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P33557 (XYN3_ASPKW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase 3
Short name=Xylanase 3
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase 3
Xylanase C
Gene names
Name:xynC
ORF Names:AKAW_07136
OrganismAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi) [Complete proteome]
Taxonomic identifier1033177 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.1
Chain28 – 211184Endo-1,4-beta-xylanase 3
PRO_0000007991

Sites

Active site1061Nucleophile By similarity
Active site1971Proton donor

Amino acid modifications

Disulfide bond119 ↔ 138

Experimental info

Sequence conflict71F → S in AAC60542. Ref.1
Sequence conflict71F → S in BAA03576. Ref.1
Sequence conflict12 – 132VT → GH in AAC60542. Ref.1
Sequence conflict12 – 132VT → GH in BAA03576. Ref.1
Sequence conflict211E → Q in AAC60542. Ref.1
Sequence conflict211E → Q in BAA03576. Ref.1
Sequence conflict421G → A in AAC60542. Ref.1
Sequence conflict421G → A in BAA03576. Ref.1
Sequence conflict801T → S in AAC60542. Ref.1
Sequence conflict801T → S in BAA03576. Ref.1

Secondary structure

1 .............................. 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33557 [UniParc].

Last modified March 21, 2012. Version 2.
Checksum: 86EFBEE12A869022

FASTA21122,627
        10         20         30         40         50         60 
MKVTAAFAGL LVTAFAAPVP EPVLVSRSAG INYVQNYNGN LGDFTYDESA GTFSMYWEDG 

        70         80         90        100        110        120 
VSSDFVVGLG WTTGSSNAIT YSAEYSASGS SSYLAVYGWV NYPQAEYYIV EDYGDYNPCS 

       130        140        150        160        170        180 
SATSLGTVYS DGSTYQVCTD TRTNEPSITG TSTFTQYFSV RESTRTSGTV TVANHFNFWA 

       190        200        210 
QHGFGNSDFN YQVMAVEAWS GAGSASVTIS S

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the xynC gene encoding acid xylanase of Aspergillus kawachii."
Ito K., Iwashita K., Iwano K.
Biosci. Biotechnol. Biochem. 56:1338-1340(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-34.
Strain: NBRC 4308.
[2]"Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBRC 4308.
[3]"Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp-37 for catalysis at low pH."
Fushinobu S., Ito K., Konno M., Wakagi T., Matsuzawa H.
Protein Eng. 11:1121-1128(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-210.
Strain: NBRC 4308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S45138 Genomic DNA. Translation: AAC60542.1.
D14848 Genomic DNA. Translation: BAA03576.1.
DF126466 Genomic DNA. Translation: GAA89022.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK1X-ray2.00A28-211[»]
3RI8X-ray2.00A28-211[»]
3RI9X-ray2.00A28-211[»]
ProteinModelPortalP33557.
SMRP33557. Positions 29-210.
ModBaseSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11C_ASPKA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33557.

Entry information

Entry nameXYN3_ASPKW
AccessionPrimary (citable) accession number: P33557
Secondary accession number(s): G7XQI2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 21, 2012
Last modified: April 3, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

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