ID   XYND_RUMFL              Reviewed;         802 AA.
AC   Q53317;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Xylanase/beta-glucanase;
DE   Includes:
DE     RecName: Full=Endo-1,4-beta-xylanase;
DE              Short=Xylanase;
DE              EC=3.2.1.8;
DE   Includes:
DE     RecName: Full=Endo-beta-1,3-1,4 glucanase;
DE              EC=3.2.1.73;
DE     AltName: Full=1,3-1,4-beta-D-glucan 4-glucanohydrolase;
DE     AltName: Full=Lichenase;
DE   Flags: Precursor;
GN   Name=xynD;
OS   Ruminococcus flavefaciens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=17;
RX   PubMed=8491715; DOI=10.1128/jb.175.10.2943-2951.1993;
RA   Flint H.J., Martin J., McPherson C.A., Daniel A.S., Zhang J.-X.;
RT   "A bifunctional enzyme, with separate xylanase and beta(1,3-1,4)-glucanase
RT   domains, encoded by the xynD gene of Ruminococcus flavefaciens.";
RL   J. Bacteriol. 175:2943-2951(1993).
CC   -!- FUNCTION: Contains two catalytic domains with xylanase and endo-
CC       beta-1,3-1,4 glucanase activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-
CC         glucans containing (1->3)- and (1->4)-bonds.; EC=3.2.1.73;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC       hydrolase 11 (cellulase G) family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; S61204; AAB26620.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53317; -.
DR   SMR; Q53317; -.
DR   STRING; 1265.SAMN02910280_1302; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   CLAE; ZXG11D_RUMFL; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042972; F:licheninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02175; GH16_lichenase; 1.
DR   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_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; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
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; PF02018; CBM_4_9; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Multifunctional enzyme;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..802
FT                   /note="Xylanase/beta-glucanase"
FT                   /id="PRO_0000008009"
FT   DOMAIN          32..239
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   DOMAIN          258..404
FT                   /note="CBM-cenC"
FT   DOMAIN          434..513
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01102"
FT   DOMAIN          556..792
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          245..523
FT                   /note="B"
FT   REGION          414..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..555
FT                   /note="Linker"
FT   REGION          533..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063,
FT                   ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        684
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   802 AA;  89091 MW;  2880A689647284AF CRC64;
     MKKSIFKRYA AAVGLMASVL MFTAVPTTSN AADDQKTGKV GGFDWEMWNQ NYTGTVSMNP
     GAGSFTCSWS GIENFLARMG KNYDDQKKNY KAFGDIVLTY DVEYTPRGNS YMCIYGWTRN
     PLMEYYIVEG WGDWEPPGND GVDNFGTTTI DGKTYKIRKS MRYNQPSIEG TKTFPQYWSV
     RTTSGSRNNT TNYMKDQVSV TKHFDAWSKA GLDMSGTLYE VSLNIEGYRS NGSANVKSIS
     FDGGIDIPDP EPIKPDENGY YLKENFESGE GNWSGRGSAK VKSSSGYDGT KGIFVSGRED
     TWNGASINLD ELTFKAGETY SLGTAVMQDF ESSVDFKLTL QYTDADGKEN YDEVKTVTAA
     KGQWVDLSNS SYTIPSGATG LVLYVEVPES KTDFYMDGAY AGVKGTKPLI SISSQSVDPP
     VTEPTNPTNP TGPSVTKWGD ANCDGGVDLS DAIFIMQFLA NPNKYGLTGT ETNHMTNQGK
     VNGDVCEHGS GLTEDDAVSI QKYLIRAISE LPESYLEGHD PSKTTTTTTR ITTTTTTTTT
     TTTSKTTTTT TTTSPAMHGG YRDLGTPMNT SATMISDFRT GKAGDFFASD GWTNGKPFDC
     WWYKRNAVIN DGCLQLSIDQ KWTNDKNPDW DPRYSGGEFR TNNFYHYGYY ECSMQAMKND
     GVVSSFFTYT GPSDDNPWDE IDIEILGKNT TQVQFNYYTN GQGKHEKLYD LGFDSSEAYH
     TYGFDWQPNY IAWYVDGREV YRATQDIPKT PGKIMMNAWP GLTVDDWLKA FNGRTPLTAH
     YQWVTYNKNG VQHSSQGQNP WG
//