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Database: UniProt
Entry: D1BXQ7_XYLCX
LinkDB: D1BXQ7_XYLCX
Original site: D1BXQ7_XYLCX 
ID   D1BXQ7_XYLCX            Unreviewed;      1242 AA.
AC   D1BXQ7;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   25-OCT-2017, entry version 50.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Xcel_2684 {ECO:0000313|EMBL:ACZ31698.1};
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:ACZ31698.1, 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:ACZ31698.1, 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; ACZ31698.1; -; Genomic_DNA.
DR   RefSeq; WP_012879440.1; NC_013530.1.
DR   STRING; 446471.Xcel_2684; -.
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; ACZ31698; ACZ31698; Xcel_2684.
DR   KEGG; xce:Xcel_2684; -.
DR   eggNOG; ENOG4105D9F; Bacteria.
DR   eggNOG; COG3693; LUCA.
DR   OrthoDB; POG091H0423; -.
DR   BioCyc; XCEL446471:GHA2-2709-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; -; 2.
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.
DR   InterPro; IPR001000; GH10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
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; 1.
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:ACZ31698.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:ACZ31698.1};
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:ACZ31698.1}.
FT   SIGNAL        1     44       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        45   1242       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003021029.
FT   DOMAIN      381    752       GH10. {ECO:0000259|PROSITE:PS51760}.
SQ   SEQUENCE   1242 AA;  135209 MW;  2700E0EF0A909639 CRC64;
     MHQLLRPGNP RRARTKTWQR VTAAGTAGVL LAGGLLTTAG SAVAAPVEPA YEPTVVGTAE
     DPAAPAELVH TWTFETAADL ATVDANGGVE LSRVPNLDGD GYVLQVARGA DDWRAPVFGA
     GFTEAGALYE LRTDARVSAD APDARLEFRS MGGFGYAGGA DVAADAWTPI VSGEFRAGGT
     VDAIMVQLGG GGAAAGSTYY LDNVELWRLE AAPQVDEDFE FEDLFFDFED GAPGGWFARD
     ASGQGPTLEV VSPGADGSGH ALRVDGRGTQ GDGPMLDVVD LLAPMTRLQF EADIRFVDHA
     DGSGAITLSS QTGASTFTNL VQNMQVGNDW TRVGGEFMMP AFTTVANLYL ETPWQSGAAG
     DTTAFEVDNI RIVEPAPLEW QRYLPGLQET LDIDAVGVAV DSRELSGSHA ELVTHHFNHI
     VGENHMKPES WFAGSSMDTF RRHPEATAML DFAVANDLTL FGHVLVWHSQ TPSWFFQQDG
     RDLQNNPADR AFMEARTVEF FRLIAEDITR DYGLFGTDGN PMNSWEVVNE VVAGNPAVAS
     GMREASPWFR IFGRDFVDMA FRHADAIFNG EFHVDSQDAD APVPHGHPNR ITLWINDYNT
     ERGLGVLNEN TKRWVLFELV NELLENDAPI DGVGHQFHAG LEWPVSGLAD ALNLFAFDNG
     HIHQSRPLLQ AITEVDVTIP GGEATERNLL RQGHYYREAF DIIRAHQAAH GDIDNVTIWG
     LTDGRSWRAA QAPLLFNDDL TAKPAFFGSI YGGLTPELIA AAEEAAGRPI EWALPVLVEA
     ADVFGADVPF DAATFAAPYW THLNPQALGT ADRGFTTRWT PEHLTVLAEI GPSTHATVPS
     RLRITYGELE LVVLRDGSVV TDGDHGIEAL VDGDRFLVRI PHDVAEDDHA SLRVASIHGS
     EQSPLEHGYW NGVVTFREDL SVVEIARTET APLLDGVLDD VWATAPAITT GNRLSGTDEH
     ATADVRTLWY DGEEFDRIYL FAEITDEVVD TSNPDAAAPH TRDSIEFFLS LLNSRDTSYV
     GLYDAQFRIS ADGELTFSSA NAAIHAQRLN AEVALTDTGW VVEASIDLRT DTGHLQGQWN
     TAFGGEGAVF GFDVQVNDAR GGDRVSHASW ADPTGLGWQS TYRWGVARLV DTLETEPEVP
     SYDAWDASRV YLAGDRVVVD GRVFEAQWWT QGQSPDTSGP WGSWMELGAV VTVLDGEPVR
     AWTDSWVFDD GDVVAHDGDV WRARWWTRNQ APGDPHGPWV RL
//
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