Reviewed, UniProtKB/Swiss-Prot P23360 (XYNA_THEAU)

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
    TAXI

Gene names

Name:

XYNA

Organism

Thermoascus aurantiacus

Taxonomic identifier

5087 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Thermoascus

Protein attributes

Sequence length	329 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.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.
Caution	Ref.2, Ref.3 and Ref.5 N-terminal modification was incorrect. X-ray structure has cyclic pyroglutamic acid.
Sequence caution	The sequence described in Ref.2 differs from that shown. Reason: Miscellaneous discrepancy. Sequencing errors. The sequence described in Ref.3 differs from that shown. Reason: Miscellaneous discrepancy. Sequencing errors.

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-KW
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro 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 – 26

26

Ref.2 Ref.3 Ref.4

Chain

27 – 329

303

Endo-1,4-beta-xylanase

PRO_0000007985

Sites

Active site

157

1

Proton donor

Active site

263

1

Nucleophile

Amino acid modifications

Modified residue

27

1

Pyrrolidone carboxylic acid

Disulfide bond

281 ↔ 287

Experimental info

Sequence conflict

243

1

G → S in CAB65468. Ref.1

Sequence conflict

243

1

G → S in AAF24127. Ref.1

Sequence conflict

271

1

P → S in CAB65468. Ref.1

Sequence conflict

271

1

P → S in AAF24127. Ref.1

Secondary structure

1

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329

Helix Strand Turn

Details...

Helix

32 – 38

7

Beta strand

42 – 48

7

Helix

50 – 53

4

Helix

58 – 65

8

Beta strand

67 – 73

7

Helix

77 – 80

4

Helix

90 – 101

12

Beta strand

105 – 112

8

Beta strand

114 – 116

3

Helix

119 – 122

4

Helix

127 – 144

18

Turn

145 – 148

4

Beta strand

150 – 157

8

Beta strand

163 – 165

3

Helix

169 – 174

6

Helix

178 – 189

12

Beta strand

193 – 200

8

Helix

208 – 222

15

Beta strand

229 – 232

4

Turn

238 – 240

3

Helix

241 – 252

12

Beta strand

257 – 266

10

Helix

271 – 283

13

Beta strand

287 – 293

7

Helix

297 – 299

3

Helix

303 – 305

3

Beta strand

308 – 310

3

Helix

318 – 327

10

Sequences

	Sequence		Length	Mass (Da)
	P23360-1 [UniParc]. Last modified April 27, 2001. Version 4. Checksum: 8FE2F3D1A9F89815	FASTA	329	35,686
	10 20 30 40 50 60 MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ NRLTTGKNAA 70 80 90 100 110 120 IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ QNGKLIRGHT LVWHSQLPSW 130 140 150 160 170 180 VSSITDKNTL TNVMKNHITT LMTRYKGKIR AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP 190 200 210 220 230 240 IAFQTARAAD PNAKLYINDY NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ 250 260 270 280 290 300 GAGVLQALPL LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS 310 320 WRASTTPLLF DGNFNPKPAY NAIVQDLQQ

References

[1]	"Cloning, sequencing and overexpression of Thermoascus aurantiacus xylanase A (xynA)." Bousson J.-C., Parriche M. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Significance of structural homology of Thermoascus aurantiacus xylanase with the exoglucanase of Cellulomonas fimi." Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R. J. Protein Chem. 9:337-338(1990) Cited for: PROTEIN SEQUENCE OF 27-328.
[3]	"The primary structure of xylanase from Thermoascus aurantiacus." Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K., Vithayathil P.J. Protein Seq. Data Anal. 4:15-20(1991) [PubMed: 1924265] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-328.
[4]	"Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I." Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C. Acta Crystallogr. D 57:385-392(2001) [PubMed: 11223515] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-328, X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS). Strain: IMI 216529.
[5]	"High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture." Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W. Proteins 36:295-306(1999) [PubMed: 10409823] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS). Strain: IMI 216529.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ132635 Genomic DNA. Translation: CAB65468.1.
AF127529 Genomic DNA. Translation: AAF24127.1.

PIR

A59381.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GOK	X-ray	1.14	A	28-329	[»]
1GOM	X-ray	1.92	A	28-329	[»]
1GOO	X-ray	1.87	A	28-329	[»]
1GOQ	X-ray	1.80	A	28-329	[»]
1GOR	X-ray	1.70	A	28-329	[»]
1I1W	X-ray	0.89	A	28-329	[»]
1I1X	X-ray	1.11	A	28-329	[»]
1K6A	X-ray	1.14	A	27-329	[»]
1TUX	X-ray	1.80	A	28-325	[»]
2BNJ	X-ray	1.60	A	28-329	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA

3.2.1.8. 16693.

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

PRINTS

PR00134. GLHYDRLASE10.

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

PROSITE

PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XYNA_THEAU

Accession

Primary (citable) accession number: P23360
Secondary accession number(s): Q9UQZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	April 27, 2001
Last modified:	June 16, 2009
This is version 72 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)