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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

  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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061Substrate1 Publication
Binding sitei110 – 1101Substrate1 Publication
Active sitei119 – 1191Nucleophile1 Publication1 Publication
Binding sitei121 – 1211Substrate1 Publication
Binding sitei155 – 1551Substrate1 Publication
Binding sitei159 – 1591Substrate; via carbonyl oxygen1 Publication
Binding sitei169 – 1691Substrate1 Publication
Binding sitei204 – 2041Substrate1 Publication
Active sitei210 – 2101Proton donor1 Publication1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 33141 PublicationPRO_0000436702Add
BLAST
Chaini34 – 223190Endo-1,4-beta-xylanase 2PRO_0000008014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Pyrrolidone carboxylic acid2 Publications
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis

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

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 436Combined sources
Beta strandi46 – 527Combined sources
Beta strandi58 – 625Combined sources
Beta strandi67 – 748Combined sources
Beta strandi77 – 8610Combined sources
Beta strandi92 – 11423Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 12811Combined sources
Turni131 – 1344Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi146 – 15813Combined sources
Beta strandi163 – 17614Combined sources
Beta strandi179 – 1846Combined sources
Helixi185 – 19410Combined sources
Beta strandi201 – 21313Combined sources
Beta strandi215 – 2228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36217.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 222189GH11PROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911A → V no nucleotide entry (PubMed:17416973).Curated

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
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.
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: September 7, 2016
This is version 107 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.