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Protein

Endo-1,4-beta-xylanase 2

Gene

xyn2

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. 5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).4 Publications

Catalytic activityi

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

Kineticsi

kcat is 68 sec(-1) with xylohexaose, 50.3 sec(-1) with xylopentaose, 0.162 sec(-1) with xylotetraose and 0.045 sec(-1) with xylotriose as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=0.14 mg/ml for beechwood (unsubstituted) xylan1 Publication
  2. KM=13.8 mg/ml for birchwood xylan1 Publication
  3. KM=3.0 mg/ml for acetylated glucuronoxylan1 Publication
  4. KM=3.8 mg/ml for deactetylated glucuronoxylan1 Publication
  5. KM=6.8 mg/ml for unsubstituted xylan1 Publication
  6. KM=73 µM for xylohexaose1 Publication
  7. KM=136 µM for xylopentaose1 Publication
  1. Vmax=1600 µmol/min/mg enzyme for beechwood xylan1 Publication
  2. Vmax=336 µmol/min/mg enzyme for birchwood xylan1 Publication

pH dependencei

Optimum pH is 4.5-5.5 (PubMed:1369024). Stable from pH 3.0 to 8.5 at room temperature and from pH 4.0 to 7.5 at 40 degrees Celsius (Ref. 5).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 sitei106Substrate1 Publication1
Binding sitei110Substrate1 Publication1
Active sitei119Nucleophile1 Publication1 Publication1
Binding sitei121Substrate1 Publication1
Binding sitei155Substrate1 Publication1
Binding sitei159Substrate; via carbonyl oxygen1 Publication1
Binding sitei169Substrate1 Publication1
Binding sitei204Substrate1 Publication1
Active sitei210Proton donor1 Publication1 Publication1

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.
mycoCLAPiXYN11B_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase 21 Publication (EC:3.2.1.82 Publications)
Short name:
EX 21 Publication
Short name:
Xylanase 21 Publication
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 21 Publication
Alkaline endo-beta-1,4-xylanase1 Publication
Gene namesi
Name:xyn21 Publication
ORF Names:M419DRAFT_124931
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_000043670220 – 331 PublicationAdd BLAST14
ChainiPRO_000000801434 – 223Endo-1,4-beta-xylanase 2Add BLAST190

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34Pyrrolidone carboxylic acid2 Publications1
Glycosylationi71N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1

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.By similarity

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI123818.

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 43Combined sources6
Beta strandi46 – 52Combined sources7
Beta strandi58 – 62Combined sources5
Beta strandi67 – 74Combined sources8
Beta strandi77 – 86Combined sources10
Beta strandi92 – 114Combined sources23
Turni115 – 117Combined sources3
Beta strandi118 – 128Combined sources11
Turni131 – 134Combined sources4
Beta strandi136 – 143Combined sources8
Beta strandi146 – 158Combined sources13
Beta strandi163 – 176Combined sources14
Beta strandi179 – 184Combined sources6
Helixi185 – 194Combined sources10
Beta strandi201 – 213Combined sources13
Beta strandi215 – 223Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ENXX-ray1.50A/B35-223[»]
1REDX-ray1.60A/B35-223[»]
1REEX-ray1.60A/B35-223[»]
1REFX-ray1.80A/B35-223[»]
1XYOX-ray1.50A/B35-223[»]
1XYPX-ray1.50A/B35-223[»]
2D97X-ray2.01A35-223[»]
2D98X-ray2.00A35-223[»]
2DFBX-ray1.11A34-223[»]
2DFCX-ray1.19A34-223[»]
3LGRX-ray1.64A35-223[»]
4HK8X-ray1.15A35-223[»]
4HK9X-ray1.55A36-223[»]
4HKLX-ray1.10A35-223[»]
4HKOX-ray1.50A35-223[»]
4HKWX-ray1.65A35-223[»]
4S2DOther1.60A35-223[»]
4S2FOther1.70A35-223[»]
4S2GOther1.60A35-223[»]
4S2HOther1.60A35-223[»]
4XPVOther1.70A35-223[»]
4XQ4X-ray1.25A/B35-223[»]
4XQDX-ray1.50A/B35-223[»]
4XQWX-ray1.50A35-223[»]
ProteinModelPortaliP36217.
SMRiP36217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 222GH11PROSITE-ProRule annotationAdd BLAST189

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JB05. Eukaryota.
ENOG410YH6C. LUCA.

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.

P36217-1 [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:July 6, 2016 - v2
Checksum:i79668149EADA22F9
GO

Sequence cautioni

The sequence CAA49293 differs from that shown. Reason: Frameshift at positions 10, 19 and 20.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191A → V no nucleotide entry (PubMed:17416973).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1. Frameshift.
EU532196 mRNA. Translation: ACB38137.1.
KI911164 Genomic DNA. Translation: ETR98242.1.
PIRiS39154.

Genome annotation databases

EnsemblFungiiETR98242; ETR98242; M419DRAFT_124931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69573 Genomic DNA. Translation: CAA49293.1. Frameshift.
EU532196 mRNA. Translation: ACB38137.1.
KI911164 Genomic DNA. Translation: ETR98242.1.
PIRiS39154.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ENXX-ray1.50A/B35-223[»]
1REDX-ray1.60A/B35-223[»]
1REEX-ray1.60A/B35-223[»]
1REFX-ray1.80A/B35-223[»]
1XYOX-ray1.50A/B35-223[»]
1XYPX-ray1.50A/B35-223[»]
2D97X-ray2.01A35-223[»]
2D98X-ray2.00A35-223[»]
2DFBX-ray1.11A34-223[»]
2DFCX-ray1.19A34-223[»]
3LGRX-ray1.64A35-223[»]
4HK8X-ray1.15A35-223[»]
4HK9X-ray1.55A36-223[»]
4HKLX-ray1.10A35-223[»]
4HKOX-ray1.50A35-223[»]
4HKWX-ray1.65A35-223[»]
4S2DOther1.60A35-223[»]
4S2FOther1.70A35-223[»]
4S2GOther1.60A35-223[»]
4S2HOther1.60A35-223[»]
4XPVOther1.70A35-223[»]
4XQ4X-ray1.25A/B35-223[»]
4XQDX-ray1.50A/B35-223[»]
4XQWX-ray1.50A35-223[»]
ProteinModelPortaliP36217.
SMRiP36217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI123818.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiETR98242; ETR98242; M419DRAFT_124931.

Phylogenomic databases

eggNOGiENOG410JB05. Eukaryota.
ENOG410YH6C. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6451.

Miscellaneous databases

EvolutionaryTraceiP36217.

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 nameiXYN2_HYPJR
AccessioniPrimary (citable) accession number: P36217
Secondary accession number(s): A0A024RZG2, B2CNY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 6, 2016
Last modified: November 2, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

In PubMed:1369024 Figure 2, this sequence is erroneously labeled xyn1, but in the remainder of the paper and all subsequent publications, this protein is referred to as xylanase 2 (xyn2).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.