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Database: UniProt
Entry: D7EZJ3
LinkDB: D7EZJ3
Original site: D7EZJ3 
ID   XYNB_STRSQ              Reviewed;         340 AA.
AC   D7EZJ3;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   05-DEC-2018, entry version 34.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   Flags: Precursor;
GN   Name=xynBS9;
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=S9;
RA   Yao G., Li N., Wang Y., Shi P., Chen Q., Yao B.;
RT   "Cloning, expression, and characterization of a xylanase gene, xynBS9,
RT   from Streptomyces sp. S9.";
RL   J. Agric. Sci. Technol. (Beijing) 11:64-70(2009).
CC   -!- FUNCTION: Endo-acting xylanase which specifically cleaves internal
CC       linkages on the xylan backbone, releasing xylooligosaccharides. Is
CC       able to hydrolyze oat spelt xylan and birchwood xylan, releasing
CC       xylobiose and xylotriose as the major products.
CC       {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Is inhibited by Ag(+) and Hg(2+) in vitro.
CC       EDTA and other metal cations such as Na(+), K(+), Ca(2+), Cu(2+),
CC       Mg(2+), Fe(3+), and Zn(2+) have no effect on catalytic activity.
CC       {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=3741 umol/min/mg enzyme with oat spelt xylan as substrate
CC         (at pH 6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1};
CC         Vmax=2320 umol/min/mg enzyme with birchwood xylan as substrate
CC         (at pH 6.5 and 60 degrees Celsius) {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 6-7. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; EU660499; ACF57947.1; -; Genomic_DNA.
DR   SMR; D7EZJ3; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     52       {ECO:0000255}.
FT   CHAIN        53    340       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000424417.
FT   DOMAIN       54    239       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      248    340       CBM2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01135}.
FT   ACT_SITE    138    138       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    227    227       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   340 AA;  36245 MW;  84EBAF44059CCCB3 CRC64;
     MHDAPAQRKR RRPGRIGPLP RSSRFARLKL LIASACAALL ATLALPPGAA HAQTVTSNQT
     GNHNGYFYSF WTDAPGTVSA TMGSGGNYST SWRNTGNFVI GKGWSTGGRR TVTYSGSFNP
     SGNAYLTLYG WSRNPLVEYY IVDNWGTYRP TGTFKGTVTT DGGTYDIYQT TRYNAPSIEG
     NKTFNQYWSV RQQKRTGGTI TTGNHFDAWA RAGMQLGSHD YMIMATEGYQ SSGSSNITVG
     GTSGGGGGGG GGGGCTATLS AGERWDDRYN LNVSVSGSSN WTVTMNVPSP ATILSTWNIT
     ATWPSSQVLV ARPNGSGNNF GVTIKHNGNW TWPTVSCSTG
//
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