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Database: UniProt
Entry: W4QW60_BACA3
LinkDB: W4QW60_BACA3
Original site: W4QW60_BACA3 
ID   W4QW60_BACA3            Unreviewed;       956 AA.
AC   W4QW60;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   22-NOV-2017, entry version 23.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=JCM9157_3285 {ECO:0000313|EMBL:GAE36137.1};
OS   Bacillus akibai (strain ATCC 43226 / DSM 21942 / JCM 9157 / 1139).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1236973 {ECO:0000313|EMBL:GAE36137.1, ECO:0000313|Proteomes:UP000018896};
RN   [1] {ECO:0000313|EMBL:GAE36137.1, ECO:0000313|Proteomes:UP000018896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 9157 {ECO:0000313|EMBL:GAE36137.1,
RC   ECO:0000313|Proteomes:UP000018896};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Three Alkaliphilic Bacillus Strains,
RT   Bacillus wakoensis JCM 9140T, Bacillus akibai JCM 9157T, and Bacillus
RT   hemicellulosilyticus JCM 9152T.";
RL   Genome Announc. 2:e01258-13(2014).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-xylosidic
CC       linkages in xylans. {ECO:0000256|RuleBase:RU361174}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F)
CC       family. {ECO:0000256|RuleBase:RU361174}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAE36137.1}.
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DR   EMBL; BAUV01000028; GAE36137.1; -; Genomic_DNA.
DR   EnsemblBacteria; GAE36137; GAE36137; JCM9157_3285.
DR   Proteomes; UP000018896; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018896};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:GAE36137.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:GAE36137.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018896};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:GAE36137.1}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33    956       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004848953.
FT   DOMAIN      380    714       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   ACT_SITE    637    637       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   956 AA;  107010 MW;  CB1BD03EA3EA41D3 CRC64;
     MSRKFKQFKK ILALLLIAAL VIPTGWVVPV LANSETQTVY HETIKNGDGA AQHSGETLSE
     SNEIAFYDFE DGVQGWAGRG DASVSVTNDG YDGSQALKTT GRTAGWHGPS INVSNLMEKG
     ATYEVSGYAK LVEGQSPSGM KLSANQPGAG NEFPNISGTT PLQVTDSAWV EFKGEYTYDL
     SATSVSLYFE SDNSTVEFIV DNVKVVQTAP APDFGDDGDL DQSGVFSDFE DGVQGWVPRG
     SGYNVVATDA DAFDGSQSLL TNAPEQYQGP LLDVMGKMHP GHIYDLSVWV KMAEGQPDTS
     VRISVQSGSS SFTNVSSDTT ATDEEWVQLS GRFTLNSAPS VLNAYVELVN QPESERLFYI
     DNFELKHIGK VQSEDRPTFN GDLPSIYETY QDQFLIGNAI TMNEFQGVRL EHLKHHHNLI
     TAENVMKPEY YYNRATGEFD FADQDEFVNA AVEEDLKIHG HVLVWHEQSR PELHTVNGTP
     LSREEALANM ETHIETVMTR YGNKVMSWDV VNEAIVVTSN PSEEWEKSLR DTGWKRAIGD
     DYVEQAFRIA KKIVDKNGWD MKLYYNDYND HIKEKAEIMY HMVKDINERY AKENPGEVLI
     SGLGMQGHYN EFTNPDTIRA SLELFTSLEG VEIGVTELDI TSGSADSPQT EAEEIRQAQL
     YAQLFQIYKE YSNEISRVTF WGLDDGASWR GERTPLLFKS NLQPKLAYHA VVNPEKFLED
     YPLGGRVYRQ GEAVYGTPEI NGTIDSVWDN APTLLLDRVS GAWNVRNGYG KVLWDEENLY
     VMIQVYGANL DKSATNAHEQ DSVEVFLDRE NLKTSSYQDG IAQYRVNFDN EASFNPGTDV
     VRQGFESATK ITGNDYVVEM KIPFNETTPE DMKKIGLDLQ INYANNGQRA NFATWNDITG
     QGWNDPSVFG VITLVAPEQD PGTEDREQIQ GKNQEQTNRV RVMETDRIHH QDLRRE
//
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