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Entry: C5BN19_TERTT
LinkDB: C5BN19_TERTT
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ID   C5BN19_TERTT            Unreviewed;      1149 AA.
AC   C5BN19;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-SEP-2017, entry version 51.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=TERTU_0513 {ECO:0000313|EMBL:ACR13391.1};
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR13391.1, ECO:0000313|Proteomes:UP000009080};
RN   [1] {ECO:0000313|EMBL:ACR13391.1, ECO:0000313|Proteomes:UP000009080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G.,
RA   Elshahawi S., Hanora A., Schmidt E.W., Haygood M.G., Posfai J.,
RA   Benner J., Madinger C., Nove J., Anton B., Chaudhary K., Foster J.,
RA   Holman A., Kumar S., Lessard P.A., Luyten Y.A., Slatko B., Wood N.,
RA   Wu B., Teplitski M., Mougous J.D., Ward N., Eisen J.A., Badger J.H.,
RA   Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an
RT   intracellular endosymbiont of marine wood-boring bivalves
RT   (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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}.
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DR   EMBL; CP001614; ACR13391.1; -; Genomic_DNA.
DR   RefSeq; WP_015819505.1; NC_012997.1.
DR   ProteinModelPortal; C5BN19; -.
DR   STRING; 377629.TERTU_0513; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; ACR13391; ACR13391; TERTU_0513.
DR   GeneID; 29649902; -.
DR   KEGG; ttu:TERTU_0513; -.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   OrthoDB; POG091H0Y2G; -.
DR   BioCyc; TTUR377629:GHSU-462-MONOMER; -.
DR   Proteomes; UP000009080; Chromosome.
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; -; 5.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02018; CBM_4_9; 5.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 5.
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:UP000009080};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ACR13391.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ACR13391.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ACR13391.1}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1149       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002948918.
FT   DOMAIN       42    359       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   ACT_SITE    280    280       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1149 AA;  122843 MW;  C6F44ACBF85B53CF CRC64;
     MRFRTKRLGL AMLALGVFPS AAMATSDFSL ELLFPGLSRP APGQVETLAD AAEQSRRLVG
     VAAGYGLVTN DEQFVDIVTG EFNYMTPENS GKWGPLQPAP GVWNFDTHDQ MVEFAGQSEL
     AYKGHALVWH SQAPGFVTDD LSADELQSLI DDHITTVMSR YSGEIRAYDV VNEAMGDDAE
     YRDSVLYRTL GADFIANAFR TAHSVDRRAV LFYNDYNIAG LNAKSDAVYE MVKGLVHNRV
     PIDGVGFQMH LTAATAPSYD ELVANLSRFA NLGLRVNISE LDVRVADLPW DYQTNIAIQR
     QVYHRVVSAC MAVRRCEAVT TWGVSDKNSW INYTFGEDAA LAWDDDNQRK PAYYGMLDGF
     MGVEPDESPL PNLVANSEFE GGVQGWTGEN ADVHRIRAVG KPQANSMLVI GRGSREAGAS
     YDFSDVALAG QSYDISSQVK IPQLSLVPLL SRLFGLARGD TVEMNVRTLC SDGTEELTNL
     ETAFATFGRW QTIGGTVTLP NCEIEAVDLL VNGPRAGTSI QVDSVVARPQ VLVPTAEGFS
     ENLVTNPYFE DGAYDWFGFG SAVVETTTDN VKSGAQSGYV TGRTDSWQGP ATNVTAGVQA
     GDIYDMFAWV QAEGADSRIG ATLKVSCAGE DDSYLNIGNV NVTAGEWALL RGSVLVPDCE
     LLDATLYFEG PAADVNMLID EVYLRRDNKA SDALDIVDDG NLHLNGGFEL GTESWTTWGG
     ALGTSDEYVH SGSAAGVLSS RTASWQGPVF DLLSVASAGG EYEITAWGMV QGVSQDTLNI
     TVKTTCGGES AYHQLASTLV NNTDWTELSG AVTLPSDCDL TEATLYFDGP AVGVDTYLDD
     VFISGEAPSV PNLVINGDFE AGINDWQVWG GVLSVSDDAH TGAQSALHSG RTADWQGPVY
     PLSVVADTDY NVSAFIKIDG AATATANITL KTTCADGSEE YLWGGQAEVN SSGWTELSGV
     VTTTSCEPMD AVVYFSGPAV GIDILLDDVV VWQEGAVVEP PAGNLVANSS FEESLDGWIS
     WGGTLERSAD QAYDGSYSAY LTTRTGDWEG PVYSLLSSVT AGASYDIAAF ARVDAGSAEA
     MNITVKVACD DGSEEYIWAG SAEVNESDWT EVAGSVTLPA CNLTEVSMYF GGPAQAAGIY
     LDQVSVVAL
//
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