XYN5_ASPNG
ID XYN5_ASPNG Reviewed; 211 AA.
AC Q12549;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Endo-1,4-beta-xylanase 5;
DE Short=Xylanase 5;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 5;
DE Flags: Precursor;
GN Name=XYN5;
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 [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL 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 and
RT their expression in Saccharomyces cerevisiae.";
RL Biotechnol. Lett. 19:411-415(1997).
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. {ECO:0000250, ECO:0000269|Ref.1}.
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 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) family.
CC {ECO:0000305}.
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DR EMBL; U39784; AAA99065.1; -; mRNA.
DR AlphaFoldDB; Q12549; -.
DR SMR; Q12549; -.
DR STRING; 5061.CADANGAP00011453; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11E_ASPNG; -.
DR VEuPathDB; FungiDB:An14g07390; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1101058; -.
DR VEuPathDB; FungiDB:ATCC64974_22790; -.
DR VEuPathDB; FungiDB:M747DRAFT_300402; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..211
FT /note="Endo-1,4-beta-xylanase 5"
FT /id="PRO_0000393172"
FT DOMAIN 19..210
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 22794 MW; B546955778BF1ED0 CRC64;
MKVTAAFASL LLTAFAAPAP EPVLVSRSAG INYVQNYNGN LGDFTYDEST GTFSMYWEDG
VSSDFVVGLG WTTGSSKSIT YSAQYSASSS SSYLAVYGWV NSPQAEYYIV EDYGDYNPCS
SATSLGTVYS DGSTYQVCTD TRRTRPSITG TSTFTQYFSV RESTRTSGTV TIANHFNFWA
QHGFGNSNFN YQVMAVEAWN GVGSASVTIS S
