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Database: UniProt
Entry: L0EAT5_THECK
LinkDB: L0EAT5_THECK
Original site: L0EAT5_THECK 
ID   L0EAT5_THECK            Unreviewed;      1472 AA.
AC   L0EAT5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-NOV-2017, entry version 29.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   OrderedLocusNames=Theco_0011 {ECO:0000313|EMBL:AGA56270.1};
OS   Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Thermobacillus.
OX   NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA56270.1, ECO:0000313|Proteomes:UP000010795};
RN   [1] {ECO:0000313|Proteomes:UP000010795}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18247 / JCM 13945 / KWC4
RC   {ECO:0000313|Proteomes:UP000010795};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL   Submitted (JAN-2012) 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; CP003255; AGA56270.1; -; Genomic_DNA.
DR   RefSeq; WP_015253038.1; NC_019897.1.
DR   EnsemblBacteria; AGA56270; AGA56270; Theco_0011.
DR   KEGG; tco:Theco_0011; -.
DR   KO; K01181; -.
DR   OMA; IARVTFW; -.
DR   OrthoDB; POG091H0Y2G; -.
DR   BioCyc; TCOM717605:G13HH-11-MONOMER; -.
DR   Proteomes; UP000010795; 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_sf.
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; 3.
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:UP000010795};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AGA56270.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361174,
KW   ECO:0000313|EMBL:AGA56270.1};
KW   Polysaccharide degradation {ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:AGA56270.1}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30   1472       Beta-xylanase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003940896.
FT   DOMAIN      518    865       GH10. {ECO:0000259|PROSITE:PS51760}.
FT   DOMAIN     1291   1354       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1356   1415       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   DOMAIN     1418   1472       SLH. {ECO:0000259|PROSITE:PS51272}.
FT   ACT_SITE    789    789       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU10061}.
SQ   SEQUENCE   1472 AA;  159979 MW;  55A55C449A741D65 CRC64;
     MRGKLRKHVA SLLALLLLIP GGMAAPASAV DDPVVVYHET FEHGIGKTAQ SGGASLQHAT
     GVYFDGNTDG GALYVTNRKN EWDAADYYVS SIPLQTGITY TVTASVYADP ADLNGLDKLT
     IVAAVVTKND QYRQQKSVEL EPGKPATLTE TFTVEDHDKS FRIQTDAAGK ATPFYIGEIK
     FVLTGTGGPD EPDGKVVLSQ SFEDGDYTGW SRKSWGGQGT LEVSSDVASD GSKSLKFTNR
     ESADSQPLLN ATGVMKSGRT YDVSLKVRLG AGSGQFHIAS KINSPLLDNQ YPWLVGNQDV
     TANDWTTFAA KGVEIPADTS EVLLWIESAE SNTLTSDIYI DEVLIVDVTS GGEDPGDVDT
     SGIFDDFESG IGNWVRRFGA GGIEVTQEDN HTEGGKHSLK TTASAQYDGP LLDVHGKMAR
     GHQYELSAWV KMARGEEPTV LRISIQYGES GFANVSPNVT VTDGEWVKLS GRYTQSVTPG
     DHLNAYVEVA NDYGGPRTFL IDDFELKYIG PVAGPNPDFT LPAIKDIYKD QFLIGNIMNP
     GNFDDEIRSK MLKHHYNLLT AENAMKPEYA YKPGTREFDL TDEIALAEQA IANGFKVHGH
     VLVWHSQSPD WLHTQVDANG TPLRDANGNI LYLDKEEALN NLRTHIRTVV KTTGDRVISW
     DVVNEAMNDN PPNPADWRDS LRRSGWYYAI GPDYIYEAYK TAREVIDENG WDIELYYNDY
     NDDNQNKATA IANMVKELNE RYAAETNSDK KLIDGIGMQS HYNLNTNPDN VRASIERIIG
     LGLKVGITEL DVMAGTNGTI TEDQAIRQGW LYAQLFQLYK EYADHITRVT FWGVDDGTSW
     RSENSPLLFD GRYQAKPAYY AVMDPAKFIE DHPPAEKEYQ EGTAAYGTPA VDGTEDAVWS
     RAEELPIARF QTAHNGATGT ARVLWDDRNL YVLIKVQDTA LDQTSDLPYE QDSVEVFLDE
     TNSKAPSYGP GIGQYRVNYE NAATFNPESI AEGFESAVVV NGTNYTVEMK IPFKTITPAN
     GRKIGFDAQI NDAKDGVRQS VAIWNDLTGQ GWQDPSVFGV LTLTGKPQSG GGPSPTPSPA
     PAPEPAVAED GTVTVKPTIA NGRAKASLSG GTLSQALELA AADDTGRKIV VLDIDAEDAE
     AVDVELPAGF LAADEPYVIR LRTPLGIVDL PSNMLAGIAG DAETITIAIS GVDDLELDEA
     VRNRIGDRPA ISLNVLADGE AIAWNNPNAP VTVSIPYEPT AEELANPGHL VVWYIDGEGR
     ATAVPNGRYD AESGAVVFRT THFSVYAVAY VVKTFDDIDR VPWAKQAIEA MASRDIIDGS
     GGSNFDPHAF VTRAEFAALL VRALELKDTG KTVAMFSDVA KTDEFYDEVR IAKQHGIVSG
     NLLNRFNPNS PITRQDMMVM VDLALRAAGR PLPEGGSLLR FKDAGDVAAY ARSSAEKLVA
     AGIVQGAGGT LVPGNRLTRA EAAVILYRIW AH
//
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