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Protein

Endo-1,4-beta-xylanase 2

Gene

xyn2

Organism
Hypocrea jecorina (strain QM6a) (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose.By similarity

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.By similarity

pH dependencei

Optimum pH is 4-6.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.1 Publication

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei110 – 1101SubstrateBy similarity
Active sitei119 – 1191NucleophilePROSITE-ProRule annotation
Binding sitei121 – 1211SubstrateBy similarity
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei159 – 1591Substrate; via carbonyl oxygenBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Active sitei210 – 2101Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11C_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 21 Publication (EC:3.2.1.8PROSITE-ProRule annotation)
Short name:
Xylanase 2
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 2
Alkaline endo-beta-1,4-xylanase1 Publication
Gene namesi
Name:xyn21 Publication
Synonyms:xln21 Publication
ORF Names:TRIREDRAFT_123818
OrganismiHypocrea jecorina (strain QM6a) (Trichoderma reesei)
Taxonomic identifieri431241 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma
Proteomesi
  • UP000008984 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Secreted 1 Publication

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351T → C in Mxyn2: Forms a disufide bridge with C-61, increasing thermal stability of the recombinant protein; when associated with C-61. 1 Publication
Mutagenesisi61 – 611T → C in Mxyn2: Forms a disufide bridge with C-35, increasing thermal stability of the recombinant protein; when associated with C-35.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 3314By similarity1 PublicationPRO_0000436704Add
BLAST
Chaini34 – 223190Endo-1,4-beta-xylanase 2PRO_5003409032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Pyrrolidone carboxylic acidBy similarity
Glycosylationi71 – 711N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi94 – 941N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Expressioni

Inductioni

Induced by D-xylose, dependent on the cellulase and xylanase regulator xyr1. Repressed by glucose through negative regulation by the crabon catabolite repressor cre1.1 Publication

Structurei

3D structure databases

ProteinModelPortaliG0RUP7.
SMRiG0RUP7. Positions 35-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 223190GH11PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.PROSITE-ProRule annotation
Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JB05. Eukaryota.
ENOG410YH6C. LUCA.
KOiK01181.
OMAiTYDIYTT.
OrthoDBiEOG7VQJQX.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

G0RUP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFTSLLAG VAAISGVLAA PAAEVESVAV EKRQTIQPGT GYNNGYFYSY
60 70 80 90 100
WNDGHGGVTY TNGPGGQFSV NWSNSGNFVG GKGWQPGTKN KVINFSGSYN
110 120 130 140 150
PNGNSYLSVY GWSRNPLIEY YIVENFGTYN PSTGATKLGE VTSDGSVYDI
160 170 180 190 200
YRTQRVNQPS IIGTATFYQY WSVRRNHRSS GSVNTANHFN AWAQQGLTLG
210 220
TMDYQIVAVE GYFSSGSASI TVS
Length:223
Mass (Da):24,069
Last modified:October 19, 2011 - v1
Checksum:i79668149EADA22F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271S → P in AAB50278 (PubMed:8975597).Curated
Sequence conflicti48 – 481Y → H in AAB50278 (PubMed:8975597).Curated
Sequence conflicti124 – 1241E → G in AAB50278 (PubMed:8975597).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67387 Genomic DNA. Translation: AAB29346.1.
U24191 mRNA. Translation: AAB50278.1.
GL985082 Genomic DNA. Translation: EGR45030.1.
PIRiS39883.
RefSeqiXP_006968947.1. XM_006968885.1.

Genome annotation databases

EnsemblFungiiEGR45030; EGR45030; TRIREDRAFT_123818.
GeneIDi18483743.
KEGGitre:TRIREDRAFT_123818.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67387 Genomic DNA. Translation: AAB29346.1.
U24191 mRNA. Translation: AAB50278.1.
GL985082 Genomic DNA. Translation: EGR45030.1.
PIRiS39883.
RefSeqiXP_006968947.1. XM_006968885.1.

3D structure databases

ProteinModelPortaliG0RUP7.
SMRiG0RUP7. Positions 35-223.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11C_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEGR45030; EGR45030; TRIREDRAFT_123818.
GeneIDi18483743.
KEGGitre:TRIREDRAFT_123818.

Phylogenomic databases

eggNOGiENOG410JB05. Eukaryota.
ENOG410YH6C. LUCA.
KOiK01181.
OMAiTYDIYTT.
OrthoDBiEOG7VQJQX.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and enhanced expression of the Trichoderma reesei endoxylanase II (pI 9) gene xln2."
    Saarelainen R., Paloheimo M., Fagerstrom R., Suominen P.L., Nevalainen K.M.
    Mol. Gen. Genet. 241:497-503(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: QM6a.
  2. "Expression of a Trichoderma reesei beta-xylanase gene (XYN2) in Saccharomyces cerevisiae."
    la Grange D.C., Pretorius I.S., van Zyl W.H.
    Appl. Environ. Microbiol. 62:1036-1044(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: QM6a.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: QM6a.
  4. "Role of endoproteolytic dibasic proprotein processing in maturation of secretory proteins in Trichoderma reesei."
    Goller S.P., Schoisswohl D., Baron M., Parriche M., Kubicek C.P.
    Appl. Environ. Microbiol. 64:3202-3208(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  5. "Xylanase gene transcription in Trichoderma reesei is triggered by different inducers representing different hemicellulosic pentose polymers."
    Herold S., Bischof R., Metz B., Seiboth B., Kubicek C.P.
    Eukaryot. Cell 12:390-398(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "High-level expression and characterization of a thermostable xylanase mutant from Trichoderma reesei in Pichia pastoris."
    Li Y.Y., Zhong K.X., Hu A.H., Liu D.N., Chen L.Z., Xu S.D.
    Protein Expr. Purif. 108:90-96(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF THR-35 AND THR-61.
    Strain: QM6a.

Entry informationi

Entry nameiXYN2_HYPJQ
AccessioniPrimary (citable) accession number: G0RUP7
Secondary accession number(s): Q02244, Q99015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: October 19, 2011
Last modified: July 6, 2016
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.