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C5J411 (XYNC_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable endo-1,4-beta-xylanase C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene names
Name:xlnC
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Induction

Expressed in presence of xylan and repressed by glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 327308Probable endo-1,4-beta-xylanase C
PRO_0000393190

Sites

Active site1571Proton donor By similarity
Active site2631Nucleophile By similarity

Amino acid modifications

Disulfide bond281 ↔ 287 By similarity

Experimental info

Sequence conflict11 – 133MLF → KLI in ACR83565. Ref.1
Sequence conflict231D → E in ACR83565. Ref.1
Sequence conflict771W → R in ACR83565. Ref.1
Sequence conflict1231S → A in ACR83565. Ref.1
Sequence conflict1321E → G in ACR83565. Ref.1
Sequence conflict2081S → P in ACR83565. Ref.1
Sequence conflict2681G → D in ACR83565. Ref.1
Sequence conflict2831N → D in ACR83565. Ref.1
Sequence conflict321 – 3233DAI → FAV in ACR83565. Ref.1

Sequences

Sequence LengthMass (Da)Tools
C5J411 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: 90B2F71FFCA70A65

FASTA32735,476
        10         20         30         40         50         60 
MVQIKVAALA MLFASQVLSE PIDPRQASVS IDTKFKAHGK KYLGNIGDQY TLTKNSKTPA 

        70         80         90        100        110        120 
IIKADFGALT PENSMKWDAT EPSRGQFSFS GSDYLVNFAQ SNNKLIRGHT LVWHSQLPSW 

       130        140        150        160        170        180 
VQSITDKNTL IEVMKNHITT VMQHYKGKIY AWDVVNEIFN EDGSLRDSVF YKVIGEDYVR 

       190        200        210        220        230        240 
IAFETARAAD PNAKLYINDY NLDSASYSKL TGMVSHVKKW IAAGIPIDGI GSQTHLSAGG 

       250        260        270        280        290        300 
GAGISGALNA LAGAGTKEIA VTELDIAGAS STDYVEVVEA CLNQPKCIGI TVWGVADPDS 

       310        320 
WRSSSTPLLF DSNYNPKPAY DAIANAL 

« Hide

References

[1]"Gene cloning, sequencing, expression and characterization of a xylanase A gene from Aspergillus niger DMS1957."
Nguyen S.L.T., Quyen D.T.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: DMS1957.
[2]Huang J.Z., Xu Y., Tian B.Y., Huang Q.G.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: IME-216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ986225 mRNA. Translation: ACR83565.1.
EU848304 mRNA. Translation: ACJ26381.1.

3D structure databases

ProteinModelPortalC5J411.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3693.

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNC_ASPNG
AccessionPrimary (citable) accession number: C5J411
Secondary accession number(s): C6F1T1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 23, 2010
Last modified: November 13, 2013
This is version 23 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries