O43097 (XYNA_THELA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase
Short name=Xylanase
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase

Gene names

Name:

XYNA

Organism

Thermomyces lanuginosus (Humicola lanuginosa)

Taxonomic identifier

5541 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Thermomyces

Protein attributes

Sequence length	225 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. Ref.3
Pathway	Glycan degradation; xylan degradation.
Induction	By xylan. Ref.3
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family.
Biophysicochemical properties	Kinetic parameters: Vmax=2223.3 µmol/min/mg enzyme Ref.3 pH dependence: Optimum pH is 6.0. Temperature dependence: Optimum temperature is 60 degrees Celsius. Thermostable.
Mass spectrometry	Molecular mass is 21300 Da from positions 32 - 225. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 – 31

31

Chain

32 – 225

194

Endo-1,4-beta-xylanase

PRO_0000008012

Sites

Active site

117

1

Nucleophile

Active site

209

1

Proton donor

Amino acid modifications

Modified residue

32

1

Pyrrolidone carboxylic acid

Disulfide bond

141 ↔ 185

Experimental info

Sequence conflict

130

1

S → P in ACY69861. Ref.2

Sequence conflict

177

1

T → A in ACY69861. Ref.2

Secondary structure

1

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225

Helix Strand Turn

Details...

Beta strand

37 – 41

5

Beta strand

44 – 50

7

Beta strand

52 – 54

3

Beta strand

56 – 60

5

Beta strand

65 – 70

6

Beta strand

72 – 84

13

Beta strand

90 – 112

23

Turn

113 – 115

3

Beta strand

116 – 127

12

Turn

129 – 132

4

Beta strand

134 – 141

8

Beta strand

144 – 158

15

Beta strand

161 – 174

14

Beta strand

177 – 182

6

Helix

183 – 192

10

Beta strand

199 – 212

14

Beta strand

214 – 223

10

Sequences

	Sequence		Length	Mass (Da)
	O43097 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: FAA79A914C5C676C	FASTA	225	24,356
	10 20 30 40 50 60 MVGFTPVALA ALAATGALAF PAGNATELEK RQTTPNSEGW HDGYYYSWWS DGGAQATYTN 70 80 90 100 110 120 LEGGTYEISW GDGGNLVGGK GWNPGLNARA IHFEGVYQPN GNSYLAVYGW TRNPLVEYYI 130 140 150 160 170 180 VENFGTYDPS SGATDLGTVE CDGSIYRLGK TTRVNAPSID GTQTFDQYWS VRQDKRTSGT 190 200 210 220 VQTGCHFDAW ARAGLNVNGD HYYQIVATEG YFSSGYARIT VADVG

References

[1]	"Cloning and characterization of the gene for the thermostable xylanase XynA from Thermomyces lanuginosus." Schlacher A., Holzmann K., Hayn M., Steiner W., Schwab H. J. Biotechnol. 49:211-218(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 5826 / Tsiklinsky.
[2]	"Expression and characterization of the xylanase gene xynA from Thermomyces lanuginosus in Pichia pastoris." Guo R., Zhao N. Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-225.
[3]	"Thermomyces lanuginosus SS-8 endo-beta-1,4-D-xylanase precursor." Shrivastava S., Deepalakshmi P.D., Shukla P., Mukhopadhyay K. Submitted (JUL-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 81-89; 154-172 AND 193-225, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MASS SPECTROMETRY. Strain: SS-8.
[4]	"Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies." Gruber K., Klintschar G., Hayn M., Schlacher A., Steiner W., Kratky C. Biochemistry 37:13475-13485(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS). Strain: DSM 5826 / Tsiklinsky.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U35436 Genomic DNA. Translation: AAB94633.1.
GU166389 Genomic DNA. Translation: ACY69861.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YNA	X-ray	1.55	A	33-225	[»]

ProteinModelPortal

O43097.

SMR

O43097. Positions 32-225.

ModBase

Search...

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

mycoCLAP

XYN11A_THELA.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.8. 6317.

UniPathway

UPA00114.

Family and domain databases

Gene3D

2.60.120.180. 1 hit.

InterPro

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

Pfam

PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]

PRINTS

PR00911. GLHYDRLASE11.

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

O43097.

Entry information

Entry name

XYNA_THELA

Accession

Primary (citable) accession number: O43097
Secondary accession number(s): D1MH26

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program