ID   XYN_PENCH               Reviewed;         353 AA.
AC   Q6PRW6; Q2PS23;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
DE   Flags: Precursor;
GN   Name=Xyn; Synonyms=xyl;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-153 AND THR-274, SUBCELLULAR
RP   LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHISICOCHEMICAL PROPERTIES.
RC   STRAIN=A3969.2, and FS010;
RX   PubMed=16474906; DOI=10.1111/j.1745-7270.2006.00135.x;
RA   Hou Y.H., Wang T.H., Long H., Zhu H.Y.;
RT   "Novel cold-adaptive Penicillium strain FS010 secreting thermo-labile
RT   xylanase isolated from Yellow Sea.";
RL   Acta Biochim. Biophys. Sin. 38:142-149(2006).
CC   -!- FUNCTION: Cold active endo-1,4-beta-xylanase involved in the hydrolysis
CC       of xylan, a major structural heterogeneous polysaccharide found in
CC       plant biomass representing the second most abundant polysaccharide in
CC       the biosphere, after cellulose. {ECO:0000269|PubMed:16474906}.
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:16474906};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5.;
CC       Temperature dependence:
CC         Optimum temperature is 15 degrees Celsius.;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16474906}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; AY583585; AAS93681.1; -; mRNA.
DR   EMBL; DQ304546; ABC18330.1; -; mRNA.
DR   AlphaFoldDB; Q6PRW6; -.
DR   SMR; Q6PRW6; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   CLAE; XYN10B_PENCH; -.
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   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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..353
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000429663"
FT   DOMAIN          50..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        285..291
FT                   /evidence="ECO:0000250"
FT   VARIANT         153
FT                   /note="V -> L (in strain: A3969.2)"
FT                   /evidence="ECO:0000269|PubMed:16474906"
FT   VARIANT         274
FT                   /note="S -> T (in strain: A3969.2)"
FT                   /evidence="ECO:0000269|PubMed:16474906"
SQ   SEQUENCE   353 AA;  38165 MW;  8C40976394FABD8E CRC64;
     MIPNITQLKT AALVMLFAGQ ALSGPVESRQ ASESIDAKFK AHGKKYLGNI ADQGTLNGNP
     KTPAIIKANF GQLSPENSMK WDATEPSQGQ FSFAGSDYFV EFAETNGKLI RGHTLVWHSQ
     LPSWVSSITD KTTLTDVMKN HITTVMKQYK GKVYAWDVVN EIFEEDGTLR DSVFSRVLGE
     DFVRIAFETA READPEAKLY INDYNLDSAT SAKLQGMVSH VKKWIAAGVP IDGIGSQTHL
     GAGAGAAASG ALNALASAGT EEVAVTELDI AGASSTDYVD VVNACLDQPK CVGITVWGVA
     DPDSWRADES PLLFDASYNP KEAYNVSQLL SRQHAFDLYL KLGNLLLSRL HSD