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Database: UniProt
Entry: Q4JHP5
LinkDB: Q4JHP5
Original site: Q4JHP5 
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   10-MAY-2017, entry version 47.
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.
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
CC       xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide
CC       in the biosphere, after cellulose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expressed in presence of xylan and repressed by
CC       glucose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000305}.
DR   EMBL; DQ087436; AAY86996.1; -; mRNA.
DR   ProteinModelPortal; Q4JHP5; -.
DR   SMR; Q4JHP5; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   mycoCLAP; XYN10A_ASPTE; -.
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; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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       {ECO:0000255}.
FT   CHAIN        20    326       Probable endo-1,4-beta-xylanase C.
FT                                /FTId=PRO_0000393193.
FT   DOMAIN       46    325       GH10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01096}.
FT   ACT_SITE    156    156       Proton donor. {ECO:0000250}.
FT   ACT_SITE    262    262       Nucleophile. {ECO:0000250}.
FT   DISULFID    280    286       {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
//
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