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Database: UniProt
Entry: P36217
LinkDB: P36217
Original site: P36217 
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   16-JAN-2019, entry version 118.
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
OS   C-30) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=1344414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-42; 49-60;
RP   83-89; 120-152; 168-171; 205-211 AND 213-217, PYROGLUTAMATE FORMATION
RP   AT GLN-34, 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.,
RA   Harkki A., Kubicek C.P.;
RT   "The two major xylanases from Trichoderma reesei: characterization of
RT   both 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/s12010-007-0013-8;
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
RT   reesei Rut C-30 and characterization of the recombinant enzyme and its
RT   activity on 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-
RT   1,4-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-
RT   catalyzed hydrolysis of neutral underivatized xylooligosaccharides by
RT   mass 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;
RA   Toerroenen A., Harkki A., Rouvinen J.;
RT   "Three-dimensional structure of endo-1,4-beta-xylanase II from
RT   Trichoderma 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
RT   Trichoderma 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
RT   endo-1,4-xylanase II from Trichoderma reesei.";
RL   Biochemistry 35:9617-9624(1996).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS), AND CARBOXYLATION AT 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
RT   reesei 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.,
RA   Coates L., Langan P., Graham D., Kovalevsky A.;
RT   "X-ray crystallographic studies of family 11 xylanase Michaelis and
RT   product 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.,
RA   Schrader T.E., Graham D.E., Coates L., Langan P., Kovalevsky A.;
RT   "Direct determination of protonation states and visualization of
RT   hydrogen bonding in a glycoside hydrolase with neutron
RT   crystallography.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:12384-12389(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 (PubMed:1369024,
CC       Ref.5). The catalysis proceeds by a double-displacement reaction
CC       mechanism with a putative covalent glycosyl-enzyme intermediate,
CC       with retention of the anomeric configuration (PubMed:7988708).
CC       Produces xylobiose and xylose as the main degradation products
CC       (PubMed:19556747). {ECO:0000269|PubMed:1369024,
CC       ECO:0000269|PubMed:19556747, ECO:0000269|PubMed:7988708,
CC       ECO:0000269|Ref.5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in
CC         xylans.; EC=3.2.1.8; Evidence={ECO:0000269|PubMed:1369024,
CC         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 deactetylated glucuronoxylan
CC         {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)
CC         with 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
CC         8.5 at room temperature and from pH 4.0 to 7.5 at 40 degrees
CC         Celsius (Ref.5). {ECO:0000269|PubMed:1369024,
CC         ECO:0000269|Ref.5};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000255|PROSITE-ProRule:PRU01097}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.5}.
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:0000250|UniProtKB:G0RUP7}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {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; Positions=10, 19, 20; Evidence={ECO:0000305};
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   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   ProteinModelPortal; P36217; -.
DR   SMR; P36217; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11B_TRIRE; -.
DR   EnsemblFungi; ETR98242; ETR98242; M419DRAFT_124931.
DR   eggNOG; ENOG410JB05; Eukaryota.
DR   eggNOG; ENOG410YH6C; LUCA.
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; Complete proteome;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     33       {ECO:0000269|PubMed:1369024}.
FT                                /FTId=PRO_0000436702.
FT   CHAIN        34    223       Endo-1,4-beta-xylanase 2.
FT                                /FTId=PRO_0000008014.
FT   DOMAIN       34    222       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    119    119       Nucleophile.
FT                                {ECO:0000269|PubMed:26392527,
FT                                ECO:0000305|PubMed:24419374}.
FT   ACT_SITE    210    210       Proton donor.
FT                                {ECO:0000269|PubMed:26392527,
FT                                ECO:0000305|PubMed:24419374}.
FT   BINDING     106    106       Substrate. {ECO:0000269|PubMed:24419374}.
FT   BINDING     110    110       Substrate. {ECO:0000269|PubMed:24419374}.
FT   BINDING     121    121       Substrate. {ECO:0000269|PubMed:24419374}.
FT   BINDING     155    155       Substrate. {ECO:0000269|PubMed:24419374}.
FT   BINDING     159    159       Substrate; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:24419374}.
FT   BINDING     169    169       Substrate. {ECO:0000269|PubMed:24419374}.
FT   BINDING     204    204       Substrate. {ECO:0000269|PubMed:24419374}.
FT   MOD_RES      34     34       Pyrrolidone carboxylic acid.
FT                                {ECO:0000269|PubMed:1369024,
FT                                ECO:0000269|PubMed:16790934}.
FT   CARBOHYD     71     71       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    191    191       A -> V (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   STRAND       38     43       {ECO:0000244|PDB:4HKL}.
FT   STRAND       46     52       {ECO:0000244|PDB:4HKL}.
FT   STRAND       58     62       {ECO:0000244|PDB:4HKL}.
FT   STRAND       67     74       {ECO:0000244|PDB:4HKL}.
FT   STRAND       77     86       {ECO:0000244|PDB:4HKL}.
FT   STRAND       92    114       {ECO:0000244|PDB:4HKL}.
FT   TURN        115    117       {ECO:0000244|PDB:4HKL}.
FT   STRAND      118    128       {ECO:0000244|PDB:4HKL}.
FT   TURN        131    134       {ECO:0000244|PDB:4HKL}.
FT   STRAND      136    143       {ECO:0000244|PDB:4HKL}.
FT   STRAND      146    158       {ECO:0000244|PDB:4HKL}.
FT   STRAND      163    176       {ECO:0000244|PDB:4HKL}.
FT   STRAND      179    184       {ECO:0000244|PDB:4HKL}.
FT   HELIX       185    194       {ECO:0000244|PDB:4HKL}.
FT   STRAND      201    213       {ECO:0000244|PDB:4HKL}.
FT   STRAND      215    223       {ECO:0000244|PDB:4HKL}.
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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