Endo-1,4-beta-xylanase precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P09850 (XYNA_BACCI)

Last modified June 16, 2009. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

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:

xlnA

Organism

Bacillus circulans

Taxonomic identifier

1397 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Hide | Top

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

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

Hide | Top

Ontologies

Keywords
Biological process	Xylan degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

Chain

29 – 213

185

Endo-1,4-beta-xylanase Ref.1

PRO_0000007996

Sites

Active site

106

Nucleophile Ref.2

Active site

200

Proton donor Ref.2

Secondary structure

213

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P09850-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 4BA0A35238CC0135
Show »

FASTA

213

23,359

        10         20         30         40         50         60 
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS GGNYSVNWSN 

        70         80         90        100        110        120 
TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT RSPLIEYYVV DSWGTYRPTG 

       130        140        150        160        170        180 
TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR TTFTQYWSVR QSKRPTGSNA TITFTNHVNA 

       190        200        210 
WKSHGMNLGS NWAYQVMATE GYQSSGSSNV TVW

« Hide

Hide | Top

References

[1]	"Nucleotide sequence of a Bacillus circulans xylanase gene." Yang R.C.A., MacKenzie C.R., Narang S.A. Nucleic Acids Res. 16:7187-7187(1988) [PubMed: 3405767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase." Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M. Protein Sci. 3:467-475(1994) [PubMed: 8019418] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS.
[3]	"The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of Bacillus circulans xylanase." McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Koerner M., Plesniak L.A., Ziser L., Wakarchuk W.W., Withers S.G. Biochemistry 35:9958-9966(1996) [PubMed: 8756457] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X07723 Genomic DNA. Translation: CAA30553.1.

PIR

S01734.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCX	X-ray	1.81	A	29-213	[»]
1BVV	X-ray	1.80	A	29-213	[»]
1C5H	X-ray	1.55	A	29-213	[»]
1C5I	X-ray	1.80	A	29-213	[»]
1HV0	X-ray	1.60	A	29-213	[»]
1HV1	X-ray	1.80	A	29-213	[»]
1XNB	X-ray	1.49	A	29-213	[»]
1XNC	X-ray	1.60	A	29-213	[»]
2BVV	X-ray	1.50	A	29-213	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH11. Glycoside Hydrolase Family 11.

Enzyme and pathway databases

BRENDA

3.2.1.8. 1207.

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

Search...

Hide | Top

Entry information

Entry name

XYNA_BACCI

Accession

Primary (citable) accession number: P09850

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 72 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)

Hide | Top