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Database: UniProt
Entry: P55329
LinkDB: P55329
Original site: P55329 
ID   XYNA_ASPNG              Reviewed;         211 AA.
AC   P55329;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 95.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   AltName: Full=Endo-1,4-beta-xylanase I;
DE            Short=Xylanase I;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hessing J.G.M., van Gorcom R.F.M., Verbakel J.M.A., Roza M., Maat J.;
RT   "Xylanase production.";
RL   Patent number WO9119782, 26-DEC-1991.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=8890913; DOI=10.1006/jmbi.1996.0556;
RA   Krengel U., Dijkstra B.W.;
RT   "Three-dimensional structure of Endo-1,4-beta-xylanase I from
RT   Aspergillus niger: molecular basis for its low pH optimum.";
RL   J. Mol. Biol. 263:70-78(1996).
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.
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 3.0.;
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; A19535; CAA01470.1; -; Unassigned_DNA.
DR   PDB; 1T6G; X-ray; 1.80 A; C/D=28-211.
DR   PDB; 1UKR; X-ray; 2.40 A; A/B/C/D=28-211.
DR   PDB; 2QZ2; X-ray; 2.80 A; A=28-211.
DR   PDBsum; 1T6G; -.
DR   PDBsum; 1UKR; -.
DR   PDBsum; 2QZ2; -.
DR   ProteinModelPortal; P55329; -.
DR   SMR; P55329; -.
DR   Allergome; 980; Asp n Hemicellulase.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   BRENDA; 3.2.1.8; 518.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P55329; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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   3D-structure; Carbohydrate metabolism; Disulfide bond; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     27
FT   CHAIN        28    211       Endo-1,4-beta-xylanase A.
FT                                /FTId=PRO_0000007992.
FT   DOMAIN       28    210       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    106    106       Nucleophile.
FT   ACT_SITE    197    197       Proton donor.
FT   DISULFID    119    138
FT   STRAND       33     38       {ECO:0000244|PDB:1T6G}.
FT   HELIX        39     41       {ECO:0000244|PDB:1T6G}.
FT   STRAND       42     47       {ECO:0000244|PDB:1T6G}.
FT   TURN         48     51       {ECO:0000244|PDB:1T6G}.
FT   STRAND       52     63       {ECO:0000244|PDB:1T6G}.
FT   STRAND       65     73       {ECO:0000244|PDB:1T6G}.
FT   STRAND       79     86       {ECO:0000244|PDB:1T6G}.
FT   STRAND       90    100       {ECO:0000244|PDB:1T6G}.
FT   TURN        101    104       {ECO:0000244|PDB:1T6G}.
FT   STRAND      105    115       {ECO:0000244|PDB:1T6G}.
FT   STRAND      120    130       {ECO:0000244|PDB:1T6G}.
FT   STRAND      133    145       {ECO:0000244|PDB:1T6G}.
FT   STRAND      150    163       {ECO:0000244|PDB:1T6G}.
FT   STRAND      166    170       {ECO:0000244|PDB:1T6G}.
FT   HELIX       172    179       {ECO:0000244|PDB:1T6G}.
FT   HELIX       180    182       {ECO:0000244|PDB:1T6G}.
FT   STRAND      187    209       {ECO:0000244|PDB:1T6G}.
SQ   SEQUENCE   211 AA;  22642 MW;  82BEBEE12ED79303 CRC64;
     MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG
     VSSDFVVGLG WTTGSSKAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS
     SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA
     QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S
//
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