XYN3_HYPJQ
ID XYN3_HYPJQ Reviewed; 347 AA.
AC G0RA32;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Endo-1,4-beta-xylanase 3;
DE Short=Xylanase 3;
DE EC=3.2.1.8 {ECO:0000255|PROSITE-ProRule:PRU01096};
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 3;
DE Flags: Precursor;
GN Name=xyn3; ORFNames=TRIREDRAFT_120229;
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] {ECO:0007744|PDB:4XV0}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 47-347, AND DISULFIDE BOND.
RC STRAIN=QM6a;
RA Stogios P.J., Xu X., Cui H., Savchenko A.;
RT "Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family
RT 10/GH10) enzyme from Trichoderma reesei.";
RL Submitted (JAN-2015) to the PDB data bank.
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. Produces xylobiose and
CC xylotriose as the main degradation products.
CC {ECO:0000250|UniProtKB:Q9P973}.
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:Q9P973};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01096}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9P973}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9P973}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q9P973}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000255|PROSITE-ProRule:PRU01096}.
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DR EMBL; GL985057; EGR52056.1; -; Genomic_DNA.
DR RefSeq; XP_006962419.1; XM_006962357.1.
DR PDB; 4XV0; X-ray; 1.97 A; A=47-347.
DR PDBsum; 4XV0; -.
DR AlphaFoldDB; G0RA32; -.
DR SMR; G0RA32; -.
DR STRING; 51453.EGR52056; -.
DR EnsemblFungi; EGR52056; EGR52056; TRIREDRAFT_120229.
DR GeneID; 18482826; -.
DR KEGG; tre:TRIREDRAFT_120229; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_120229; -.
DR eggNOG; ENOG502QSCW; Eukaryota.
DR HOGENOM; CLU_020161_2_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 InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..45
FT /evidence="ECO:0000250|UniProtKB:Q9P973"
FT /id="PRO_0000436705"
FT CHAIN 46..347
FT /note="Endo-1,4-beta-xylanase 3"
FT /id="PRO_5003408236"
FT DOMAIN 46..345
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 282
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT MOD_RES 46
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q9P973"
FT DISULFID 300..306
FT /evidence="ECO:0007744|PDB:4XV0"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:4XV0"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4XV0"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:4XV0"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:4XV0"
SQ SEQUENCE 347 AA; 38076 MW; 1AD305498D0216CF CRC64;
MKANVILCLL APLVAALPTE TIHLDPELAA LRANLTERTA DLWDRQASQS IDQLIKRKGK
LYFGTATDRG LLQREKNAAI IQADLGQVTP ENSMKWQSLE NNQGQLNWGD ADYLVNFAQQ
NGKSIRGHTL IWHSQLPAWV NNINNADTLR QVIRTHVSTV VGRYKGKIRA WDVVNEIFNE
DGTLRSSVFS RLLGEEFVSI AFRAARDADP SARLYINDYN LDRANYGKVN GLKTYVSKWI
SQGVPIDGIG SQSHLSGGGG SGTLGALQQL ATVPVTELAI TELDIQGAPT TDYTQVVQAC
LSVSKCVGIT VWGISDKDSW RASTNPLLFD ANFNPKPAYN SIVGILQ
