ID XYNA_PENCN Reviewed; 327 AA.
AC Q5S7A8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 22-FEB-2023, entry version 60.
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 Flags: Precursor;
GN Name=xylA;
OS Penicillium canescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5083;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION,
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=F178;
RX PubMed=12391748;
RA Serebrianyi V.A., Vavilova E.A., Chulkin A.M., Vinetskii I.U.P.;
RT "Cloning of an endo-1,4-beta-xylanase gene from Penicillium canescens and
RT construction of multicopy strains.";
RL Appl. Biochem. Microbiol. 38:495-501(2002).
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:0000269|PubMed:12391748}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:12391748};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12391748}.
CC -!- INDUCTION: Nucleotide sequences for binding catabolite repression
CC protein CREA were detected in the promoter region.
CC {ECO:0000269|PubMed:12391748}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000305}.
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DR EMBL; AY756109; AAV65488.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5S7A8; -.
DR SMR; Q5S7A8; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CLAE; XYN10A_PENCA; -.
DR UniPathway; UPA00114; -.
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; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..327
FT /note="Endo-1,4-beta-xylanase A"
FT /id="PRO_0000429614"
FT DOMAIN 46..326
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT DISULFID 281..287
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 35091 MW; 62C0BB32926005ED CRC64;
MVQLKTAALA LLFAGQALSG PVDSRQASVS IDAKFKAHGK KYLGTIGDQY TLTKNTKNPA
IIKADFGQLT PENSMKWDAT EPNRGQFTFS GSDYLVNFAQ SNGKLIRGHT LVWHSQLPGW
VSSITDKNTL ISVLKNHITT VMTRYKGKIY AWDVLNEIFN EDGSLRNSVF YNVIGEDYVR
IAFETARSVD PNAKLYINDY NLDSAGYSKV NGMVSHVKKW LAAGIPIDGI GSQTHLGAGA
GSAVAGALNA LASAGTKEIA ITELDIAGAS STDYVNVVNA CLNQAKCVGI TVWGVADPDS
WRSSSSPLLF DGNYNPKAAY NAIANAL
//
