XYND_RUMFL
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 03-AUG-2022, entry version 101.
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; Firmicutes; 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-beta-
CC 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 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 PRIDE; Q53317; -.
DR UniPathway; UPA00114; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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 Gene3D; 1.10.1330.10; -; 1.
DR Gene3D; 2.60.120.180; -; 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 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; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF63446; SSF63446; 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
