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Database: UniProt
Entry: A0A089IE77_9BACL
LinkDB: A0A089IE77_9BACL
Original site: A0A089IE77_9BACL 
ID   A0A089IE77_9BACL        Unreviewed;      1485 AA.
AC   A0A089IE77;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 22.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=H70737_07200 {ECO:0000313|EMBL:AIQ22656.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22656.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ22656.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22656.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) 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; CP009279; AIQ22656.1; -; Genomic_DNA.
DR   RefSeq; WP_042185887.1; NZ_CP009279.1.
DR   EnsemblBacteria; AIQ22656; AIQ22656; H70737_07200.
DR   KEGG; paej:H70737_07200; -.
DR   KO; K01181; -.
DR   Proteomes; UP000029519; Chromosome.
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; 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   InterPro; IPR001119; SLH_dom.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF00395; SLH; 3.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF49785; SSF49785; 3.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361174};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029519};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AIQ22656.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AIQ22656.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:AIQ22656.1}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33   1485       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001843602.
FT   DOMAIN      522    859       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1304   1364       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1365   1428       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1431   1485       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   ACT_SITE    783    783       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1485 AA;  161457 MW;  1136150EAC172EF0 CRC64;
     MSRMFKQVIS ILLAAALLIP SSWLAPITEA AAPDAIVPSD SVMVYHETFA NGKGIAGQSG
     SASLTPVTDK AFAGNADGAA LYVSNRTNNY DAVDFKFSDM GLENGKTYMV TASVYVDADV
     TVPSGAQAYL QTINSYGLLA SVNYEAGKAI TLTKEFTVDT SENTTLRILS DEIGKAVPFY
     IGDVLITAKK AVTETDKEIY HESFVSGKGL ATQSGSANLT AVTGKVFAGN ADGAALYVSD
     RTNDWDAADF TFSDIGLKNG KTYTVTATVY VDPDVTVPSG AQAYIQAIGS YALLASGDYE
     AGKGITLTKE FIVDTSKDTK LRVQSNAIGK AVPFYIGDVL VTEKVTAEPT PLPTPEPPRD
     PALPFTTVTF EDQKAGGFEG RAGSETLTIT DDENHTDNGS YALKVEGRTS TWHGPSLRVE
     KYVDKGYEYK ISLWVKLIQP ASSQLQLSTQ VGNGSSANYV QLAPKTISAN DGWVQFEGTY
     RYNNVSSEYL TIYVESSSNS TASFYIDDIS FEKTGSGPVG IQKDLIPIKD AYEDHFLIGN
     AISAEDLEGV RLDLLKMHHN VATAGNAMKP DALQPTKGNF TFTGADELVD KVLHEGMQMH
     GHVLVWHQQS PAWMNTTSDA DNNTIPLGRD EALDNMRTHI KTVMEHFGDK VISWDVVNEA
     MSDNPSNPTD WKTALRSAPW KSAIGADYVE QAFLAAREVL DANPDWNIKL YYNDYNEDNQ
     NKAQAIYSMV KEINDKYALT HPGKLLIDGV GMQAHYSINT NPENVERSLE KFISLGVEVS
     ITELDIQAGS NYQLSEKLAN AQGYLYAQLL NIFRANDEHI KRVTFWGMDD NTSWRASSNP
     LLFDKNLQAK PAYYGVIDPD TFIEEHEPET VEANHSTAKF AAPVIDGTVD EIWSQTAEMP
     INRYQTAWQG ASGVAKALWD DQNLYVLIQV SDTQLDKSSV NAHEQDSVEI FVDQNNGKTT
     FYQEDDGQYR VNFDNETSFN PTSIAAGFES ATHISGTNYT VEVKIPLHGI TPDDDTKLGF
     DVQINDAKDG SRQSVAAWND TTGTGYMDTS VYGVLTLKGK STDTEPTPTP TPTPTNEPTG
     SSNTGSAVTT PQPVAIANKD GVVTITLEVK SDNGRAIGTI SSDNLKKALE QATAAANGKK
     QIVIEVPKQT DAKVYDIQLP TQSLMGKENF ELLLKTENAT IQIPSNMLPD LTDHAEQVSI
     RISKVSADSL SAATRNLIGS HPVIDLSVVS GDKVIPWNNP NAPVTVSIPY TPTAEELSNP
     DLIVVWYIDD KGNVVPVPNG RYDAATQTVV FQTTHFSIYA VTFVKKNFGD LQNVSWAKQA
     IDVMAARDVI QGTSVNSFSP ADSMKRADFI ALLVRALELK GTGKSAALFS DVQKTDYYYD
     ELVIAKELGI ATGFEDDTFR PNIEVSRQDM MVLTARALAA SGKQIKASGT LNAYLDEASI
     SSYAKDSALL LVKFGVVNGK NDRIAPNDTL TRAEAAVILY RIWKL
//
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