GenomeNet

Database: UniProt
Entry: Q6QJ75
LinkDB: Q6QJ75
Original site: Q6QJ75 
ID   XYN6_ASPNG              Reviewed;         211 AA.
AC   Q6QJ75;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 54.
DE   RecName: Full=Endo-1,4-beta-xylanase 6;
DE            Short=Xylanase 6;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 6;
DE   Flags: Precursor;
GN   Name=XYN6;
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], SUBCELLULAR LOCATION, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=IBT-90;
RX   DOI=10.1016/j.enzmictec.2005.12.003;
RA   Korona B., Korona D., Bielecki S.;
RT   "Efficient expression and secretion of two co-produced xylanases from
RT   Aspergillus niger in Pichia pastoris directed by their native signal
RT   peptides and the Saccharomyces cerevisiae a-mating factor.";
RL   Enzyme Microb. Technol. 39:683-689(2006).
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 3.5. {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}.
DR   EMBL; AY536638; AAS46913.1; -; mRNA.
DR   ProteinModelPortal; Q6QJ75; -.
DR   SMR; Q6QJ75; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11F_ASPNG; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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; 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   SUPFAM; SSF49899; SSF49899; 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     16       {ECO:0000255}.
FT   CHAIN        17    211       Endo-1,4-beta-xylanase 6.
FT                                /FTId=PRO_0000393173.
FT   DOMAIN       19    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    106    106       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    197    197       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   211 AA;  22561 MW;  973CD0651D5F8C9A CRC64;
     MKVTAAFAGL LVTALAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
     VSSDFVVGLG WTTGSSNPIT YSADYSASGS SSYLAVYGWD NYPQAEYYIV EDYGDYNPCS
     SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA
     QHGFGNSDFN YQVVAVEAWS GAGSASVTIS S
//
DBGET integrated database retrieval system