Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P55330 (XYNB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 73. 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:
Endo-1,4-beta-xylanase B

Short name=Xylanase B
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Endo-1,4-beta-xylanase G1
Short name=Xylanase G1
Endo-1,4-beta-xylanase II
Short name=Xylanase II
Gene names
Name:xlnB
Synonyms:xyn2, xynB, xynG1
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.4 Ref.5

Catalytic activity

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

Enzyme regulation

Metal ions, copper, iron and N-bromosuccinimide decrease enzyme activity. Manganese, calcium, L-tryptophan, beta-mercaptoethanol, L-cysteine and dithiodipyridine stimulate the enzyme activity. Ref.4

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted By similarity.

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Retains about 76 percent of its activity after being incubated at pH 2.0 for 30 min at 37 degrees Celsius. Ref.4 Ref.5

Temperature dependence:

Optimum temperature is 50 degrees Celsius. Displays about 95 percent of peak activity in the temperature range from 37 to 41 degrees Celsius.

Ontologies

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

Inferred from direct assay. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 3719
PRO_0000007993
Chain38 – 225188Endo-1,4-beta-xylanase B
PRO_0000007994

Sites

Active site1211Nucleophile By similarity
Active site2121Proton donor By similarity

Experimental info

Sequence conflict161A → V in AAM08362. Ref.2
Sequence conflict161A → V in AAM95167. Ref.3
Sequence conflict161A → V in ABA00146. Ref.4
Sequence conflict161A → V in AAS46914. Ref.5
Sequence conflict161A → V in ACA51680. Ref.7
Sequence conflict25 – 262AQ → VE in AAM08362. Ref.2
Sequence conflict25 – 262AQ → VE in AAM95167. Ref.3
Sequence conflict25 – 262AQ → VE in ABA00146. Ref.4
Sequence conflict25 – 262AQ → VE in AAS46914. Ref.5
Sequence conflict25 – 262AQ → VE in ACA51680. Ref.7
Sequence conflict331M → K in AAM08362. Ref.2
Sequence conflict331M → K in AAM95167. Ref.3
Sequence conflict331M → K in ABA00146. Ref.4
Sequence conflict331M → K in AAS46914. Ref.5
Sequence conflict331M → K in ACA51680. Ref.7
Sequence conflict701A → S in AAM08362. Ref.2
Sequence conflict701A → S in AAM95167. Ref.3
Sequence conflict701A → S in ABA00146. Ref.4
Sequence conflict701A → S in AAS46914. Ref.5
Sequence conflict701A → S in ACA51680. Ref.7
Sequence conflict761S → P in ACJ26382. Ref.8
Sequence conflict1301D → V in ACA24724. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P55330 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C4B8BB007AB2B8FD

FASTA22524,057
        10         20         30         40         50         60 
MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY YSFWTDGGGD 

        70         80         90        100        110        120 
VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT FTPSGNGYLS VYGWTTDPLI 

       130        140        150        160        170        180 
EYYIVESYGD YNPGSGGTYK GTVTSDGSVY DIYTATRTNA ASIQGTATFT QYWSVRQNKR 

       190        200        210        220 
VGGTVTTSNH FNAWAKLGMN LGTHNYQIVA TEGYQSSGSS SITVQ 

« Hide

References

[1]Ito K.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IFO 4066 / RIB 1061.
[2]Gu S., Sun J., Xu Z., Li W., Zhao H.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"High-level expression of xylanase B of Aspergillus niger in Pichia pastoris."
Zhu L., Liu W., Dong Z., Yu W.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of a gene encoding an acidophilic endo-beta-1,4-xylanase obtained from Aspergillus niger CGMCC1067 and constitutive expression in Pichia pastoris."
Deng P., Li D., Cao Y., Lu W., Wang C.
Enzyme Microb. Technol. 39:1096-1102(2006)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[5]"Efficient expression and secretion of two co-produced xylanases from Aspergillus niger in Pichia pastoris directed by their native signal peptides and the Saccharomyces cerevisiae a-mating factor."
Korona B., Korona D., Bielecki S.
Enzyme Microb. Technol. 39:683-689(2006)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: IBT-90.
[6]"Isolation and identification of xynB from Aspergillus niger."
Su Y., Bai J., Chen G.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Cloning, expression and characterization of the xylanase B from Aspergillus niger F19 in Escherichia coli."
Cui L., Zhang Z., Zhu M., Wang C.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: F19.
[8]"Gene cloning, sequencing, expression and characterization of a xylanase 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.
[9]"Expression of Xylanase Gene xynB from Aspergillus niger in Escherichia coli and Characterization of Its Recombinant Xylanase."
Yi X., Qiao D., Cao Y.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: SCTCC 400264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38071 Genomic DNA. Translation: BAA07265.1.
AF490982 mRNA. Translation: AAM08362.1.
AY126481 Genomic DNA. Translation: AAM95167.1.
DQ174549 Genomic DNA. Translation: ABA00146.1.
AY536639 mRNA. Translation: AAS46914.1.
EU423881 Genomic DNA. Translation: ACA24724.1.
EU430370 mRNA. Translation: ACA51680.1.
EU848305 mRNA. Translation: ACJ26382.1.
FJ772090 mRNA. Translation: ACN89393.1.

3D structure databases

ProteinModelPortalP55330.
SMRP55330. Positions 39-224.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11G_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG05353.

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. SSF49899. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_ASPNG
AccessionPrimary (citable) accession number: P55330
Secondary accession number(s): B1A5N7 expand/collapse secondary AC list , C0LVA6, C6F1T2, Q12557, Q8TG22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 13, 2013
This is version 73 of the entry and version 1 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