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Database: UniProt
Entry: D8DVU6_PREBR
LinkDB: D8DVU6_PREBR
Original site: D8DVU6_PREBR 
ID   D8DVU6_PREBR            Unreviewed;       560 AA.
AC   D8DVU6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-SEP-2017, entry version 37.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=PBR_0377 {ECO:0000313|EMBL:EFI72438.1}, SAMN05444375_11828
GN   {ECO:0000313|EMBL:SEQ96473.1};
OS   Prevotella bryantii B14.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=752555 {ECO:0000313|EMBL:EFI72438.1, ECO:0000313|Proteomes:UP000004524};
RN   [1] {ECO:0000313|EMBL:EFI72438.1, ECO:0000313|Proteomes:UP000004524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B14 {ECO:0000313|EMBL:EFI72438.1,
RC   ECO:0000313|Proteomes:UP000004524};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
RN   [2] {ECO:0000213|PDB:4MGQ}
RP   X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 136-303 IN COMPLEX WITH
RP   CALCIUM.
RX   PubMed=25136124; DOI=10.1073/pnas.1406156111;
RA   Zhang M., Chekan J.R., Dodd D., Hong P.Y., Radlinski L., Revindran V.,
RA   Nair S.K., Mackie R.I., Cann I.;
RT   "Xylan utilization in human gut commensal bacteria is orchestrated by
RT   unique modular organization of polysaccharide-degrading enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:E3708-E3717(2014).
RN   [3] {ECO:0000313|EMBL:SEQ96473.1, ECO:0000313|Proteomes:UP000183837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B14 {ECO:0000313|EMBL:SEQ96473.1,
RC   ECO:0000313|Proteomes:UP000183837};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; ADWO01000043; EFI72438.1; -; Genomic_DNA.
DR   EMBL; FOEM01000018; SEQ96473.1; -; Genomic_DNA.
DR   RefSeq; WP_006282137.1; NZ_FOEM01000018.1.
DR   PDB; 4MGQ; X-ray; 1.68 A; A=136-303.
DR   PDBsum; 4MGQ; -.
DR   ProteinModelPortal; D8DVU6; -.
DR   SMR; D8DVU6; -.
DR   STRING; 752555.PBR_0377; -.
DR   EnsemblBacteria; EFI72438; EFI72438; PBR_0377.
DR   OrthoDB; POG091H0Y2G; -.
DR   Proteomes; UP000004524; Unassembled WGS sequence.
DR   Proteomes; UP000183837; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 2.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 2.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:4MGQ}; Calcium {ECO:0000213|PDB:4MGQ};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004524,
KW   ECO:0000313|Proteomes:UP000183837};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:EFI72438.1}; Metal-binding {ECO:0000213|PDB:4MGQ};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004524};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    560       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010495314.
FT   DOMAIN       41    556       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   METAL       152    152       Calcium; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:4MGQ}.
FT   METAL       251    251       Calcium. {ECO:0000213|PDB:4MGQ}.
FT   METAL       268    268       Calcium; via carbonyl oxygen.
FT                                {ECO:0000213|PDB:4MGQ}.
FT   METAL       270    270       Calcium. {ECO:0000213|PDB:4MGQ}.
SQ   SEQUENCE   560 AA;  62002 MW;  5252BC40A63987D0 CRC64;
     MKVLNSLLYV AAGLSLTACA DQDIPGFTTD EPAEVIAQDE INSYGTLKSY VNRDKYPQFV
     MAGAVNAEQF NQVGQLYSLA KANYDEVVTG NAFKYASVVG SDGTLNTATV ESFVNNATNA
     GLTVFGHTLC WHSQQQVAYL NSLITDPNAT KHVLYIHMGE PKTNNWDREL YVNPTTELQS
     GKTYTLKLRV KTSAACDVTV WPQGDATQYW PTPSFKSTTE WTTVAQAFEA KSALKQLRFE
     LGTLGGDIWM DDVQLLDPDG NNLIANGTFE ENADGWTKPS WHEYEIKTVA DPDQEGGGGG
     MTEEVKKDTL TWALNNFISG MMKACNGKVK AWDVVNEPMS DAAPAELKTA GRDGDPKKCF
     FWQDHLGKDY ARLAVKLARK AASDSVQLKL FINDYNLEAA YNKNAKLQGL IDMIKYWESD
     GVTKIDGIGS QMHVTYSMNP KTQAANEEAY VNHLKMMAAT GKLVRISELD MGIADAEGNT
     INTADVTEEQ QQLMAQYYKF IVSKYFEIIP ANQQYGICNW GLQDSPKGSG WRADEPIGLW
     DANWVRKPAY VGFCEGLKQE
//
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