ID XYNA_BACOV Reviewed; 376 AA. AC P49942; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 28-JUN-2023, entry version 92. DE RecName: Full=Endo-1,4-beta-xylanase A; DE Short=Xylanase A; DE EC=3.2.1.8; DE AltName: Full=1,4-beta-D-xylan xylanohydrolase A; DE Flags: Precursor; GN Name=xylI; OS Bacteroides ovatus. OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=28116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=V975; RX PubMed=7766665; DOI=10.1016/0304-4165(95)00051-c; RA Whitehead T.R.; RT "Nucleotide sequences of xylan-inducible xylanase and RT xylosidase/arabinosidase genes from Bacteroides ovatus V975."; RL Biochim. Biophys. Acta 1244:239-241(1995). 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 -!- INDUCTION: By xylan. 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; U04957; AAB08023.1; -; Genomic_DNA. DR PIR; S55892; S55892. DR RefSeq; WP_004300839.1; NZ_WQQT01000015.1. DR AlphaFoldDB; P49942; -. DR SMR; P49942; -. DR STRING; 28116.Bovatus_01725; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR GeneID; 29451514; -. DR UniPathway; UPA00114; -. 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; 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 2: Evidence at transcript level; KW Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Signal; Xylan degradation. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..376 FT /note="Endo-1,4-beta-xylanase A" FT /id="PRO_0000007966" FT DOMAIN 25..371 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 160 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 265 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" SQ SEQUENCE 376 AA; 42980 MW; 40C3B36E2DAA3499 CRC64; MKLKRIILLL LTVMFSFSYG EVFAKDGSSL KKALKNKFLI GVSVNTHQSS GKDVAAVEIV KKNFNSIVAE NCMKSSVIHP KENKYNFAQA DEFVSFGESN QMAIIGHCLI WHSQLAPWFC VDKDGNNVSP EVLKKRMKDH ITTIVKRYKG RIKGWDVVNE AIEDNGAYRK TKFYEILGEE YIPLAFQYAH EADPDAELYY NDYSMAQPGR REAVVKMVND LKKRGIRIDA IGMQGHIGMD YPKISEFEKS MLAFAGTGVK IMITELDLTV IPSPNPNVGA EVSASFEYKK EMNPYPDGLP EEVSKAWTER MNDFFRLFLK HHNLITRVTL WGVADQNSWR NDWPMRGRTD YPLLFDRNYQ PKPVVGLIIK EAEKTK //