XYN2_HYPJR
ID XYN2_HYPJR Reviewed; 223 AA.
AC P36217; A0A024RZG2; B2CNY5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Endo-1,4-beta-xylanase 2 {ECO:0000303|PubMed:1369024};
DE Short=EX 2 {ECO:0000303|PubMed:7988708};
DE Short=Xylanase 2 {ECO:0000303|Ref.5};
DE EC=3.2.1.8 {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.5};
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase 2 {ECO:0000303|PubMed:1369024};
DE AltName: Full=Alkaline endo-beta-1,4-xylanase {ECO:0000303|PubMed:7988708};
DE Flags: Precursor;
GN Name=xyn2 {ECO:0000303|PubMed:1369024}; ORFNames=M419DRAFT_124931;
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-42; 49-60; 83-89;
RP 120-152; 168-171; 205-211 AND 213-217, PYROGLUTAMATE FORMATION AT GLN-34,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=1369024; DOI=10.1038/nbt1192-1461;
RA Toerroenen A., Mach R.L., Messner R., Gonzalez R., Kalkkinen N., Harkki A.,
RA Kubicek C.P.;
RT "The two major xylanases from Trichoderma reesei: characterization of both
RT enzymes and genes.";
RL Biotechnology (N.Y.) 10:1461-1465(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=17416973; DOI=10.1007/bf02685934;
RA Tung M.Y., Chang C.T., Chung Y.C.;
RT "Biochemical properties of genetic recombinant xylanase II.";
RL Appl. Biochem. Biotechnol. 136:1-16(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-223, AND FUNCTION.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=19556747; DOI=10.1159/000226590;
RA He J., Yu B., Zhang K., Ding X., Chen D.;
RT "Sequencing and expression of the xylanase gene 2 from Trichoderma reesei
RT Rut C-30 and characterization of the recombinant enzyme and its activity on
RT xylan.";
RL J. Mol. Microbiol. Biotechnol. 17:101-109(2009).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1016/0141-0229(92)90128-B;
RA Tenkanen M., Puls J., Poutanen K.;
RT "Two major xylanases of Trichoderma reesei.";
RL Enzyme Microb. Technol. 14:566-574(1992).
RN [6]
RP FUNCTION.
RX PubMed=7988708; DOI=10.1016/0014-5793(94)01248-2;
RA Biely P., Kremnicky L., Alfoeldi J., Tenkanen M.;
RT "Stereochemistry of the hydrolysis of glycosidic linkage by endo-beta-1,4-
RT xylanases of Trichoderma reesei.";
RL FEBS Lett. 356:137-140(1994).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=17475200; DOI=10.1016/j.ab.2007.03.034;
RA Jaenis J., Pulkkinen P., Rouvinen J., Vainiotalo P.;
RT "Determination of steady-state kinetic parameters for a xylanase-catalyzed
RT hydrolysis of neutral underivatized xylooligosaccharides by mass
RT spectrometry.";
RL Anal. Biochem. 365:165-173(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=8013449; DOI=10.1002/j.1460-2075.1994.tb06536.x;
RA Toerroenen A., Harkki A., Rouvinen J.;
RT "Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma
RT reesei: two conformational states in the active site.";
RL EMBO J. 13:2493-2501(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=7827044; DOI=10.1021/bi00003a019;
RA Toerroenen A., Rouvinen J.;
RT "Structural comparison of two major endo-1,4-xylanases from Trichoderma
RT reesei.";
RL Biochemistry 34:847-856(1995).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=8755744; DOI=10.1021/bi953052n;
RA Havukainen R., Toerroenen A., Laitinen T., Rouvinen J.;
RT "Covalent binding of three epoxyalkyl xylosides to the active site of endo-
RT 1,4-xylanase II from Trichoderma reesei.";
RL Biochemistry 35:9617-9624(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
RP GLN-34.
RX PubMed=16790934; DOI=10.1107/s0907444906017379;
RA Watanabe N., Akiba T., Kanai R., Harata K.;
RT "Structure of an orthorhombic form of xylanase II from Trichoderma reesei
RT and analysis of thermal displacement.";
RL Acta Crystallogr. D 62:784-792(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=24419374; DOI=10.1107/s1399004713023626;
RA Wan Q., Zhang Q., Hamilton-Brehm S., Weiss K., Mustyakimov M., Coates L.,
RA Langan P., Graham D., Kovalevsky A.;
RT "X-ray crystallographic studies of family 11 xylanase Michaelis and product
RT complexes: implications for the catalytic mechanism.";
RL Acta Crystallogr. D 70:11-23(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS), AND ACTIVE SITES.
