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Database: UniProt
Entry: B7SIW1
LinkDB: B7SIW1
Original site: B7SIW1 
ID   XYNB_PHACH              Reviewed;         290 AA.
AC   B7SIW1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 35.
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   Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum
OS   pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=5306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION,
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=RP78;
RX   PubMed=15278289; DOI=10.1007/s00294-004-0520-x;
RA   Decelle B., Tsang A., Storms R.K.;
RT   "Cloning, functional expression and characterization of three
RT   Phanerochaete chrysosporium endo-1,4-beta-xylanases.";
RL   Curr. Genet. 46:166-175(2004).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16348798;
RA   Dobozi M.S., Szakacs G., Bruschi C.V.;
RT   "Xylanase Activity of Phanerochaete chrysosporium.";
RL   Appl. Environ. Microbiol. 58:3466-3471(1992).
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. {ECO:0000269|PubMed:15278289,
CC       ECO:0000269|PubMed:16348798}.
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:15278289,
CC         ECO:0000269|PubMed:16348798};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.96 mg/ml for birchwood xylan {ECO:0000269|PubMed:15278289};
CC       pH dependence:
CC         Optimum pH is 4.5. {ECO:0000269|PubMed:15278289};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:15278289};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15278289}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
DR   EMBL; EU302793; ABZ88798.1; -; Genomic_DNA.
DR   SMR; B7SIW1; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11B_PHACH; -.
DR   eggNOG; ENOG410IGA5; Eukaryota.
DR   eggNOG; ENOG410YH6C; LUCA.
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; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    290       Endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_5000419220.
FT   DOMAIN       34    222       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      255    290       CBM1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00597}.
FT   ACT_SITE    118    118       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    209    209       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   290 AA;  30466 MW;  6D0583921B4F6580 CRC64;
     MVSFNSLLVA VSAATCALAF PFEFHNGTHV FPRQSTPAGT GTNNGYFYSF WTDGGGSVTY
     NNGPAGEYSV TWSNADNFVA GKGWNPGSAQ AISFTANYQP NGNSYLSVYG WSTNPLVEYY
     ILEDFGTYNP AVSLTHKGTL TSDGATYDVY EGTRVNEPSI QGTATFNQYW SIRSSKRSSG
     TVTTANHFAA WKQLGLPLGT FNYQIVATEG YQSSGSSTVT VNPAGGVTSP IAPTGPSSVS
     TTPSGPSSSP SPVGTCSALY GQCGGQGWTG PTCCSSGTCK FSNNWYSQCL
//
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