Endo-1,4-beta-xylanase precursor - Bacillus stearothermophilus

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Reviewed, UniProtKB/Swiss-Prot P40943 (XYN1_BACST)

Last modified June 16, 2009. Version 66. History...

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

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

28

Chain

379

Endo-1,4-beta-xylanase

PRO_0000007968

Sites

Active site

1

Proton donor By similarity

Active site

1

Nucleophile By similarity

Secondary structure

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407

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P40943-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: AD385C90B252B82A
Show »

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

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

PIR

3D structure databases

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

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.
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

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:	June 16, 2009
This is version 66 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)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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