ID XYN2_GEOSE Reviewed; 330 AA. AC P45703; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 97. 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; GN Name=xynA; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Anoxybacillaceae; OC Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-7. RC STRAIN=No. 21; RX PubMed=8074507; DOI=10.1128/aem.60.7.2252-2258.1994; RA Baba T., Shinke R., Nanmori T.; RT "Identification and characterization of clustered genes for thermostable RT xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus RT stearothermophilus 21."; RL Appl. Environ. Microbiol. 60:2252-2258(1994). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- PATHWAY: Glycan degradation; xylan degradation. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- INDUCTION: By xylan and xylose. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. CC Cytoplasmic xylanase subfamily. {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; D28121; BAA05668.1; -; Genomic_DNA. DR PIR; I39760; I39760. DR PDB; 9FKH; X-ray; 2.30 A; A/B=1-330. DR PDB; 9FKI; X-ray; 2.30 A; A/B=1-330. DR PDB; 9FKJ; X-ray; 2.00 A; A/B=1-330. DR PDB; 9FKK; X-ray; 2.40 A; A/B=1-330. DR PDB; 9FKL; X-ray; 2.40 A; A/B=1-330. DR AlphaFoldDB; P45703; -. DR SMR; P45703; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR UniPathway; UPA00114; -. DR GO; GO:0005737; C:cytoplasm; 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; Glycosidases; 1. DR InterPro; IPR044846; GH10. DR InterPro; IPR031158; GH10_AS. DR InterPro; IPR001000; GH10_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR PANTHER; PTHR31490:SF90; ENDO-1,4-BETA-XYLANASE A; 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. DR PDBsum; 9FKH; -. DR PDBsum; 9FKI; -. DR PDBsum; 9FKJ; -. DR PDBsum; 9FKK; -. DR PDBsum; 9FKL; -. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cytoplasm; KW Direct protein sequencing; Glycosidase; Hydrolase; KW Polysaccharide degradation; Xylan degradation. FT CHAIN 1..330 FT /note="Endo-1,4-beta-xylanase" FT /id="PRO_0000007969" FT DOMAIN 2..330 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 133 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 240 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:9FKJ" FT TURN 12..15 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 24..29 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 31..37 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 39..45 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 62..66 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 69..74 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 76..87 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 90..93 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 103..121 FT /evidence="ECO:0007829|PDB:9FKJ" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:9FKI" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 156..167 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 171..179 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 219..230 FT /evidence="ECO:0007829|PDB:9FKJ" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 235..246 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 260..279 FT /evidence="ECO:0007829|PDB:9FKJ" FT TURN 280..283 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 284..293 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:9FKJ" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:9FKJ" FT HELIX 322..328 FT /evidence="ECO:0007829|PDB:9FKJ" SQ SEQUENCE 330 AA; 38473 MW; 0A2026B23502EB48 CRC64; MCSSIPSLRE VFANDFRIGA AVNPVTLEAQ QSLLIRHVNS LTAENHMKFE HLQPEEGRFT FDIAIKSSTS PFSSHGVRGH TLVWHNQTPS WVFQDSQGHF VGRDVLLERM KSHISTVVQR YKGKVYCWDV INEAVADEGS EWLRSSTWRQ IIGDDFIQQA FLYAHEADPE ALLFYNDYNE CFPEKREKIY TLVKSLRDKG IPIHGIGMQA HWSLNRPTLD EIRAAIERYA SLGVILHITE LDISMFEFDD HRKDLAAPTN EMVERQAERY EQIFSLFKEY RDVIQNVTFW GIADDHTWLD HFPVQGRKNW PLLFDEQHNP KPAFWRVVNI //