Reviewed, UniProtKB/Swiss-Prot P36217 (XYN2_TRIRE)

Names and origin

Protein names

Recommended name:
    Endo-1,4-beta-xylanase 2
      Short name=Xylanase 2
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase 2

Gene names

Name:

xyn2

Organism

Trichoderma reesei (Hypocrea jecorina)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Pathway	Glycan degradation; xylan degradation.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 222

190

Endo-1,4-beta-xylanase 2

PRO_0000008014

Sites

Active site

118

1

Nucleophile

Active site

209

1

Proton donor

Amino acid modifications

Glycosylation

70

1

N-linked (GlcNAc...) Potential

Glycosylation

93

1

N-linked (GlcNAc...) Potential

Glycosylation

129

1

N-linked (GlcNAc...) Potential

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

37 – 42

6

Beta strand

45 – 51

7

Beta strand

57 – 61

5

Beta strand

66 – 73

8

Beta strand

76 – 85

10

Beta strand

91 – 113

23

Turn

114 – 116

3

Beta strand

117 – 127

11

Turn

130 – 133

4

Beta strand

135 – 142

8

Beta strand

145 – 157

13

Beta strand

162 – 175

14

Beta strand

178 – 183

6

Helix

184 – 193

10

Beta strand

200 – 212

13

Sequences

	Sequence		Length	Mass (Da)
	P36217-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 15F7032FACF963FF	FASTA	222	24,172
	10 20 30 40 50 60 MVSFTSLLAA SPPSRASCRP AAEVESVAVE KRQTIQPGTG YNNGYFYSYW NDGHGGVTYT 70 80 90 100 110 120 NGPGGQFSVN WSNSGNFVGG KGWQPGTKNK VINFSGSYNP NGNSYLSVYG WSRNPLIEYY 130 140 150 160 170 180 IVENFGTYNP STGATKLGEV TSDGSVYDIY RTQRVNQPSI IGTATFYQYW SVRRNHRSSG 190 200 210 220 SVNTANHFNA WAQQGLTLGT MDYQIVAVEG YFSSGSASIT VS

References

[1]	"The two major xylanases from Trichoderma reesei: characterization of both enzymes and genes." Toerroenen A., Mach R.L., Messner R., Gonzalez R., Kalkkinen N., Harkki A., Kubicek C.P. Biotechnology (N.Y.) 10:1461-1465(1992) [PubMed: 1369024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: C30.
[2]	"Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site." Toerroenen A., Harkki A., Rouvinen J. EMBO J. 13:2493-2501(1994) [PubMed: 8013449] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). Strain: C30.
[3]	"Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei." Toerroenen A., Rouvinen J. Biochemistry 34:847-856(1995) [PubMed: 7827044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). Strain: C30.
[4]	"Covalent binding of three epoxyalkyl xylosides to the active site of endo-1,4-xylanase II from Trichoderma reesei." Havukainen R., Toerroenen A., Laitinen T., Rouvinen J. Biochemistry 35:9617-9624(1996) [PubMed: 8755744] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). Strain: C30.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X69573 Genomic DNA. Translation: CAA49293.1.

PIR

S39154.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ENX	X-ray	1.50	A/B	34-222	[»]
1RED	X-ray	1.60	A/B	34-222	[»]
1REE	X-ray	1.60	A/B	34-222	[»]
1REF	X-ray	1.80	A/B	34-222	[»]
1XYO	X-ray	1.50	A/B	34-222	[»]
1XYP	X-ray	1.50	A/B	34-222	[»]
2D97	X-ray	2.01	A	34-222	[»]
2D98	X-ray	2.00	A	34-222	[»]
2DFB	X-ray	1.11	A	34-222	[»]
2DFC	X-ray	1.19	A	34-222	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA

3.2.1.8. 280374.

Family and domain databases

InterPro

IPR008985. ConA-like_lec_gl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12_cat.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]

Gene3D

G3DSA:2.60.120.180. Glyco_hydro_11/12_cat. 1 hit.

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

PROSITE

PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYN2_TRIRE

Accession

Primary (citable) accession number: P36217

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 24, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)