ID CEXY_THEST Reviewed; 387 AA. AC P40942; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 03-MAY-2023, entry version 94. DE RecName: Full=Thermostable celloxylanase; DE EC=3.2.1.4; DE EC=3.2.1.8; GN Name=xynB; OS Thermoclostridium stercorarium (Clostridium stercorarium). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Thermoclostridium. OX NCBI_TaxID=1510; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=F-9; RX PubMed=7765974; DOI=10.1271/bbb.59.40; RA Fukumura M., Sakka K., Shimada K., Ohmiya K.; RT "Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an RT extremely thermostable xylanase, and characterization of the translated RT product."; RL Biosci. Biotechnol. Biochem. 59:40-46(1995). CC -!- FUNCTION: Active toward xylan, carboxymethylcellulose, P-nitrophenyl- CC beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0.; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius.; CC -!- PATHWAY: Glycan degradation; xylan degradation. 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; D12504; BAA02069.1; -; Genomic_DNA. DR PIR; JC2484; JC2484. DR PDB; 2DEP; X-ray; 1.80 A; A/B=41-387. DR PDBsum; 2DEP; -. DR AlphaFoldDB; P40942; -. DR SMR; P40942; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; P40942; -. DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 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; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; KW Hydrolase; Polysaccharide degradation; Xylan degradation. FT CHAIN 1..387 FT /note="Thermostable celloxylanase" FT /id="PRO_0000184061" FT DOMAIN 41..382 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 185 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 293 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:2DEP" FT TURN 51..54 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 68..77 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 102..113 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 117..128 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 148..173 FT /evidence="ECO:0007829|PDB:2DEP" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 207..220 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 222..231 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 236..251 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 272..283 FT /evidence="ECO:0007829|PDB:2DEP" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 288..299 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 313..331 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 332..336 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 351..353 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 355..359 FT /evidence="ECO:0007829|PDB:2DEP" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:2DEP" FT HELIX 374..380 FT /evidence="ECO:0007829|PDB:2DEP" SQ SEQUENCE 387 AA; 44378 MW; C7221BD5E32C8E48 CRC64; MNKFLNKKWS LILTMGGIFL MATLSLIFAT GKKAFNDQTS AEDIPSLAEA FRDYFPIGAA IEPGYTTGQI AELYKKHVNM LVAENAMKPA SLQPTEGNFQ WADADRIVQF AKENGMELRF HTLVWHNQTP TGFSLDKEGK PMVEETDPQK REENRKLLLQ RLENYIRAVV LRYKDDIKSW DVVNEVIEPN DPGGMRNSPW YQITGTEYIE VAFRATREAG GSDIKLYIND YNTDDPVKRD ILYELVKNLL EKGVPIDGVG HQTHIDIYNP PVERIIESIK KFAGLGLDNI ITELDMSIYS WNDRSDYGDS IPDYILTLQA KRYQELFDAL KENKDIVSAV VFWGISDKYS WLNGFPVKRT NAPLLFDRNF MPKPAFWAIV DPSRLRE //