XYNA_ASPNG
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 25-MAY-2022, entry version 105.
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;
OC Aspergillus subgen. Circumdati.
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 Aspergillus
RT 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 xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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) family.
CC {ECO:0000305}.
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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 PDB; 6QE8; X-ray; 1.79 A; A=1-211.
DR PDBsum; 1T6G; -.
DR PDBsum; 1UKR; -.
DR PDBsum; 2QZ2; -.
DR PDBsum; 6QE8; -.
DR AlphaFoldDB; P55329; -.
DR SMR; P55329; -.
DR Allergome; 980; Asp n Hemicellulase.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR VEuPathDB; FungiDB:An14g07390; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1101058; -.
DR VEuPathDB; FungiDB:ATCC64974_22790; -.
DR VEuPathDB; FungiDB:M747DRAFT_300402; -.
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; Xylan degradation.
FT SIGNAL 1..27
FT CHAIN 28..211
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000007992"
FT DOMAIN 28..210
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 106
FT /note="Nucleophile"
FT ACT_SITE 197
FT /note="Proton donor"
FT DISULFID 119..138
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6QE8"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6QE8"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:6QE8"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:6QE8"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 133..147
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 150..163
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6QE8"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:6QE8"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 187..201
FT /evidence="ECO:0007829|PDB:6QE8"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6QE8"
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
