Reviewed, UniProtKB/Swiss-Prot P40943 (XYN1_BACST)

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
Organism	Bacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier	1422 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	407 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.
Subcellular location	Secreted.
Induction	By xylose.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 28

28

Ref.2

Chain

29 – 407

379

Endo-1,4-beta-xylanase

PRO_0000007968

Sites

Active site

187

1

Proton donor By similarity

Active site

293

1

Nucleophile By similarity

Secondary structure

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407

Helix Strand Turn

Details...

Helix

42 – 44

3

Helix

48 – 52

5

Turn

53 – 55

3

Beta strand

57 – 62

6

Helix

64 – 68

5

Helix

70 – 79

10

Beta strand

81 – 87

7

Helix

91 – 94

4

Helix

104 – 115

12

Beta strand

119 – 123

5

Helix

133 – 136

4

Beta strand

141 – 143

3

Helix

144 – 146

3

Helix

150 – 175

26

Turn

176 – 178

3

Beta strand

181 – 187

7

Beta strand

193 – 195

3

Helix

199 – 204

6

Helix

207 – 220

14

Beta strand

224 – 231

8

Helix

238 – 251

14

Beta strand

258 – 261

4

Beta strand

267 – 270

4

Helix

272 – 284

13

Beta strand

288 – 296

9

Helix

309 – 311

3

Helix

314 – 333

20

Helix

335 – 337

3

Beta strand

338 – 347

10

Helix

352 – 356

5

Beta strand

359 – 361

3

Beta strand

376 – 379

4

Beta strand

388 – 390

3

Beta strand

394 – 396

3

Helix

398 – 404

7

Sequences

	Sequence		Length	Mass (Da)
	P40943-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: AD385C90B252B82A	FASTA	407	46,763
	10 20 30 40 50 60 MRNVVRKPLT IGLALTLLLP MGMTATSAKN ADSYAKKPHI SALNAPQLDQ RYKNEFTIGA 70 80 90 100 110 120 AVEPYQLQNE KDVQMLKRHF NSIVAENVMK PISIQPEEGK FNFEQADRIV KFAKANGMDI 130 140 150 160 170 180 RFHTLVWHSQ VPQWFFLDKE GKPMVNETDP VKREQNKQLL LKRLETHIKT IVERYKDDIK 190 200 210 220 230 240 YWDVVNEVVG DDGKLRNSPW YQIAGIDYIK VAFQAARKYG GDNIKLYMND YNTEVEPKRT 250 260 270 280 290 300 ALYNLVKQLK EEGVPIDGIG HQSHIQIGWP SEAEIEKTIN MFAALGLDNQ ITELDVSMYG 310 320 330 340 350 360 WPPRAYPTYD AIPKQKFLDQ AARYDRLFKL YEKLSDKISN VTFWGIADNH TWLDSRADVY 370 380 390 400 YDANGNVVVD PNAPYAKVEK GKGKDAPFVF GPDYKVKPAY WAIIDHK

References

[1]	"Cloning and DNA sequence of the gene coding for Bacillus stearothermophilus T-6 xylanase." Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y. Appl. Environ. Microbiol. 60:1889-1896(1994) [PubMed: 8031084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: T-6 / NCIMB 40221.
[2]	"Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6." Khasin A., Alchanati I., Shoham Y. Appl. Environ. Microbiol. 59:1725-1730(1993) [PubMed: 8328796] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-73. Strain: T-6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ868502 Genomic DNA. Translation: ABI49951.1. Different initiation.

PIR

I40570.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HIZ	X-ray	2.40	A	29-407	[»]
1R85	X-ray	1.45	A	29-407	[»]
1R86	X-ray	1.80	A	29-407	[»]
1R87	X-ray	1.67	A	29-407	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA

3.2.1.8. 266715.

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR017853. Glyco_hydro_catalytic_core.
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

XYN1_BACST

Accession

Primary (citable) accession number: P40943
Secondary accession number(s): Q09LX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)