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 24-JUN-2015, entry version 46. 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 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 RP 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 CC hydrolysis of xylan, a major structural heterogeneous CC polysaccharide found in plant biomass representing the second most CC abundant polysaccharide in the biosphere, after cellulose. CC {ECO:0000269|PubMed:16474906}. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic CC linkages in xylans. {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) CC family. {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 ProteinModelPortal; Q6PRW6; -. DR SMR; Q6PRW6; 30-325. DR STRING; 500485.XP_002563227.1; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR mycoCLAP; 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 Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001000; Glyco_hydro_10. DR InterPro; IPR031158; Glyco_hydro_10_AS. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. 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; GLYCOSYL_HYDROL_F10; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Polysaccharide degradation; Secreted; Signal; KW Xylan degradation. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 353 Endo-1,4-beta-xylanase. FT /FTId=PRO_0000429663. FT ACT_SITE 161 161 Proton donor. {ECO:0000250}. FT ACT_SITE 267 267 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU10061}. FT CARBOHYD 4 4 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 325 325 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 285 291 {ECO:0000250}. FT VARIANT 153 153 V -> L (in strain: A3969.2). FT {ECO:0000269|PubMed:16474906}. FT VARIANT 274 274 S -> T (in strain: A3969.2). FT {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 //