RX PubMed=26392527; DOI=10.1073/pnas.1504986112;
RA Wan Q., Parks J.M., Hanson B.L., Fisher S.Z., Ostermann A., Schrader T.E.,
RA Graham D.E., Coates L., Langan P., Kovalevsky A.;
RT "Direct determination of protonation states and visualization of hydrogen
RT bonding in a glycoside hydrolase with neutron crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:12384-12389(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 (PubMed:1369024, Ref.5). The
CC catalysis proceeds by a double-displacement reaction mechanism with a
CC putative covalent glycosyl-enzyme intermediate, with retention of the
CC anomeric configuration (PubMed:7988708). Produces xylobiose and xylose
CC as the main degradation products (PubMed:19556747).
CC {ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:19556747,
CC ECO:0000269|PubMed:7988708, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:1369024, ECO:0000269|Ref.5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mg/ml for beechwood (unsubstituted) xylan
CC {ECO:0000269|PubMed:1369024};
CC KM=13.8 mg/ml for birchwood xylan {ECO:0000269|PubMed:17416973};
CC KM=3.0 mg/ml for acetylated glucuronoxylan {ECO:0000269|Ref.5};
CC KM=3.8 mg/ml for deacetylated glucuronoxylan {ECO:0000269|Ref.5};
CC KM=6.8 mg/ml for unsubstituted xylan {ECO:0000269|Ref.5};
CC KM=73 uM for xylohexaose {ECO:0000269|PubMed:17475200};
CC KM=136 uM for xylopentaose {ECO:0000269|PubMed:17475200};
CC Vmax=1600 umol/min/mg enzyme for beechwood xylan
CC {ECO:0000269|PubMed:1369024};
CC Vmax=336 umol/min/mg enzyme for birchwood xylan
CC {ECO:0000269|PubMed:17416973};
CC Note=kcat is 68 sec(-1) with xylohexaose, 50.3 sec(-1) with
CC xylopentaose, 0.162 sec(-1) with xylotetraose and 0.045 sec(-1) with
CC xylotriose as substrate. {ECO:0000269|PubMed:17475200};
CC pH dependence:
CC Optimum pH is 4.5-5.5 (PubMed:1369024). Stable from pH 3.0 to 8.5 at
CC room temperature and from pH 4.0 to 7.5 at 40 degrees Celsius
CC (Ref.5). {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.5};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01097}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.5}.
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:0000250|UniProtKB:G0RUP7}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
CC -!- CAUTION: In PubMed:1369024 Figure 2, this sequence is erroneously
CC labeled xyn1, but in the remainder of the paper and all subsequent
CC publications, this protein is referred to as xylanase 2 (xyn2).
CC {ECO:0000305|PubMed:1369024}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49293.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X69573; CAA49293.1; ALT_FRAME; Genomic_DNA.
DR EMBL; EU532196; ACB38137.1; -; mRNA.
DR EMBL; KI911164; ETR98242.1; -; Genomic_DNA.
DR PIR; S39154; S39154.
DR PDB; 1ENX; X-ray; 1.50 A; A/B=35-223.
DR PDB; 1RED; X-ray; 1.60 A; A/B=35-223.
DR PDB; 1REE; X-ray; 1.60 A; A/B=35-223.
DR PDB; 1REF; X-ray; 1.80 A; A/B=35-223.
DR PDB; 1XYO; X-ray; 1.50 A; A/B=35-223.
DR PDB; 1XYP; X-ray; 1.50 A; A/B=35-223.
DR PDB; 2D97; X-ray; 2.01 A; A=35-223.
DR PDB; 2D98; X-ray; 2.00 A; A=35-223.
DR PDB; 2DFB; X-ray; 1.11 A; A=34-223.
DR PDB; 2DFC; X-ray; 1.19 A; A=34-223.
DR PDB; 3LGR; X-ray; 1.64 A; A=35-223.
DR PDB; 4HK8; X-ray; 1.15 A; A=35-223.
DR PDB; 4HK9; X-ray; 1.55 A; A=36-223.
DR PDB; 4HKL; X-ray; 1.10 A; A=35-223.
DR PDB; 4HKO; X-ray; 1.50 A; A=35-223.
DR PDB; 4HKW; X-ray; 1.65 A; A=35-223.
DR PDB; 4S2D; Other; 1.60 A; A=35-223.
DR PDB; 4S2F; Other; 1.70 A; A=35-223.
DR PDB; 4S2G; Other; 1.60 A; A=35-223.
DR PDB; 4S2H; Other; 1.60 A; A=35-223.
DR PDB; 4XPV; Other; 1.70 A; A=35-223.
DR PDB; 4XQ4; X-ray; 1.25 A; A/B=35-223.
DR PDB; 4XQD; X-ray; 1.50 A; A/B=35-223.
DR PDB; 4XQW; X-ray; 1.50 A; A=35-223.
DR PDB; 5K7P; EM; 2.30 A; A=34-223.
DR PDB; 5ZF3; X-ray; 1.20 A; A=35-223.
DR PDB; 5ZH0; X-ray; 1.08 A; A=35-223.
DR PDB; 5ZH9; X-ray; 1.15 A; A=35-223.
