ID XYNA_CALSR Reviewed; 684 AA. AC P40944; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 100. 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=xynA; OS Caldicellulosiruptor sp. (strain Rt8B.4). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=28238; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8920183; DOI=10.1007/s002530050653; RA Dwivedi P.P., Gibbs M.D., Saul D.J., Bergquist P.L.; RT "Cloning, sequencing and overexpression in Escherichia coli of a xylanase RT gene, xynA from the thermophilic bacterium Rt8B.4 genus RT Caldicellulosiruptor."; RL Appl. Microbiol. Biotechnol. 45:86-93(1996). 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 -!- 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; L18965; AAB42044.1; -; Genomic_DNA. DR PIR; S41788; S41788. DR AlphaFoldDB; P40944; -. DR SMR; P40944; -. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR CAZy; GH10; Glycoside Hydrolase Family 10. 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; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR003305; CenC_carb-bd. DR InterPro; IPR008979; Galactose-bd-like_sf. 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; PF02018; CBM_4_9; 2. DR Pfam; PF00331; Glyco_hydro_10; 1. DR PRINTS; PR00134; GLHYDRLASE10. DR SMART; SM00633; Glyco_10; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Repeat; Signal; Xylan degradation. FT SIGNAL 1..34 FT /evidence="ECO:0000255" FT CHAIN 35..684 FT /note="Endo-1,4-beta-xylanase A" FT /id="PRO_0000007981" FT DOMAIN 40..190 FT /note="CBM-cenC 1" FT DOMAIN 193..342 FT /note="CBM-cenC 2" FT DOMAIN 350..678 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT ACT_SITE 490 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 598 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" SQ SEQUENCE 684 AA; 78354 MW; 0AE575F4FB4BA5E6 CRC64; MMRSLKSRKL VFILAMLFLI NAIVSLKFIT YSSANQLASK SKYIEYNFEN KSVSPLAKYP SNVVLKVTNS TCAEGTFSVL VAGRKNANDG VIVDITKFLD FSREYEVSFY VLQTTKKLQR ISVTLEILDS NDKNQVIAAE KVLLPNIWTK VSAKVQASNY KKAKRINLIV NMPTSKSDSF YIDLFTIKDL ENAYVLKQEN FENKNTGGFL PEDKNCKITL AKDRAYSSAY SLKVQPSQKT KNGKILFPIK GLLQKGGTYD FSLLVYQDSS KPVNFSAGIK LNDGKSTKEI VLAKQNVAPK KWTQLFATLD LDTRFSAKDV SFFVKPAAAI SYYLDLYSIS DENWGQPVPD YNLPSLCEKY KNYFKIGVAV PYRALTNPVD VEVIKRHFNS ITPENEMKPE SLQPYEGGFS FSIADEYVDF CKKDNISLRG HTLVWHQQTP SWFFTNPETG EKLTNSEKDK EILLDRLKKH IQTVVGRYKG KVYAWDVVNE AIDENQPDGY RRSDWYNILG PEYIEKAFIW AHEADPKAKL FYNDYSTEDP YKREFIYKLI KNLKAKGVPV HGVGLQCHIS LDWPDVSEIE ETVKLFSRIP GLEIHFTEID ISIAKNMTDD DAYNRYLLVQ QAQKLKAIFD VLKKYRNVVT SVTFWGLKDD YSWLRGDMPL LSDKDYQPKF AFWSLIDPSV VPKE //