ID XYNA_NEOPA Reviewed; 607 AA. AC P29127; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 22-FEB-2023, entry version 122. DE RecName: Full=Bifunctional endo-1,4-beta-xylanase A; DE Short=XYLA; DE EC=3.2.1.8; DE Flags: Precursor; GN Name=XYNA; OS Neocallimastix patriciarum (Rumen fungus). OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota; OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales; OC Neocallimastigaceae; Neocallimastix. OX NCBI_TaxID=4758; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1406248; DOI=10.1111/j.1365-2958.1992.tb01379.x; RA Gilbert H.J., Hazlewood G.P., Laurie J.I., Orpin C.G., Xue G.P.; RT "Homologous catalytic domains in a rumen fungal xylanase: evidence for gene RT duplication and prokaryotic origin."; RL Mol. Microbiol. 6:2065-2072(1992). CC -!- FUNCTION: Hydrolyzes xylans into xylobiose and xylose. 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 11 (cellulase G) 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; X65526; CAA46498.1; -; mRNA. DR PIR; S24754; S24754. DR PDB; 2C1F; X-ray; 2.10 A; A=275-499. DR PDB; 2VG9; X-ray; 2.00 A; A=275-492. DR PDBsum; 2C1F; -. DR PDBsum; 2VG9; -. DR AlphaFoldDB; P29127; -. DR SMR; P29127; -. DR CAZy; GH11; Glycoside Hydrolase Family 11. DR CLAE; XYN11A_NEOPA; -. DR BRENDA; 3.2.1.8; 6834. DR UniPathway; UPA00114; -. DR EvolutionaryTrace; P29127; -. 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; 2.60.120.180; -; 2. DR Gene3D; 3.90.1220.10; Cellulose docking domain, dockering; 2. DR InterPro; IPR002883; CBM10/Dockerin_dom. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR009034; Dockerin_dom_fun_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; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1. DR Pfam; PF02013; CBM_10; 2. DR Pfam; PF00457; Glyco_hydro_11; 2. DR PRINTS; PR00911; GLHYDRLASE11. DR SUPFAM; SSF64571; Cellulose docking domain, dockering; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR PROSITE; PS51763; CBM10; 2. DR PROSITE; PS00776; GH11_1; 2. DR PROSITE; PS00777; GH11_2; 2. DR PROSITE; PS51761; GH11_3; 2. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; KW Multifunctional enzyme; Polysaccharide degradation; Repeat; Signal; KW Xylan degradation. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..607 FT /note="Bifunctional endo-1,4-beta-xylanase A" FT /id="PRO_0000008016" FT DOMAIN 35..242 FT /note="GH11 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097" FT DOMAIN 280..487 FT /note="GH11 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097" FT DOMAIN 523..563 FT /note="CBM10 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099" FT DOMAIN 566..606 FT /note="CBM10 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01099" FT REGION 248..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 493..514 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 141 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062" FT ACT_SITE 223 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063" FT ACT_SITE 386 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062" FT ACT_SITE 474 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063" FT STRAND 275..281 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 292..299 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 327..335 FT /evidence="ECO:0007829|PDB:2VG9" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 345..375 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 385..395 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 403..407 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 410..423 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 426..440 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 443..448 FT /evidence="ECO:0007829|PDB:2VG9" FT HELIX 449..457 FT /evidence="ECO:0007829|PDB:2VG9" FT TURN 458..460 FT /evidence="ECO:0007829|PDB:2VG9" FT STRAND 468..492 FT /evidence="ECO:0007829|PDB:2VG9" SQ SEQUENCE 607 AA; 66175 MW; 9C5B73A67D0CC780 CRC64; MRTIKFFFAV AIATVAKAQW GGGGASAGQR LTVGNGQTQH KGVADGYSYE IWLDNTGGSG SMTLGSGATF KAEWNASVNR GNFLARRGLD FGSQKKATDY SYIGLDYTAT YRQTGSASGN SRLCVYGWFQ NRGVQGVPLV EYYIIEDWVD WVSDAQGRMV TIDGAQYKIF QMDHTGPTIN GGSETFKQYF SVRQQKRTSG HITVSDHFKE WAKQGWGIGN LYEVALNAEG WQSSGIADVT KLDVYTTQKG SNPAPTSTGT VPSSSAGGST ANGKKFTVGN GQNQHKGVND GFSYEIWLDN TGGNGSMTLG SGATFKAEWN AAVNRGNFLA RRGLDFGSQK KATDYDYIGL DYAATYKQTA SASGNSRLCV YGWFQNRGLN GVPLVEYYII EDWVDWVPDA QGKMVTIDGA QYKIFQMDHT GPTINGGSET FKQYFSVRQQ KRTSGHITVS DHFKEWAKQG WGIGNLYEVA LNAEGWQSSG VADVTLLDVY TTPKGSSPAT SAAPRTTTRT TTRTKSLPTN YNKCSARITA QGYKCCSDPN CVVYYTDEDG TWGVENNDWC GCGVEQCSSK ITSQGYKCCS DPNCVVFYTD DDGKWGVENN DWCGCGF //