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Database: UniProt
Entry: Q12550
LinkDB: Q12550
Original site: Q12550 
ID   XYN4_ASPNG              Reviewed;         211 AA.
AC   Q12550;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   05-DEC-2018, entry version 68.
DE   RecName: Full=Endo-1,4-beta-xylanase 4;
DE            Short=Xylanase 4;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 4;
DE   Flags: Precursor;
GN   Name=XYN4;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 90196 / Alo MP-22;
RX   DOI=10.1023/A:1018327623422;
RA   Luttig M., Pretorius I.S., van Zyl W.H.;
RT   "Cloning of two beta-xylanase-encoding genes from Aspergillus niger
RT   and their expression in Saccharomyces cerevisiae.";
RL   Biotechnol. Lett. 19:411-415(1997).
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:0000250,
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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.0. {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:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA99066.1; Type=Frameshift; Positions=102, 178; Evidence={ECO:0000305};
DR   EMBL; U39785; AAA99066.1; ALT_FRAME; mRNA.
DR   SMR; Q12550; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11D_ASPNG; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IDA:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 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     16       {ECO:0000255}.
FT   CHAIN        17    211       Endo-1,4-beta-xylanase 4.
FT                                /FTId=PRO_0000393171.
FT   DOMAIN       19    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   COMPBIAS     86     92       Poly-Ser.
FT   ACT_SITE    106    106       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000250}.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   211 AA;  22669 MW;  B27B7D7F692979EE CRC64;
     MKVTAAFAGL LVTAFAPPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
     VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV NLSQAEYYIV EDYGDYNPCS
     SATSLGTEYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVAIHFNFWA
     QHGFGNSDFN YQVMAVEAWS GACSASVTIS S
//
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