ID   XYNC_ASPTE              Reviewed;         326 AA.
AC   Q4JHP5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Probable endo-1,4-beta-xylanase C;
DE            Short=Xylanase C;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE   Flags: Precursor;
GN   Name=xlnC;
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BCC129;
RX   PubMed=16275128; DOI=10.1016/j.pep.2005.09.013;
RA   Chantasingh D., Pootanakit K., Champreda V., Kanokratana P.,
RA   Eurwilaichitr L.;
RT   "Cloning, expression, and characterization of a xylanase 10 from
RT   Aspergillus terreus (BCC129) in Pichia pastoris.";
RL   Protein Expr. Purif. 46:143-149(2006).
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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expressed in presence of xylan and repressed by glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; DQ087436; AAY86996.1; -; mRNA.
DR   AlphaFoldDB; Q4JHP5; -.
DR   SMR; Q4JHP5; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10A_ASPTE; -.
DR   VEuPathDB; FungiDB:ATEG_08906; -.
DR   UniPathway; UPA00114; -.
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   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript 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..326
FT                   /note="Probable endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000393193"
FT   DOMAIN          46..325
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..286
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  35346 MW;  9DC41D6EC492DE23 CRC64;
     MVRLTVLAGF LLTSAACSAC VIGERQAASS INNAFKAKGK KYFGTCGDQG TLSDSTNSAI
     VKADFGQLTP ENSMKWDATE PNRGQFSFGG ADYLVNYAAS NGKMIRGHTL VWHSQLPGWV
     QGITDKNTLT SVLKNHITTV MQRYKGKVYA WDVVNEIFNE DGSLRKSVFY NVLGEDFVRI
     AFETARSVDP QAKLYINDYN LDNANYAKTK GMADHVRKWI SQGIPIDGIG SQTHLGSGGS
     WTVKDALNTL ASSGVSEVAI TELDIAGASS TDYVNVVNAC LSVSKCVGIT VWGVSDKYSW
     RSNDKPLLFD SNFQPKAAYN AIISAL