ID A0A1C6ZZN8_COLLN Unreviewed; 222 AA. AC A0A1C6ZZN8; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 22-FEB-2023, entry version 21. DE RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|RuleBase:RU362015}; DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU362015}; GN Name=xyl1 {ECO:0000313|EMBL:AKO22614.1}; OS Colletotrichum lindemuthianum (Bean anthracnose fungus) (Glomerella OS lindemuthiana). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum; OC Colletotrichum orbiculare species complex. OX NCBI_TaxID=290576 {ECO:0000313|EMBL:AKO22614.1}; RN [1] {ECO:0000313|EMBL:AKO22614.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=0 {ECO:0000313|EMBL:AKO22614.1}, and 1472 RC {ECO:0000313|EMBL:AIG53790.1}; RA Conejo-Saucedo U., Cano-Camacho H., Lopez-Romero E., Villa-Rivera M.G., RA Lara-Marquez A., Zavala-Paramo M.G.; RT "Cloning and characterization of an endo-beta-1, 4-xylanase gene from RT Colletotrichum lindemuthianum and phylogenetic analysis of similar genes RT from phytopathogenic fungus."; RL Afr J Microbiol Res 10:1292-1305(2016). CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681, CC ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015}; CC -!- PATHWAY: Glycan degradation; xylan degradation. CC {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097, CC ECO:0000256|RuleBase:RU362015}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family. CC {ECO:0000256|ARBA:ARBA00007792, ECO:0000256|PROSITE-ProRule:PRU01097, CC ECO:0000256|RuleBase:RU362015}. 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; KF487129; AIG53790.1; -; mRNA. DR EMBL; KM587707; AKO22614.1; -; mRNA. DR AlphaFoldDB; A0A1C6ZZN8; -. DR SMR; A0A1C6ZZN8; -. DR UniPathway; UPA00114; -. DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule. DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 2.60.120.180; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR013319; GH11/12. DR InterPro; IPR018208; GH11_AS_1. DR InterPro; IPR033119; GH11_AS_2. DR InterPro; IPR033123; GH11_dom. DR InterPro; IPR001137; Glyco_hydro_11. DR PANTHER; PTHR46828:SF3; ENDO-1,4-BETA-XYLANASE; 1. DR PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR Pfam; PF00457; Glyco_hydro_11; 1. DR PRINTS; PR00911; GLHYDRLASE11. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00776; GH11_1; 1. DR PROSITE; PS00777; GH11_2; 1. DR PROSITE; PS51761; GH11_3; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|PROSITE-ProRule:PRU01097}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE- KW ProRule:PRU01097}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01097}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|PROSITE-ProRule:PRU01097}; Signal {ECO:0000256|SAM:SignalP}; KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE- KW ProRule:PRU01097}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..222 FT /note="Endo-1,4-beta-xylanase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015063029" FT DOMAIN 30..219 FT /note="GH11" FT /evidence="ECO:0000259|PROSITE:PS51761" FT ACT_SITE 115 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01097" SQ SEQUENCE 222 AA; 23624 MW; 24FC7D570B814569 CRC64; MVSFTHIVLA LAASAGVIAS PTGELIEKRQ STPSSTGFHN GYYYSWWTDG GSQVTYTNGA GGSYSVNWGG GGGNFVGGKG WNPGGAKTIN YSGTYNPNGN SYLAVYGWTQ NPLIEYYIVE NYGTYNPASQ ATKKGSVTSD GGTYDIYVST RVNQPSIEGT RTFQQYWSIR TSKRTGGTVT TGNHFAAWAK VGLNLGNHNY MIVATEGYFS SGSATITVNT PA //