ID A4XM50_CALS8 Unreviewed; 337 AA. AC A4XM50; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 82. DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174}; DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174}; GN OrderedLocusNames=Csac_2408 {ECO:0000313|EMBL:ABP67985.1}; OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T OS 6331). OC Bacteria; Bacillati; Bacillota; Bacillota incertae sedis; OC Caldicellulosiruptorales; Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP67985.1, ECO:0000313|Proteomes:UP000000256}; RN [1] {ECO:0000313|EMBL:ABP67985.1, ECO:0000313|Proteomes:UP000000256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331 RC {ECO:0000313|Proteomes:UP000000256}; RX PubMed=18776029; DOI=10.1128/AEM.00968-08; RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K., RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E., RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J., RA Kelly R.M., Kengen S.W.; RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor RT saccharolyticus."; RL Appl. Environ. Microbiol. 74:6720-6729(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; Evidence={ECO:0000256|PROSITE-ProRule:PRU01096, CC ECO:0000256|RuleBase:RU361174}; CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000256|PROSITE- CC ProRule:PRU01096}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. CC {ECO:0000256|PROSITE-ProRule:PRU01096, ECO:0000256|RuleBase:RU361174}. 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; CP000679; ABP67985.1; -; Genomic_DNA. DR AlphaFoldDB; A4XM50; -. DR SMR; A4XM50; -. DR STRING; 351627.Csac_2408; -. DR CAZy; GH10; Glycoside Hydrolase Family 10. DR KEGG; csc:Csac_2408; -. DR eggNOG; COG3693; Bacteria. DR HOGENOM; CLU_020161_6_1_9; -. DR Proteomes; UP000000256; Chromosome. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. 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. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PROSITE-ProRule:PRU01096}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU01096}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01096}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|PROSITE-ProRule:PRU01096}; KW Reference proteome {ECO:0000313|Proteomes:UP000000256}; KW Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01096}. FT DOMAIN 6..337 FT /note="GH10" FT /evidence="ECO:0000259|PROSITE:PS51760" FT ACT_SITE 139 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01096" FT ACT_SITE 247 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061" SQ SEQUENCE 337 AA; 39871 MW; B266A1B3740CC108 CRC64; MCENLEMLNL SLAKTYKDYF KIGAAVTAKD LEGVHRDILL KHFNSLTPEN AMKFENIHPE EQRYNFEEVA RIKEFAIKND MKLRGHTFVW HNQTPGWVFL DKNGEEASKE LVIERLREHI KTLCERYKDV VYAWDVVNEA VEDKTEKLLR ESNWRKIIGD DYIKIAFEIA REYAGDAKLF YNDYNNEMPY KLEKTYKVLK ELLERGTPID GIGIQAHWNI WDKNLVSNLK KAIEVYASLG LEIHITELDI SVFEFEDKRT DLFEPTPEML ELQAKVYEDV FAVFREYKDV ITSVTLWGIS DRHTWKDNFP VKGRKDWPLL FDVNGKPKEA LYRILRF //