Endo-1,4-beta-xylanase - Bacillus subtilis

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Unreviewed, UniProtKB/TrEMBL Q7SID8 (Q7SID8_BACSU)

Last modified May 5, 2009. Version 38. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names	Recommended name: Endo-1,4-beta-xylanase RuleBase RU004392V0 EC=3.2.1.8
Organism	Bacillus subtilis PDB 1IGO
Taxonomic identifier	1423 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. RuleBase RU004392V0
Pathway	Glycan degradation; xylan degradation. RuleBase RU004392V0
Sequence similarities	Belongs to the glycosyl hydrolase 11 (cellulase G) family. RuleBase RU003433V0

Ontologies

Keywords
Biological process	Xylan degradation RuleBase RU003433V0
Molecular function	Glycosidase RuleBase RU003433V0 Hydrolase
Technical term	3D-structure PDB 1IGO
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q7SID8-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 35F4E6BC657BBC74
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205

22,562

        10         20         30         40         50         60 
ATTITSNQTG THDGYDYELW KDSGNTSMTL NSGGAFSAQW SNIGNALFRK GKKFDSTKTH 

        70         80         90        100        110        120 
SQLGNISINY NATFNPGGNS YLCVYGWTKD PLTEYYIVDN WGTYRPTGTP KGTFTVDGGT 

       130        140        150        160        170        180 
YDIYETTRIN QPSIIGIATF KQYWSVRQTK RTSGTVSVSE HFKKWESLGM PMGKMYETAL 

       190        200 
TVEGYQSNGS ANVTANVLTI GGKPL

References

[1]	Oakley A.J., Thomson C., Heinrich T., Dunlop R., Wilce M.C.J. Submitted (APR-2001) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[2]	"Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching." Oakley A.J., Heinrich T., Thompson C.A., Wilce M.C. Acta Crystallogr. D Biol. Crystallogr. 59:627-636(2003) [PubMed: 12657781] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IGO	X-ray	2.20	A/B	1-205	[»]

ModBase

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Family and domain databases

InterPro

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

Entry information

Entry name

Q7SID8_BACSU

Accession

Primary (citable) accession number: Q7SID8

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	May 5, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information