ID   BGLX_ERWCH              Reviewed;         654 AA.
AC   Q46684;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Periplasmic beta-glucosidase/beta-xylosidase;
DE   Includes:
DE     RecName: Full=Beta-glucosidase;
DE              EC=3.2.1.21;
DE     AltName: Full=Gentiobiase;
DE     AltName: Full=Cellobiase;
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   Erwinia chrysanthemi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D1;
RX   MEDLINE=95198684; 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
RT   chrysanthemi D1 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: Hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-xylans, to remove
CC       successive D-xylose residues from the non-reducing termini.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
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DR   EMBL; U08606; AAA80156.1; -; Genomic_DNA.
DR   PIR; S53805; S53805.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   BRENDA; 3.2.1.21; 1459.
DR   BRENDA; 3.2.1.37; 1459.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:EC.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   Gene3D; G3DSA:3.20.20.300; Glyco_hydro_3_N; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 2.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Multifunctional enzyme; Periplasm; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    654       Periplasmic beta-glucosidase/beta-
FT                                xylosidase.
FT                                /FTId=PRO_0000011783.
FT   ACT_SITE    235    235       By similarity.
FT   ACT_SITE    360    360       By similarity.
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
//