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P55330

- XYNB_ASPNG

UniProt

P55330 - XYNB_ASPNG

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Protein
Endo-1,4-beta-xylanase B
Gene
xlnB, xyn2, xynB, xynG1
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Metal ions, copper, iron and N-bromosuccinimide decrease enzyme activity. Manganese, calcium, L-tryptophan, beta-mercaptoethanol, L-cysteine and dithiodipyridine stimulate the enzyme activity.1 Publication

pH dependencei

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.2 Publications

Temperature dependencei

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei121 – 1211Nucleophile By similarity
Active sitei212 – 2121Proton donor By similarity

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
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 namesi
Name:xlnB
Synonyms:xyn2, xynB, xynG1
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 3719
PRO_0000007993Add
BLAST
Chaini38 – 225188Endo-1,4-beta-xylanase B
PRO_0000007994Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP55330.
SMRiP55330. Positions 39-224.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55330-1 [UniParc]FASTAAdd to Basket

« Hide

MLTKNLLLCF AAAKAALAVP HDSVAQRSDA LHMLSERSTP SSTGENNGFY    50
YSFWTDGGGD VTYTNGDAGA YTVEWSNVGN FVGGKGWNPG SAQDITYSGT 100
FTPSGNGYLS VYGWTTDPLI EYYIVESYGD YNPGSGGTYK GTVTSDGSVY 150
DIYTATRTNA ASIQGTATFT QYWSVRQNKR VGGTVTTSNH FNAWAKLGMN 200
LGTHNYQIVA TEGYQSSGSS SITVQ 225
Length:225
Mass (Da):24,057
Last modified:October 1, 1996 - v1
Checksum:iC4B8BB007AB2B8FD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → V in AAM08362. 1 Publication
Sequence conflicti16 – 161A → V in AAM95167. 1 Publication
Sequence conflicti16 – 161A → V in ABA00146. 1 Publication
Sequence conflicti16 – 161A → V in AAS46914. 1 Publication
Sequence conflicti16 – 161A → V in ACA51680. 1 Publication
Sequence conflicti25 – 262AQ → VE in AAM08362. 1 Publication
Sequence conflicti25 – 262AQ → VE in AAM95167. 1 Publication
Sequence conflicti25 – 262AQ → VE in ABA00146. 1 Publication
Sequence conflicti25 – 262AQ → VE in AAS46914. 1 Publication
Sequence conflicti25 – 262AQ → VE in ACA51680. 1 Publication
Sequence conflicti33 – 331M → K in AAM08362. 1 Publication
Sequence conflicti33 – 331M → K in AAM95167. 1 Publication
Sequence conflicti33 – 331M → K in ABA00146. 1 Publication
Sequence conflicti33 – 331M → K in AAS46914. 1 Publication
Sequence conflicti33 – 331M → K in ACA51680. 1 Publication
Sequence conflicti70 – 701A → S in AAM08362. 1 Publication
Sequence conflicti70 – 701A → S in AAM95167. 1 Publication
Sequence conflicti70 – 701A → S in ABA00146. 1 Publication
Sequence conflicti70 – 701A → S in AAS46914. 1 Publication
Sequence conflicti70 – 701A → S in ACA51680. 1 Publication
Sequence conflicti76 – 761S → P in ACJ26382. 1 Publication
Sequence conflicti130 – 1301D → V in ACA24724. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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

ProteinModelPortali P55330.
SMRi P55330. Positions 39-224.
ModBasei Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG05353.

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiXYNB_ASPNG
AccessioniPrimary (citable) accession number: P55330
Secondary accession number(s): B1A5N7
, C0LVA6, C6F1T2, Q12557, Q8TG22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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