XYN1_HYPJQ
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 03-AUG-2022, entry version 51.
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; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; 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., 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 [2]
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 [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, 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:P36218}.
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:P36218};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC 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 through
CC negative regulation by the crabon catabolite repressor cre1.
CC {ECO:0000269|PubMed:23291620}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01097}.
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DR EMBL; GL985056; EGR52985.1; -; Genomic_DNA.
DR RefSeq; XP_006961811.1; XM_006961749.1.
DR AlphaFoldDB; G0R947; -.
DR SMR; G0R947; -.
DR STRING; 51453.EGR52985; -.
DR EnsemblFungi; EGR52985; EGR52985; TRIREDRAFT_74223.
DR GeneID; 18488311; -.
DR KEGG; tre:TRIREDRAFT_74223; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_74223; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_052631_0_2_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; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..51
FT /evidence="ECO:0000250|UniProtKB:P36218,
FT ECO:0000305|PubMed:9726860"
FT /id="PRO_0000436703"
FT CHAIN 52..229
FT /note="Endo-1,4-beta-xylanase 1"
FT /id="PRO_5003408111"
FT DOMAIN 42..228
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36217"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
