ID   XYNC_ASPNG              Reviewed;         327 AA.
AC   C5J411; C6F1T1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 44.
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 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].
RC   STRAIN=DMS1957;
RA   Nguyen S.L.T., Quyen D.T.;
RT   "Gene cloning, sequencing, expression and characterization of a xylanase A
RT   gene from Aspergillus niger DMS1957.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=IME-216;
RA   Huang J.Z., Xu Y., Tian B.Y., Huang Q.G.;
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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; FJ986225; ACR83565.1; -; mRNA.
DR   EMBL; EU848304; ACJ26381.1; -; mRNA.
DR   AlphaFoldDB; C5J411; -.
DR   SMR; C5J411; -.
DR   STRING; 5061.CADANGAP00003040; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10B_ASPNG; -.
DR   VEuPathDB; FungiDB:An03g00940; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1176802; -.
DR   VEuPathDB; FungiDB:ATCC64974_83150; -.
DR   VEuPathDB; FungiDB:M747DRAFT_306330; -.
DR   eggNOG; ENOG502QSCW; Eukaryota.
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; IPR031158; GH10_AS.
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; PS00591; GH10_1; 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..327
FT                   /note="Probable endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000393190"
FT   DOMAIN          55..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"
FT   CONFLICT        11..13
FT                   /note="MLF -> KLI (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="D -> E (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="W -> R (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="S -> A (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="E -> G (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="S -> P (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="G -> D (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="N -> D (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321..323
FT                   /note="DAI -> FAV (in Ref. 1; ACR83565)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   327 AA;  35476 MW;  90B2F71FFCA70A65 CRC64;
     MVQIKVAALA MLFASQVLSE PIDPRQASVS IDTKFKAHGK KYLGNIGDQY TLTKNSKTPA
     IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ SNNKLIRGHT LVWHSQLPSW
     VQSITDKNTL IEVMKNHITT VMQHYKGKIY AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR
     IAFETARAAD PNAKLYINDY NLDSASYSKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG
     GAGISGALNA LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS
     WRSSSTPLLF DSNYNPKPAY DAIANAL