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Database: UniProt
Entry: G0R947
LinkDB: G0R947
Original site: G0R947 
ID   XYN1_HYPJQ              Reviewed;         229 AA.
AC   G0R947;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   10-APR-2019, entry version 42.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=EX 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01097};
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   AltName: Full=Acidic endo-beta-1,4-xylanase;
DE   Flags: Precursor;
GN   ORFNames=TRIREDRAFT_74223;
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=431241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a;
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M.,
RA   Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D.,
RA   Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P.,
RA   Han C.S., Ho I., Larrondo L.F., de Leon A.L., Magnuson J.K.,
RA   Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A.,
RA   Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L.,
RA   Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R.,
RA   Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M.,
RA   Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus
RT   Trichoderma reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
RN   [2]
RP   SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX   PubMed=9726860;
RA   Goller S.P., Schoisswohl D., Baron M., Parriche M., Kubicek C.P.;
RT   "Role of endoproteolytic dibasic proprotein processing in maturation
RT   of secretory proteins in Trichoderma reesei.";
RL   Appl. Environ. Microbiol. 64:3202-3208(1998).
RN   [3]
RP   INDUCTION.
RX   PubMed=23291620; DOI=10.1128/EC.00182-12;
RA   Herold S., Bischof R., Metz B., Seiboth B., Kubicek C.P.;
RT   "Xylanase gene transcription in Trichoderma reesei is triggered by
RT   different inducers representing different hemicellulosic pentose
RT   polymers.";
RL   Eukaryot. Cell 12:390-398(2013).
CC   -!- FUNCTION: Glycoside hydrolase involved in the hydrolysis of xylan,
CC       a major plant cell wall hemicellulose made up of 1,4-beta-linked
CC       D-xylopyranose residues. Catalyzes the endohydrolysis of the main-
CC       chain 1,4-beta-glycosidic bonds connecting the xylose subunits
CC       yielding various xylooligosaccharides and xylose.
CC       {ECO:0000250|UniProtKB:P36218}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000250|UniProtKB:P36218};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000255|PROSITE-ProRule:PRU01097}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9726860}.
CC   -!- INDUCTION: Induced by D-xylose and L-arabinose, dependent on the
CC       cellulase and xylanase regulator xyr1. Repressed by glucose
CC       through negative regulation by the crabon catabolite repressor
CC       cre1. {ECO:0000269|PubMed:23291620}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU01097}.
DR   EMBL; GL985056; EGR52985.1; -; Genomic_DNA.
DR   RefSeq; XP_006961811.1; XM_006961749.1.
DR   ProteinModelPortal; G0R947; -.
DR   SMR; G0R947; -.
DR   STRING; 51453.EGR52985; -.
DR   EnsemblFungi; EGR52985; EGR52985; TRIREDRAFT_74223.
DR   GeneID; 18488311; -.
DR   KEGG; tre:TRIREDRAFT_74223; -.
DR   EuPathDB; FungiDB:TRIREDRAFT_74223; -.
DR   KO; K01181; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     51       {ECO:0000250|UniProtKB:P36218,
FT                                ECO:0000305|PubMed:9726860}.
FT                                /FTId=PRO_0000436703.
FT   CHAIN        52    229       Endo-1,4-beta-xylanase 1.
FT                                /FTId=PRO_5003408111.
FT   DOMAIN       42    228       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    126    126       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    215    215       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   BINDING     117    117       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     128    128       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     160    160       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     164    164       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     174    174       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     209    209       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
SQ   SEQUENCE   229 AA;  24583 MW;  F9E8BFE1607038DB CRC64;
     MVAFSSLICA LTSIASTLAM PTGLEPESSV NVTERGMYDF VLGAHNDHRR RASINYDQNY
     QTGGQVSYSP SNTGFSVNWN TQDDFVVGVG WTTGSSAPIN FGGSFSVNSG TGLLSVYGWS
     TNPLVEYYIM EDNHNYPAQG TVKGTVTSDG ATYTIWENTR VNEPSIQGTA TFNQYISVRN
     SPRTSGTVTV QNHFNAWASL GLHLGQMNYQ VVAVEGWGGS GSASQSVSN
//
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