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Database: UniProt
Entry: D1BXQ6_XYLCX
LinkDB: D1BXQ6_XYLCX
Original site: D1BXQ6_XYLCX 
ID   D1BXQ6_XYLCX            Unreviewed;      1331 AA.
AC   D1BXQ6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   22-NOV-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=Xcel_2683 {ECO:0000313|EMBL:ACZ31697.1};
OS   Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990
OS   / XIL07).
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Xylanimonas.
OX   NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ31697.1, ECO:0000313|Proteomes:UP000002255};
RN   [1] {ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Foster B., Clum A., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.F., Hugenholtz P., Woyke T., Wu D., Gehrich-Schroeter G.,
RA   Schneider S., Pukall S.R., Klenk H.P., Eisen J.A.;
RT   "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ31697.1, ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RX   PubMed=21304672; DOI=10.4056/sigs.571102;
RA   Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA   Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA   Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT   (XIL07).";
RL   Stand. Genomic Sci. 2:1-8(2010).
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; CP001821; ACZ31697.1; -; Genomic_DNA.
DR   ProteinModelPortal; D1BXQ6; -.
DR   STRING; 446471.Xcel_2683; -.
DR   CAZy; CBM22; Carbohydrate-Binding Module Family 22.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; CBM9; Carbohydrate-Binding Module Family 9.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   EnsemblBacteria; ACZ31697; ACZ31697; Xcel_2683.
DR   KEGG; xce:Xcel_2683; -.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   HOGENOM; HOG000101870; -.
DR   KO; K01181; -.
DR   OMA; IGMQMHI; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   BioCyc; XCEL446471:GHA2-2708-MONOMER; -.
DR   Proteomes; UP000002255; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; -; 3.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001000; GH10.
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; SM00495; ChtBD3; 2.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 3.
DR   SUPFAM; SSF51055; SSF51055; 2.
DR   SUPFAM; SSF51445; SSF51445; 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:UP000002255};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ACZ31697.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ACZ31697.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002255};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ACZ31697.1}.
FT   SIGNAL        1     53       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        54   1331       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003021829.
FT   DOMAIN      531    871       GH10. {ECO:0000259|PROSITE:PS51760}.
SQ   SEQUENCE   1331 AA;  140729 MW;  03B2C17FA76A5F28 CRC64;
     MESMLAPKNR RARGGGSPAR ARATGPRGWR QTVASVAAAA VAVGGVVAGG VIAASPATSA
     APTTVTAVDF EDGTTGDWTP SGAATLAVVD SPDGADDGKV LSITRAADYE GIQSPTGIFE
     PGVTYDFSMR ARLGADVTES AGIRFVAKPA YSWIGNTTIT NAEWTTVSGS WTAPADGDPA
     EFQAYLGTAD LTDGGAYEVL VDDILVTTEG PAEPGVTTVA SHDFSTGSLT DAQGVTWAQA
     GITPEFVGDP DDADNTVLSF AQTADWQGLE TPPGVIQNDV EYTISARVRW AEGTTGDVRF
     VSSDGGSAGW SWIGNTAVTD SEWTTIGGTF KVVGFTNPIV RLNAAVEGTL LVDDVVITTP
     STTPDGPTPG TVVIDTDFED QTTQGWTPRQ PDDTTPTLAV VEGGANDTAH AAQVSDRDSD
     GDGLQFDVAA AGVGGATLEF EAWVRFAEGQ PTGELTLSAR TVKDGSASFS NLSAITGVRN
     DGWVKVGGQF AMPTYETEAE IYFEAKYNSG NVSPFLVDEV RVWVPEPPVV DTSLPPLKDT
     IDIPGTGVAI DSRETTGNAS ELLLHHFNQI TPENHMKVEA WYDAEQNFRI HPEAVTLLDF
     AAANDLRLYG HVLLWHSQTP AWFFQREDGT DLTTSEADKQ FLRDRLRTHI DDVAKAITDN
     SGLFGSDTNP MVGIDVVNEV VSDANEAGDG LRRSPWYNLL GEEFISLAFE YADEAFNHTY
     AAEGSDRPVT LFINDYNTEQ SGKQDRYFAL VQRLLAAGVP VDGVGHQFHA SISTPISSLD
     AALARFADLP VVQAVTELDV TIGTPVTQAN LIKQGHWYAE AFDVFRAHAE DLFGVTVWGL
     TDNRSWRAAQ APVLFDAGLQ AKEAYFGAAG LEVSPLLTAA NVFGGDVALD ESAGDDAAWR
     NLPAEPLTGS AGSFVPRWTP EHLTLLVSVA SDASDAVEVE LDGTVVSIAK DGTVSGGAEG
     LVIDDEGDGW RAVLQVPLSG VAEGDSAQLD VRVSAAGTAV GAWNSPGSTG TLTFLEELST
     VDVVEAAEAP VVDGVIDAAW ADANVVTTAK TVEGAADGAT AEVRTLWAGE DTLYVLAEVT
     DAVVDVSSPD PWNQDSLELF LDLGNTKSGN YGPNDAQMRI SAQNATSFGT GDAATQAARL
     TSATTLTDTG YVVELAVVLR GQSGGQDDVP FGGADTFQGL DFQVNDGRNG SRYAVHTWAE
     PTGTGYQSTA RWGVGHLVEA AAPEVPEYDA WDASRVYLAG DRVVVDGRVF EAQWWTQNQS
     PVTSGPWGSW MELGAVVGTF DGEPVRAWTN SWVFDNGDVV AHDGDVWRAR WWTRNQPPGD
     VYGPWERIGS L
//
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