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Database: UniProt
Entry: Q53317
LinkDB: Q53317
Original site: Q53317 
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   05-DEC-2018, entry version 94.
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; Clostridiales; Ruminococcaceae;
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)-
RT   glucanase domains, encoded by the xynD gene of Ruminococcus
RT   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
CC         xylans.; EC=3.2.1.8;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-
CC         D-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}.
DR   EMBL; S61204; AAB26620.1; -; Genomic_DNA.
DR   ProteinModelPortal; 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   mycoCLAP; ZXG11D_RUMFL; -.
DR   PRIDE; Q53317; -.
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   Gene3D; 2.60.120.180; -; 1.
DR   Gene3D; 2.60.120.260; -; 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;
KW   Multifunctional enzyme; Polysaccharide degradation; Signal;
KW   Xylan degradation.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    802       Xylanase/beta-glucanase.
FT                                /FTId=PRO_0000008009.
FT   DOMAIN       32    239       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   DOMAIN      258    404       CBM-cenC.
FT   DOMAIN      434    513       Dockerin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01102}.
FT   DOMAIN      556    792       GH16. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01098}.
FT   REGION      245    523       B.
FT   REGION      524    555       Linker.
FT   COMPBIAS    524    529       Poly-Thr.
FT   COMPBIAS    532    543       Poly-Thr.
FT   COMPBIAS    546    553       Poly-Thr.
FT   ACT_SITE    124    124       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    226    226       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063, ECO:0000255|PROSITE-
FT                                ProRule:PRU10064}.
FT   ACT_SITE    684    684       Nucleophile. {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
//
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