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 11-DEC-2019, entry version 60. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY583585; AAS93681.1; -; mRNA. DR EMBL; DQ304546; ABC18330.1; -; mRNA. DR SMR; Q6PRW6; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR mycoCLAP; XYN10B_PENCH; -. DR eggNOG; ENOG410IH86; Eukaryota. DR eggNOG; COG3693; LUCA. 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; IPR001000; GH10. DR InterPro; IPR031158; GH10_AS. 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; 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 //