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Protein

Endo-1,4-beta-xylanase 1

Gene

xyn1

Organism
Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:1369024, Ref. 3). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708).3 Publications

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.2 Publications

Kineticsi

  1. KM=0.22 mg/ml for beechwood (unsubstituted) xylan1 Publication
  2. KM=14.8 mg/ml for acetylated glucuronoxylan1 Publication
  3. KM=22.3 mg/ml for deactetylated glucuronoxylan1 Publication
  4. KM=18.9 mg/ml for unsubstituted xylan1 Publication
  1. Vmax=100 µmol/min/mg enzyme for beechwood xylan1 Publication

pH dependencei

Optimum pH is 3.5-4.0 (PubMed:1369024). Stable from pH 2.5 to 8.5 at room temperature and from pH 2.5 to 4.5 at 40 degrees Celsius (Ref. 3).2 Publications

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)DescriptionActionsGraphical viewLength
Binding sitei117SubstrateBy similarity1
Active sitei126NucleophilePROSITE-ProRule annotation1
Binding sitei128SubstrateBy similarity1
Binding sitei160SubstrateBy similarity1
Binding sitei164Substrate; via carbonyl oxygenBy similarity1
Binding sitei174SubstrateBy similarity1
Binding sitei209SubstrateBy similarity1
Active sitei215Proton donorPROSITE-ProRule annotation1

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

BRENDAi3.2.1.8. 6451.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 11 Publication (EC:3.2.1.82 Publications)
Short name:
EX 11 Publication
Short name:
Xylanase 11 Publication
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 11 Publication
Acidic endo-beta-1,4-xylanase1 Publication
Gene namesi
Name:xyn11 Publication
ORF Names:M419DRAFT_38418
OrganismiHypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30) (Trichoderma reesei)
Taxonomic identifieri1344414 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma
Proteomesi
  • UP000024376 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000043670120 – 512 PublicationsAdd BLAST32
ChainiPRO_000000801352 – 229Endo-1,4-beta-xylanase 1Add BLAST178

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi31N-linked (GlcNAc...)PROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI74223.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 61Combined sources6
Beta strandi63 – 70Combined sources8
Beta strandi72 – 83Combined sources12
Beta strandi85 – 93Combined sources9
Beta strandi99 – 121Combined sources23
Turni122 – 124Combined sources3
Beta strandi125 – 135Combined sources11
Beta strandi140 – 148Combined sources9
Beta strandi151 – 165Combined sources15
Beta strandi168 – 181Combined sources14
Beta strandi184 – 188Combined sources5
Helixi190 – 199Combined sources10
Beta strandi206 – 228Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XYNX-ray2.00A52-229[»]
ProteinModelPortaliP36218.
SMRiP36218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36218.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 228GH11PROSITE-ProRule annotationAdd BLAST177

Sequence similaritiesi

Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIEF. Eukaryota.
ENOG4111ZP8. LUCA.
OMAiDIWKHTQ.

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.

P36218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAFSSLICA LTSIASTLAM PTGLEPESSV NVTERGMYDF VLGAHNDHRR
60 70 80 90 100
RASINYDQNY QTGGQVSYSP SNTGFSVNWN TQDDFVVGVG WTTGSSAPIN
110 120 130 140 150
FGGSFSVNSG TGLLSVYGWS TNPLVEYYIM EDNHNYPAQG TVKGTVTSDG
160 170 180 190 200
ATYTIWENTR VNEPSIQGTA TFNQYISVRN SPRTSGTVTV QNHFNAWASL
210 220
GLHLGQMNYQ VVAVEGWGGS GSASQSVSN
Length:229
Mass (Da):24,583
Last modified:June 1, 1994 - v1
Checksum:iF9E8BFE1607038DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69574 Genomic DNA. Translation: CAA49294.1.
KI911162 Genomic DNA. Translation: ETR98398.1.
PIRiS39155.

Genome annotation databases

EnsemblFungiiETR98398; ETR98398; M419DRAFT_38418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69574 Genomic DNA. Translation: CAA49294.1.
KI911162 Genomic DNA. Translation: ETR98398.1.
PIRiS39155.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XYNX-ray2.00A52-229[»]
ProteinModelPortaliP36218.
SMRiP36218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI74223.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiETR98398; ETR98398; M419DRAFT_38418.

Phylogenomic databases

eggNOGiENOG410IIEF. Eukaryota.
ENOG4111ZP8. LUCA.
OMAiDIWKHTQ.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6451.

Miscellaneous databases

EvolutionaryTraceiP36218.

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...

Entry informationi

Entry nameiXYN1_HYPJR
AccessioniPrimary (citable) accession number: P36218
Secondary accession number(s): A0A024RZA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

In PubMed:1369024 Figure 3, this sequence is erroneously labeled xyn2, but in the remainder of the paper and all subsequent publications, this protein is referred to as xylanase 1 (xyn1).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.