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Database: UniProt
Entry: P36218
LinkDB: P36218
Original site: P36218 
ID   XYN1_HYPJR              Reviewed;         229 AA.
AC   P36218; A0A024RZA6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JAN-2019, entry version 107.
DE   RecName: Full=Endo-1,4-beta-xylanase 1 {ECO:0000303|PubMed:1369024};
DE            Short=EX 1 {ECO:0000303|PubMed:7988708};
DE            Short=Xylanase 1 {ECO:0000303|Ref.3};
DE            EC=3.2.1.8 {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.3};
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1 {ECO:0000303|PubMed:1369024};
DE   AltName: Full=Acidic endo-beta-1,4-xylanase {ECO:0000303|PubMed:7988708};
DE   Flags: Precursor;
GN   Name=xyn1 {ECO:0000303|PubMed:1369024}; ORFNames=M419DRAFT_38418;
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 52-63; 118-179
RP   AND 216-225, 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 [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   [3]
RP   PROTEIN SEQUENCE OF 52-57, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR 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   [4]
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   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
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).
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.3). 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       {ECO:0000269|PubMed:1369024, ECO:0000269|PubMed:7988708,
CC       ECO:0000269|Ref.3}.
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.3};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 mg/ml for beechwood (unsubstituted) xylan
CC         {ECO:0000269|PubMed:1369024};
CC         KM=14.8 mg/ml for acetylated glucuronoxylan {ECO:0000269|Ref.3};
CC         KM=22.3 mg/ml for deactetylated glucuronoxylan
CC         {ECO:0000269|Ref.3};
CC         KM=18.9 mg/ml for unsubstituted xylan {ECO:0000269|Ref.3};
CC         Vmax=100 umol/min/mg enzyme for beechwood xylan
CC         {ECO:0000269|PubMed:1369024};
CC       pH dependence:
CC         Optimum pH is 3.5-4.0 (PubMed:1369024). Stable from pH 2.5 to
CC         8.5 at room temperature and from pH 2.5 to 4.5 at 40 degrees
CC         Celsius (Ref.3). {ECO:0000269|PubMed:1369024,
CC         ECO:0000269|Ref.3};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000255|PROSITE-ProRule:PRU01097}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
CC   -!- INDUCTION: Induced by D-xylose and L-arabinose, dependent on the
CC       cellulase and xylanase regulator xyr1. Repressed by glucose
CC       through negative regulation by the crabon catabolite repressor
CC       cre1. {ECO:0000250|UniProtKB:G0R947}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: In PubMed:1369024 Figure 3, this sequence is erroneously
CC       labeled xyn2, but in the remainder of the paper and all subsequent
CC       publications, this protein is referred to as xylanase 1 (xyn1).
CC       {ECO:0000305|PubMed:1369024}.
DR   EMBL; X69574; CAA49294.1; -; Genomic_DNA.
DR   EMBL; KI911162; ETR98398.1; -; Genomic_DNA.
DR   PIR; S39155; S39155.
DR   PDB; 1XYN; X-ray; 2.00 A; A=52-229.
DR   PDBsum; 1XYN; -.
DR   ProteinModelPortal; P36218; -.
DR   SMR; P36218; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   mycoCLAP; XYN11A_TRIRE; -.
DR   EnsemblFungi; ETR98398; ETR98398; M419DRAFT_38418.
DR   eggNOG; ENOG410IIEF; Eukaryota.
DR   eggNOG; ENOG4111ZP8; LUCA.
DR   OrthoDB; 1306131at2759; -.
DR   BRENDA; 3.2.1.8; 6451.
DR   UniPathway; UPA00114; -.
DR   EvolutionaryTrace; P36218; -.
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; Secreted; Signal; Xylan degradation.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20     51       {ECO:0000269|PubMed:1369024,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=PRO_0000436701.
FT   CHAIN        52    229       Endo-1,4-beta-xylanase 1.
FT                                /FTId=PRO_0000008013.
FT   DOMAIN       52    228       GH11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01097}.
FT   ACT_SITE    126    126       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10062}.
FT   ACT_SITE    215    215       Proton donor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10063}.
FT   BINDING     117    117       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     128    128       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     160    160       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     164    164       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     174    174       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   BINDING     209    209       Substrate.
FT                                {ECO:0000250|UniProtKB:P36217}.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   STRAND       56     61       {ECO:0000244|PDB:1XYN}.
FT   STRAND       63     70       {ECO:0000244|PDB:1XYN}.
FT   STRAND       72     83       {ECO:0000244|PDB:1XYN}.
FT   STRAND       85     93       {ECO:0000244|PDB:1XYN}.
FT   STRAND       99    121       {ECO:0000244|PDB:1XYN}.
FT   TURN        122    124       {ECO:0000244|PDB:1XYN}.
FT   STRAND      125    135       {ECO:0000244|PDB:1XYN}.
FT   STRAND      140    148       {ECO:0000244|PDB:1XYN}.
FT   STRAND      151    165       {ECO:0000244|PDB:1XYN}.
FT   STRAND      168    181       {ECO:0000244|PDB:1XYN}.
FT   STRAND      184    188       {ECO:0000244|PDB:1XYN}.
FT   HELIX       190    199       {ECO:0000244|PDB:1XYN}.
FT   STRAND      206    228       {ECO:0000244|PDB:1XYN}.
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
//
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