DE     RecName: Full=Beta-glucosidase;
DE              EC=3.2.1.21;
DE     AltName: Full=Cellobiase;
DE     AltName: Full=Gentiobiase;
DE   Includes:
DE     RecName: Full=Beta-xylosidase;
DE              EC=3.2.1.37;
DE     AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE     AltName: Full=Xylan 1,4-beta-xylosidase;
DE   Flags: Precursor;
GN   Name=bgxA;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D1;
RX   PubMed=7891660; DOI=10.1007/bf00290450;
RA   Vroemen S., Heldens J., Boyd C., Henrissat B., Keen N.T.;
RT   "Cloning and characterization of the bgxA gene from Erwinia chrysanthemi D1
RT   which encodes a beta-glucosidase/xylosidase enzyme.";
RL   Mol. Gen. Genet. 246:465-477(1995).
CC   -!- FUNCTION: Exhibits both beta-glucosidase and beta-xylosidase
CC       activities.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; U08606; AAA80156.1; -; Genomic_DNA.
DR   PIR; S53805; S53805.
DR   AlphaFoldDB; Q46684; -.
DR   SMR; Q46684; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 2.
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   Pfam; PF00933; Glyco_hydro_3; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Periplasm; Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..654
FT                   /note="Periplasmic beta-glucosidase/beta-xylosidase"
FT                   /id="PRO_0000011783"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   654 AA;  71584 MW;  5CEDFE62162A7A95 CRC64;
     MEKSATRQKA LLIALPLLFS PLASAVQQAV LDTRGAPLIT VNGLTFKDLN RDGKLNPYED
     WRLPAAERAA DLVSRMTLAE KAGVMMHGSA PTAGSVTGAG TQYDLNAAKT MIADRYVNSF
     ITRLSGDNPA QMAEENNKLQ QLAEATRLGI PLTISTDPRS SFQSLVGVSV SVGKFSKWPE
     TLGLAAIGDE ELVRRFADIV RQEYRAVGIT EALSPQADLA TEPRWPRIDG TFGEDPDLTK
     KMVRGYVTGM QNGKNGLNAQ SVISIVKHWV GYGAAKDGWD SHNVYGKYAQ FRQNNLQWHI
     DPFTGAFEAH AAGIMPTYSI LRNASWHGKP IEQVGAGFNR FLLTDLLRGQ YGFDGVILSD
     WLITNDCKGD CLTGVKPGEK PVPRGMPWGV EKLTPAERFV KAVNAGVDQF GGVTDSALLV
     QAVQDGKLTE ARLDTSVNRI LKQKFQTGLF ERPYVNATQA NDIVGRADWQ QLADDTQARS
     LVLLQNNNLL PLRKGSRVWL HGIAANAAQE VGFIVVNTPE QADVALIRTH TPYEQPHKNF
     FFGSRHHEGS LAFRNDNPDY QAIVRASAKV PTLVTVYMER PAILTNVVDK TRAVVANFGV
     SDSVLLNRLM SGAAYTAKLP FELPSSMSAV RNQQPDLPYD SAKPLFPFGY GLPH