DR PDB; 5ZII; X-ray; 1.30 A; A=35-223.
DR PDB; 5ZIW; X-ray; 1.30 A; A=35-223.
DR PDB; 5ZKZ; X-ray; 1.30 A; A=35-223.
DR PDB; 5ZO0; Neutron; 1.65 A; A=35-223.
DR PDB; 6JUG; X-ray; 1.19 A; A=35-223.
DR PDB; 6JWB; X-ray; 1.15 A; A=35-223.
DR PDB; 6JXL; X-ray; 1.30 A; A=35-223.
DR PDB; 6JZP; X-ray; 1.12 A; A=35-223.
DR PDB; 6K9O; X-ray; 1.06 A; A=35-223.
DR PDB; 6K9R; X-ray; 1.30 A; A=35-223.
DR PDB; 6K9W; X-ray; 1.10 A; A=35-223.
DR PDB; 6K9X; X-ray; 1.20 A; A=35-223.
DR PDB; 6KVV; X-ray; 1.19 A; A=35-223.
DR PDB; 6KW9; X-ray; 1.22 A; A=35-223.
DR PDB; 6KWC; X-ray; 1.30 A; A=35-223.
DR PDB; 6KWD; X-ray; 1.30 A; A=35-223.
DR PDB; 6KWE; X-ray; 1.50 A; A=35-223.
DR PDB; 6KWF; X-ray; 1.22 A; A=35-223.
DR PDB; 6KWG; X-ray; 1.69 A; A=35-223.
DR PDB; 6KWH; X-ray; 1.81 A; A=35-223.
DR PDBsum; 1ENX; -.
DR PDBsum; 1RED; -.
DR PDBsum; 1REE; -.
DR PDBsum; 1REF; -.
DR PDBsum; 1XYO; -.
DR PDBsum; 1XYP; -.
DR PDBsum; 2D97; -.
DR PDBsum; 2D98; -.
DR PDBsum; 2DFB; -.
DR PDBsum; 2DFC; -.
DR PDBsum; 3LGR; -.
DR PDBsum; 4HK8; -.
DR PDBsum; 4HK9; -.
DR PDBsum; 4HKL; -.
DR PDBsum; 4HKO; -.
DR PDBsum; 4HKW; -.
DR PDBsum; 4S2D; -.
DR PDBsum; 4S2F; -.
DR PDBsum; 4S2G; -.
DR PDBsum; 4S2H; -.
DR PDBsum; 4XPV; -.
DR PDBsum; 4XQ4; -.
DR PDBsum; 4XQD; -.
DR PDBsum; 4XQW; -.
DR PDBsum; 5K7P; -.
DR PDBsum; 5ZF3; -.
DR PDBsum; 5ZH0; -.
DR PDBsum; 5ZH9; -.
DR PDBsum; 5ZII; -.
DR PDBsum; 5ZIW; -.
DR PDBsum; 5ZKZ; -.
DR PDBsum; 5ZO0; -.
DR PDBsum; 6JUG; -.
DR PDBsum; 6JWB; -.
DR PDBsum; 6JXL; -.
DR PDBsum; 6JZP; -.
DR PDBsum; 6K9O; -.
DR PDBsum; 6K9R; -.
DR PDBsum; 6K9W; -.
DR PDBsum; 6K9X; -.
DR PDBsum; 6KVV; -.
DR PDBsum; 6KW9; -.
DR PDBsum; 6KWC; -.
DR PDBsum; 6KWD; -.
DR PDBsum; 6KWE; -.
DR PDBsum; 6KWF; -.
DR PDBsum; 6KWG; -.
DR PDBsum; 6KWH; -.
DR AlphaFoldDB; P36217; -.
DR SMR; P36217; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11B_TRIRE; -.
DR EnsemblFungi; ETR98242; ETR98242; M419DRAFT_124931.
DR KEGG; trr:M419DRAFT_124931; -.
DR OrthoDB; 1306131at2759; -.
DR BRENDA; 3.2.1.8; 6451.
DR UniPathway; UPA00114; -.
DR EvolutionaryTrace; P36217; -.
DR Proteomes; UP000024376; 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 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..33
FT /evidence="ECO:0000269|PubMed:1369024"
FT /id="PRO_0000436702"
FT CHAIN 34..223
FT /note="Endo-1,4-beta-xylanase 2"
FT /id="PRO_0000008014"
FT DOMAIN 34..222
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:26392527,
FT ECO:0000305|PubMed:24419374"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:26392527,
FT ECO:0000305|PubMed:24419374"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24419374"
FT MOD_RES 34
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1369024,
FT ECO:0000269|PubMed:16790934"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 191
FT /note="A -> V (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 77..86
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 92..114
FT /evidence="ECO:0007829|PDB:6K9O"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:6K9O"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6K9O"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 201..213
FT /evidence="ECO:0007829|PDB:6K9O"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:6K9O"
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
