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Database: UniProt
Entry: E7EF85
LinkDB: E7EF85
Original site: E7EF85 
ID   XYNB_PENOX              Reviewed;         310 AA.
AC   E7EF85;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   05-DEC-2018, entry version 25.
DE   RecName: Full=Endo-1,4-beta-xylanase B;
DE            Short=Xylanase B;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE   Flags: Precursor;
GN   Name=xynB;
OS   Penicillium oxalicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=B3-11-2;
RX   PubMed=23412069; DOI=10.4014/jmb.1208.08030;
RA   Wang J., Mai G., Liu G., Yu S.;
RT   "Molecular cloning and heterologous expression of an acid-stable
RT   endoxylanase gene from Penicillium oxalicum in Trichoderma reesei.";
RL   J. Microbiol. Biotechnol. 23:251-259(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=GZ-2;
RA   Liao H., Xu C., Tan S., Shen Q., Xu Y.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   INDUCTION.
RX   PubMed=22940308; DOI=10.1016/j.biortech.2012.07.051;
RA   Liao H., Xu C., Tan S., Wei Z., Ling N., Yu G., Raza W., Zhang R.,
RA   Shen Q., Xu Y.;
RT   "Production and characterization of acidophilic xylanolytic enzymes
RT   from Penicillium oxalicum GZ-2.";
RL   Bioresour. Technol. 123:117-124(2012).
CC   -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. Hydrolyzes birchwood xylan,
CC       beechwood xylan, and oat spelt xylan to produce short-chain
CC       xylooligosaccharides, xylopentaose, xylotriose, and xylobiose as
CC       the main products. {ECO:0000269|PubMed:22940308,
CC       ECO:0000269|PubMed:23412069}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:22940308,
CC         ECO:0000269|PubMed:23412069};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 mg/ml for birchwood xylan {ECO:0000269|PubMed:22940308,
CC         ECO:0000269|PubMed:23412069};
CC         KM=4.6 mg/ml for beechwood xylan {ECO:0000269|PubMed:22940308,
CC         ECO:0000269|PubMed:23412069};
CC         KM=11.3 mg/ml for oat spelt xylan {ECO:0000269|PubMed:22940308,
CC         ECO:0000269|PubMed:23412069};
CC         Vmax=2 umol/min/mg enzyme toward birchwood xylan
CC         {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC         Vmax=2 umol/min/mg enzyme toward beechwood xylan
CC         {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC         Vmax=2.5 umol/min/mg enzyme toward oat spelt xylan
CC         {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:22940308,
CC         ECO:0000269|PubMed:23412069};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:22940308, ECO:0000269|PubMed:23412069};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23412069}.
CC   -!- INDUCTION: Induced by soluble xylo-oligosaccharides, with
CC       beechwood xylan being the best inducer.
CC       {ECO:0000269|PubMed:22940308}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; HQ680966; ADV31286.1; -; Genomic_DNA.
DR   EMBL; KF233758; AGW24301.1; -; mRNA.
DR   SMR; E7EF85; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_PENOX; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PF00734; CBM_1; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   ProDom; PD001821; CBD_fun; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 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     19       {ECO:0000255}.
FT   CHAIN        20    310       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000429615.
FT   DOMAIN       33    223       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      275    310       CBM1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00597}.
FT   COMPBIAS    214    272       Ser-rich.
FT   ACT_SITE    119    119       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    210    210       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   310 AA;  31282 MW;  0EE37FBE5422BF73 CRC64;
     MISLSSVAIA LTTVVGALAL PSDQSVNLAA RQAITSSQTG TNNGYYYSFW TNGAGSVSYS
     NGAAGQFSVN WANQGGGDFT CGKGWNPGKA QDISFSGTFT PNGNAYLSIY GWTTGPLVEY
     YILENFGSYN PGNGMTHVGT LTSDGSDYDI YKHTQVNQPS IVGTSTFDQY WSIRKNKRSS
     GTVTTANHFS AWASHGMNLG SHNYQILSVE GYQSSGSASM TVSAGSSSSG GSGSGSGSGS
     GSGSGSGSQT TTAGSSTGTG TGSGSGSGSG GSGGNCAAQW GQCGGQGWNG PTCCSSGTCK
     ASNQWYSQCL
//
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