XYN1_HYPJR
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 03-AUG-2022, entry version 117.
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 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 52-63; 118-179 AND
RP 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., 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 [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-1,4-
RT 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 Trichoderma
RT reesei.";
RL Biochemistry 34:847-856(1995).
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.3). 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). {ECO:0000269|PubMed:1369024,
CC ECO:0000269|PubMed:7988708, ECO:0000269|Ref.3}.
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.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 deacetylated glucuronoxylan {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 8.5 at
CC room temperature and from pH 2.5 to 4.5 at 40 degrees Celsius
CC (Ref.3). {ECO:0000269|PubMed:1369024, ECO:0000269|Ref.3};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC 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 through
CC negative regulation by the crabon catabolite repressor cre1.
CC {ECO:0000250|UniProtKB:G0R947}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {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}.
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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 AlphaFoldDB; P36218; -.
DR SMR; P36218; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11A_TRIRE; -.
DR EnsemblFungi; ETR98398; ETR98398; M419DRAFT_38418.
DR KEGG; trr:M419DRAFT_38418; -.
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; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal; Xylan degradation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..51
FT /evidence="ECO:0000269|PubMed:1369024, ECO:0000269|Ref.3"
FT /id="PRO_0000436701"
FT CHAIN 52..229
FT /note="Endo-1,4-beta-xylanase 1"
FT /id="PRO_0000008013"
FT DOMAIN 52..228
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 215
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
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"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 99..121
FT /evidence="ECO:0007829|PDB:1XYN"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 151..165
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 168..181
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1XYN"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1XYN"
FT STRAND 206..228
FT /evidence="ECO:0007829|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
