Endo-1,4-beta-xylanase - Penicillium simplicissimum

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Reviewed, UniProtKB/Swiss-Prot P56588 (XYNA_PENSI)

Last modified June 16, 2009. Version 53. 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	Penicillium simplicissimum
Taxonomic identifier	69488 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	302 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.
Pathway	Glycan degradation; xylan degradation.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	3D-structure
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

Chain

302

Endo-1,4-beta-xylanase

PRO_0000184067

Sites

Active site

1

Proton donor

Active site

1

Nucleophile

Amino acid modifications

Modified residue

1

Pyrrolidone carboxylic acid

Disulfide bond

Secondary structure

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302

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P56588-1 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: EE7821FA58687FFC
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302

32,551

        10         20         30         40         50         60 
QASVSIDAKF KAHGKKYLGT IGDQYTLTKN TKNPAIIKAD FGQLTPENSM KWDATEPNRG 

        70         80         90        100        110        120 
QFTFSGSDYL VNFAQSNGKL IRGHTLVWHS QLPGWVSSIT DKNTLISVLK NHITTVMTRY 

       130        140        150        160        170        180 
KGKIYAWDVL NEIFNEDGSL RNSVFYNVIG EDYVRIAFET ARSVDPNAKL YINDYNLDSA 

       190        200        210        220        230        240 
GYSKVNGMVS HVKKWLAAGI PIDGIGSQTH LGAGAGSAVA GALNALASAG TKEIAITELD 

       250        260        270        280        290        300 
IAGASSTDYV NVVNACLNQA KCVGITVWGV ADPDSWRSSS SPLLFDGNYN PKAAYNAIAN 


AL

References

[1]	"Structure of the xylanase from Penicillium simplicissimum." Schmidt A., Schlacher A., Steiner W., Schwab H., Kratky C. Protein Sci. 7:2081-2088(1998) [PubMed: 9792094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). Strain: BT 2246.
[2]	"Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant." Schmidt A., Gubitz G.M., Kratky C. Biochemistry 38:2403-2412(1999) [PubMed: 10029534] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Cross-references

Sequence databases

AF070417 Genomic DNA. Translation: AAC23574.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B30	X-ray	2.25	A	2-302	[»]
1B31	X-ray	1.75	A	2-302	[»]
1B3V	X-ray	2.40	A	2-302	[»]
1B3W	X-ray	2.60	A	2-302	[»]
1B3X	X-ray	2.20	A	2-302	[»]
1B3Y	X-ray	2.45	A	2-302	[»]
1B3Z	X-ray	2.30	A	2-302	[»]
1BG4	X-ray	1.75	A	2-302	[»]

ModBase

Protein family/group databases

CAZy

GH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA

3.2.1.8. 6842.

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

XYNA_PENSI

Accession

Primary (citable) accession number: P56588

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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