GenomeNet

Database: UniProt
Entry: B0Y8Q8
LinkDB: B0Y8Q8
Original site: B0Y8Q8 
ID   XYNB_ASPFC              Reviewed;         221 AA.
AC   B0Y8Q8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 49.
DE   RecName: Full=Probable 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   AltName: Full=Endo-1,4-beta-xylanase G1;
DE            Short=Xylanase G1;
DE   Flags: Precursor;
GN   Name=xlnB; Synonyms=xynB, xynG1; ORFNames=AFUB_078210;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)
OS   (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8;
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; DS499599; EDP49789.1; -; Genomic_DNA.
DR   ProteinModelPortal; B0Y8Q8; -.
DR   SMR; B0Y8Q8; -.
DR   EnsemblFungi; EDP49789; EDP49789; AFUB_078210.
DR   HOGENOM; HOG000179135; -.
DR   PhylomeDB; B0Y8Q8; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; ISS:UniProtKB.
DR   GO; GO:0045493; P:xylan catabolic process; ISS: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   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    221       Probable endo-1,4-beta-xylanase B.
FT                                /FTId=PRO_0000393166.
FT   DOMAIN       33    221       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    117    117       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    208    208       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
SQ   SEQUENCE   221 AA;  23810 MW;  730177E76983C1E6 CRC64;
     MVSFSSLVLA ASTVAGVLAT PGSEQYVELA KRQLTSSQTG TNNGYYYSFW TDGGGQVTYT
     NGNGGQYQVD WNNCGNFVAG KGWNPASEKA VTYSGSWQTS GNGYLSVYGW TTSPLVEFYI
     VESYGSYDPS TGATHLGTVE SDGATYNLYK TTRTNAPSIQ GTATFDQYWS VRTSHRQSGT
     VTTKNHFDAW RNAGLQLGNF DYMIVATEGY QSSGSATITV S
//
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