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Database: UniProt
Entry: G0RUP7
LinkDB: G0RUP7
Original site: G0RUP7 
ID   XYN2_HYPJQ              Reviewed;         223 AA.
AC   G0RUP7; Q02244; Q99015;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   10-APR-2019, entry version 47.
DE   RecName: Full=Endo-1,4-beta-xylanase 2 {ECO:0000303|PubMed:8264524};
DE            Short=Xylanase 2;
DE            EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01097};
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 2;
DE   AltName: Full=Alkaline endo-beta-1,4-xylanase {ECO:0000305|PubMed:8264524};
DE   Flags: Precursor;
GN   Name=xyn2 {ECO:0000303|PubMed:8975597};
GN   Synonyms=xln2 {ECO:0000303|PubMed:8264524};
GN   ORFNames=TRIREDRAFT_123818;
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 [GENOMIC DNA].
RC   STRAIN=QM6a;
RX   PubMed=8264524; DOI=10.1007/BF00279891;
RA   Saarelainen R., Paloheimo M., Fagerstrom R., Suominen P.L.,
RA   Nevalainen K.M.;
RT   "Cloning, sequencing and enhanced expression of the Trichoderma reesei
RT   endoxylanase II (pI 9) gene xln2.";
RL   Mol. Gen. Genet. 241:497-503(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=QM6a;
RX   PubMed=8975597;
RA   la Grange D.C., Pretorius I.S., van Zyl W.H.;
RT   "Expression of a Trichoderma reesei beta-xylanase gene (XYN2) in
RT   Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 62:1036-1044(1996).
RN   [3]
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   [4]
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   [5]
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).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-35 AND THR-61.
RC   STRAIN=QM6a;
RX   PubMed=25434687; DOI=10.1016/j.pep.2014.11.014;
RA   Li Y.Y., Zhong K.X., Hu A.H., Liu D.N., Chen L.Z., Xu S.D.;
RT   "High-level expression and characterization of a thermostable xylanase
RT   mutant from Trichoderma reesei in Pichia pastoris.";
RL   Protein Expr. Purif. 108:90-96(2015).
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:P36217}.
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:P36217};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4-6. {ECO:0000269|PubMed:8975597};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:8975597};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000255|PROSITE-ProRule:PRU01097}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8975597}.
CC   -!- INDUCTION: Induced by D-xylose, dependent on the cellulase and
CC       xylanase regulator xyr1. Repressed by glucose through negative
CC       regulation by the crabon catabolite repressor cre1.
CC       {ECO:0000269|PubMed:23291620}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:8975597}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU01097}.
DR   EMBL; S67387; AAB29346.1; -; Genomic_DNA.
DR   EMBL; U24191; AAB50278.1; -; mRNA.
DR   EMBL; GL985082; EGR45030.1; -; Genomic_DNA.
DR   PIR; S39883; S39883.
DR   RefSeq; XP_006968947.1; XM_006968885.1.
DR   ProteinModelPortal; G0RUP7; -.
DR   SMR; G0RUP7; -.
DR   STRING; 51453.EGR45030; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11C_TRIRE; -.
DR   EnsemblFungi; EGR45030; EGR45030; TRIREDRAFT_123818.
DR   GeneID; 18483743; -.
DR   KEGG; tre:TRIREDRAFT_123818; -.
DR   EuPathDB; FungiDB:TRIREDRAFT_123818; -.
DR   eggNOG; ENOG410JB05; Eukaryota.
DR   eggNOG; ENOG410YH6C; LUCA.
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; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     33       {ECO:0000250|UniProtKB:P36217,
FT                                ECO:0000305|PubMed:9726860}.
FT                                /FTId=PRO_0000436704.
FT   CHAIN        34    223       Endo-1,4-beta-xylanase 2.
FT                                /FTId=PRO_5003409032.
FT   DOMAIN       34    223       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    119    119       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    210    210       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   BINDING     106    106       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     110    110       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     121    121       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     155    155       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     159    159       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     169    169       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     204    204       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   MOD_RES      34     34       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   CARBOHYD     71     71       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   MUTAGEN      35     35       T->C: In Mxyn2: Forms a disulfide bridge
FT                                with C-61, increasing thermal stability
FT                                of the recombinant protein; when
FT                                associated with C-61.
FT                                {ECO:0000269|PubMed:25434687}.
FT   MUTAGEN      61     61       T->C: In Mxyn2: Forms a disulfide bridge
FT                                with C-35, increasing thermal stability
FT                                of the recombinant protein; when
FT                                associated with C-35.
FT   CONFLICT     27     27       S -> P (in Ref. 2; AAB50278).
FT                                {ECO:0000305}.
FT   CONFLICT     48     48       Y -> H (in Ref. 2; AAB50278).
FT                                {ECO:0000305}.
FT   CONFLICT    124    124       E -> G (in Ref. 2; AAB50278).
FT                                {ECO:0000305}.
SQ   SEQUENCE   223 AA;  24069 MW;  79668149EADA22F9 CRC64;
     MVSFTSLLAG VAAISGVLAA PAAEVESVAV EKRQTIQPGT GYNNGYFYSY WNDGHGGVTY
     TNGPGGQFSV NWSNSGNFVG GKGWQPGTKN KVINFSGSYN PNGNSYLSVY GWSRNPLIEY
     YIVENFGTYN PSTGATKLGE VTSDGSVYDI YRTQRVNQPS IIGTATFYQY WSVRRNHRSS
     GSVNTANHFN AWAQQGLTLG TMDYQIVAVE GYFSSGSASI TVS
//
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