ID   XYNC_ASPFC              Reviewed;         316 AA.
AC   B0Y6E0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   03-MAY-2023, entry version 56.
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; ORFNames=AFUB_066600;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP50325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS499598; EDP50325.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B0Y6E0; -.
DR   SMR; B0Y6E0; -.
DR   PhylomeDB; B0Y6E0; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
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; 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..316
FT                   /note="Probable endo-1,4-beta-xylanase C"
FT                   /id="PRO_0000393189"
FT   DOMAIN          44..315
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..276
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  34476 MW;  4FDDF1F05E93AF30 CRC64;
     MVVLSKLVSS ILFVSLVSAG VIEERQAASI NQAFTSHGKK YFGTASDQAL LQKSQNEAIV
     RKDFGQLTPE NSMKWDATEP SQGRFNFAGA DFLVNYAKQN GKKVRGHTLV WHSQLPSWVS
     AISDKNTLTS VLKNHITTVM TRYKGQIYAW DVVNEIFNED GSLRDSVFSR VLGEDFVRIA
     FETARSVDPS AKLYINDYNL DSASYGKTQG MVRYVKKWLA AGIPIDGIGT QTHLGALTAL
     ASSGVSEVAI TELDIAGASS QDYVNVVKAC LDVPKCVGIT VWGVSDRDSW RSGSSPLLFD
     SNYQPKAAYN AIIAAL
//