ID XYNA_THEMA Reviewed; 1059 AA. AC Q60037; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 159. 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; OrderedLocusNames=TM_0061; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=7783614; DOI=10.1111/j.1365-2958.1995.tb02257.x; RA Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W.; RT "Identification of a novel cellulose-binding domain within the multidomain RT 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga RT maritima."; RL Mol. Microbiol. 15:431-444(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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 6.2.; CC Temperature dependence: CC Optimum temperature is 90 degrees Celsius. Thermostable.; CC -!- DOMAIN: The C-terminal CBM-CenC domains mediate the binding of XynA to CC microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose CC binding. 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; Z46264; CAA86406.1; -; Genomic_DNA. DR EMBL; AE000512; AAD35155.1; -; Genomic_DNA. DR PIR; S61311; S61311. DR RefSeq; NP_227877.1; NC_000853.1. DR RefSeq; WP_004082550.1; NZ_CP011107.1. DR PDB; 1I82; X-ray; 1.90 A; A=871-1059. DR PDB; 1I8A; X-ray; 1.90 A; A=871-1059. DR PDB; 1I8U; X-ray; 1.90 A; A=871-1059. DR PDBsum; 1I82; -. DR PDBsum; 1I8A; -. DR PDBsum; 1I8U; -. DR AlphaFoldDB; Q60037; -. DR SMR; Q60037; -. DR STRING; 243274.TM_0061; -. DR DrugBank; DB02379; Beta-D-Glucose. DR CAZy; CBM22; Carbohydrate-Binding Module Family 22. DR CAZy; CBM9; Carbohydrate-Binding Module Family 9. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR PaxDb; 243274-THEMA_04500; -. DR EnsemblBacteria; AAD35155; AAD35155; TM_0061. DR KEGG; tma:TM0061; -. DR eggNOG; COG3693; Bacteria. DR InParanoid; Q60037; -. DR OrthoDB; 9809277at2; -. DR BioCyc; MetaCyc:MONOMER-16897; -. DR BRENDA; 3.2.1.8; 6331. DR EvolutionaryTrace; Q60037; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW. DR CDD; cd00005; CBM9_like_1; 1. DR CDD; cd00241; DOMON_like; 1. DR Gene3D; 2.60.40.1190; -; 2. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR010502; Carb-bd_dom_fam9. 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; PF06452; CBM9_1; 2. 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; SSF49344; CBD9-like; 2. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS00591; GH10_1; 1. DR PROSITE; PS51760; GH10_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Repeat; Signal; KW Xylan degradation. FT SIGNAL 1..30 FT /evidence="ECO:0000255" FT CHAIN 31..1059 FT /note="Endo-1,4-beta-xylanase A" FT /id="PRO_0000007986" FT DOMAIN 364..692 FT /note="GH10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096" FT DOMAIN 700..870 FT /note="CBM-cenC 1" FT DOMAIN 871..1059 FT /note="CBM-cenC 2" FT REGION 47..199 FT /note="A-1" FT REGION 200..354 FT /note="A-2" FT ACT_SITE 502 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 608 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10061" FT STRAND 872..877 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 882..885 FT /evidence="ECO:0007829|PDB:1I82" FT HELIX 888..892 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 895..897 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 900..904 FT /evidence="ECO:0007829|PDB:1I82" FT TURN 906..908 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 911..918 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 920..930 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 938..940 FT /evidence="ECO:0007829|PDB:1I82" FT HELIX 941..943 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 944..952 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 965..971 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 976..978 FT /evidence="ECO:0007829|PDB:1I82" FT HELIX 984..986 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 987..994 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 997..1005 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 1015..1026 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 1032..1039 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 1041..1043 FT /evidence="ECO:0007829|PDB:1I82" FT TURN 1045..1047 FT /evidence="ECO:0007829|PDB:1I82" FT HELIX 1049..1051 FT /evidence="ECO:0007829|PDB:1I82" FT STRAND 1052..1058 FT /evidence="ECO:0007829|PDB:1I82" SQ SEQUENCE 1059 AA; 119643 MW; 045936844A2D72E2 CRC64; MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE TVLALSFEGT TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE IDLTGKVKSG ADYLLSFQVY QSSDAPQLFN VVARTEDEKG ERYDVILDKV VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA SKNTNFNFYL DKVQVLAPKE SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL FISNRQKGWQ GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV DTTSAEIKIE MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK HFNSITAENE MKPESLLAGI ENGKLKFRFE TADKYIQFVE ENGMVIRGHT LVWHNQTPDW FFKDENGNLL SKEAMTERLK EYIHTVVGHF KGKVYAWDVV NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA KLFYNDYNTF EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI TNVTFWGLKD DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK ESRISEGEAV VVGMMDDSYL MSKPIEILDE EGNVKATIRA VWKDSTIYIY GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ PDDTYAVLWT NWKTEVNRED VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI DDGKWYSWSD TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF IDENNHKTGY YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV EAAIKWKTIK PTPNTVIGFN IQVNDANEKG QRVGIISWSD PTNNSWRDPS KFGNLRLIK //