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Database: UniProt
Entry: E9S8N5_RUMAL
LinkDB: E9S8N5_RUMAL
Original site: E9S8N5_RUMAL 
ID   E9S8N5_RUMAL            Unreviewed;       540 AA.
AC   E9S8N5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-NOV-2017, entry version 34.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU01097};
GN   Name=xyn11F {ECO:0000313|EMBL:AEE64771.1};
GN   ORFNames=CUS_5151 {ECO:0000313|EMBL:EGC04349.1};
OS   Ruminococcus albus 8.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=246199 {ECO:0000313|EMBL:EGC04349.1, ECO:0000313|Proteomes:UP000004259};
RN   [1] {ECO:0000313|EMBL:AEE64771.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=8 {ECO:0000313|EMBL:AEE64771.1};
RX   PubMed=21666020; DOI=10.1128/AEM.00353-11;
RA   Moon Y.H., Iakiviak M., Bauer S., Mackie R.I., Cann I.K.;
RT   "Biochemical Analyses of Multiple Endoxylanases from the Rumen
RT   Bacterium Ruminococcus albus 8 and Their Synergistic Activities with
RT   Accessory Hemicellulose-Degrading Enzymes.";
RL   Appl. Environ. Microbiol. 77:5157-5169(2011).
RN   [2] {ECO:0000313|EMBL:EGC04349.1, ECO:0000313|Proteomes:UP000004259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8 {ECO:0000313|EMBL:EGC04349.1,
RC   ECO:0000313|Proteomes:UP000004259};
RA   Nelson K.E., Sutton G., Torralba M., Durkin S., Harkins D.,
RA   Montgomery R., Ziemer C., Klaassens E., Ocuiv P., Morrison M.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|PROSITE-ProRule:PRU01097}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000256|PROSITE-ProRule:PRU01097}.
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DR   EMBL; JF314320; AEE64771.1; -; Genomic_DNA.
DR   EMBL; ADKM02000030; EGC04349.1; -; Genomic_DNA.
DR   RefSeq; WP_002847376.1; NZ_ADKM02000030.1.
DR   STRING; 246199.CUS_5151; -.
DR   EnsemblBacteria; EGC04349; EGC04349; CUS_5151.
DR   OrthoDB; POG091H0Y2G; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000004259; Unassembled WGS sequence.
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   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004259};
KW   Glycosidase {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Polysaccharide degradation {ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004259};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|PROSITE-ProRule:PRU01097}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    540       Endo-1,4-beta-xylanase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5007913895.
FT   DOMAIN       45    253       GH11. {ECO:0000259|PROSITE:PS51761}.
FT   DOMAIN      449    540       Fibronectin type-III.
FT                                {ECO:0000259|PROSITE:PS50853}.
FT   ACT_SITE    148    148       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    240    240       Proton donor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01097}.
SQ   SEQUENCE   540 AA;  59501 MW;  D9176DDC17F22514 CRC64;
     MKNNVIKRVV SAAIVGMMMT APATVAPFVN TSLTVSAEKV LYTSPQNTRD VGWYNNYHHE
     IWQADTPNSS SMTLHDNDGG FSTTWKCGPN NSKGNFLARR GLFYDLNNPK TWKDYEGFTC
     DFDCSWSAGD SGNSRICIYG WSQNPLVEYY IIEDWKNWNP GMDPSSNYKG SVTIDGSEYK
     VYTSDRYSYT IEGNKNFTQY ISVRQNTRTS GTISISEHFK AWESMGMKMG NFYEVAFNVE
     GWESDGQADV KCTIKEGKTT PTPTPTPEPD ANGDFFTGTF ESVYDNWEGR GDASVALDNK
     NYYSGNQSLF VSGRTSEWNG AAIPLSTSTF VPGSTYSFST GVMQMSGSAT EMKLTMQYKD
     SSGTTQYDQV ASATASNGVW TKLENKAYTI PSGASDLILY VEAPDSLTDF YIDNAAGSKS
     GKASSVTTGG GTVYSSNPSP NPDPNTNTYP TNVWAESNSQ YHQIRFTWDK VENAQNYGIA
     VYLAGRWRIQ TQSISPYTTS YTTPKNLTPG KSYKVAVAAK VNGSWDVANA IKNAIVVTVR
//
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