Endo-1,4-beta-xylanase B precursor

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P55330 (XYNB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from direct assay. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay. Source: UniProtKB
Molecular_function	endo-1,4-beta-xylanase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Potential

Propeptide

19 – 37

PRO_0000007993

Chain

38 – 225

188

Endo-1,4-beta-xylanase B

PRO_0000007994

Sites

Active site

121

Nucleophile By similarity

Active site

212

Proton donor By similarity

Experimental info

Sequence conflict

A → V in AAM08362. Ref.2

Sequence conflict

A → V in AAM95167. Ref.3

Sequence conflict

A → V in ABA00146. Ref.4

Sequence conflict

A → V in AAS46914. Ref.5

Sequence conflict

A → V in ACA51680. Ref.7

Sequence conflict

25 – 26

AQ → VE in AAM08362. Ref.2

Sequence conflict

25 – 26

AQ → VE in AAM95167. Ref.3

Sequence conflict

25 – 26

AQ → VE in ABA00146. Ref.4

Sequence conflict

25 – 26

AQ → VE in AAS46914. Ref.5

Sequence conflict

25 – 26

AQ → VE in ACA51680. Ref.7

Sequence conflict

M → K in AAM08362. Ref.2

Sequence conflict

M → K in AAM95167. Ref.3

Sequence conflict

M → K in ABA00146. Ref.4

Sequence conflict

M → K in AAS46914. Ref.5

Sequence conflict

M → K in ACA51680. Ref.7

Sequence conflict

A → S in AAM08362. Ref.2

Sequence conflict

A → S in AAM95167. Ref.3

Sequence conflict

A → S in ABA00146. Ref.4

Sequence conflict

A → S in AAS46914. Ref.5

Sequence conflict

A → S in ACA51680. Ref.7

Sequence conflict

S → P in ACJ26382. Ref.8

Sequence conflict

130

D → V in ACA24724. Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P55330 [UniParc].

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

FASTA

225

24,057

        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
ProteinModelPortal	P55330.
SMR	P55330. Positions 39-224.
ModBase	Search...
Protein family/group databases
CAZy	GH11. Glycoside Hydrolase Family 11.
mycoCLAP	XYN11G_ASPNG.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG05353.
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
Gene3D	2.60.120.180. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR001137. Glyco_hydro_11. IPR013319. Glyco_hydro_11/12. IPR018208. Glyco_hydro_11_AS. [Graphical view]
Pfam	PF00457. Glyco_hydro_11. 1 hit. [Graphical view]
PRINTS	PR00911. GLHYDRLASE11.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit. PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNB_ASPNG

Accession

Primary (citable) accession number: P55330
Secondary accession number(s): B1A5N7

Q8TG22

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents