XYN2_HYPJQ
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 03-AUG-2022, entry version 57.
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}; ORFNames=TRIREDRAFT_123818;
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; 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; DOI=10.1128/aem.62.3.1036-1044.1996;
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., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
RN [4]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=9726860; DOI=10.1128/aem.64.9.3202-3208.1998;
RA Goller S.P., Schoisswohl D., Baron M., Parriche M., Kubicek C.P.;
RT "Role of endoproteolytic dibasic proprotein processing in maturation of
RT 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, a
CC major plant cell wall hemicellulose made up of 1,4-beta-linked D-
CC xylopyranose residues. Catalyzes the endohydrolysis of the main-chain
CC 1,4-beta-glycosidic bonds connecting the xylose subunits yielding
CC various xylooligosaccharides and xylose.
CC {ECO:0000250|UniProtKB:P36217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC 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. {ECO:0000255|PROSITE-
CC ProRule:PRU01097}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8975597}.
CC -!- INDUCTION: Induced by D-xylose, dependent on the cellulase and xylanase
CC regulator xyr1. Repressed by glucose through negative regulation by the
CC crabon catabolite repressor cre1. {ECO:0000269|PubMed:23291620}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8975597}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01097}.
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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 AlphaFoldDB; G0RUP7; -.
DR SMR; G0RUP7; -.
DR STRING; 51453.EGR45030; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11C_TRIRE; -.
DR EnsemblFungi; EGR45030; EGR45030; TRIREDRAFT_123818.
DR GeneID; 18483743; -.
DR KEGG; tre:TRIREDRAFT_123818; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_123818; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_0_1; -.
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; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..33
FT /evidence="ECO:0000250|UniProtKB:P36217,
FT ECO:0000305|PubMed:9726860"
FT /id="PRO_0000436704"
FT CHAIN 34..223
FT /note="Endo-1,4-beta-xylanase 2"
FT /id="PRO_5003409032"
FT DOMAIN 34..223
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT MOD_RES 34
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 35
FT /note="T->C: In Mxyn2: Forms a disulfide bridge with C-61,
FT increasing thermal stability of the recombinant protein;
FT when associated with C-61."
FT /evidence="ECO:0000269|PubMed:25434687"
FT MUTAGEN 61
FT /note="T->C: In Mxyn2: Forms a disulfide bridge with C-35,
FT increasing thermal stability of the recombinant protein;
FT when associated with C-35."
FT CONFLICT 27
FT /note="S -> P (in Ref. 2; AAB50278)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="Y -> H (in Ref. 2; AAB50278)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="E -> G (in Ref. 2; AAB50278)"
FT /evidence="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
