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P87037 (XYNB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. 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 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
Gene names
Name:xlnB
Synonyms:xynB, xynG, xynG1
ORF Names:AO090001000111
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length221 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.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.4.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
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 – 221202Probable endo-1,4-beta-xylanase B
PRO_0000393169

Sites

Active site1171Nucleophile By similarity
Active site2081Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P87037 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: C010E11E5F53C77E

FASTA22123,746
        10         20         30         40         50         60 
MVSFSSLLLA VSAVSGALAA PGDSTLVELA KRAITSSETG TNNGYYYSFW TNGGGDVEYT 

        70         80         90        100        110        120 
NGNGGQYSVK WTNCDNFVAG KGWNPGSAKT VTYSGEWESN SNSYVSLYGW TQNPLVEYYI 

       130        140        150        160        170        180 
VDKYGDYDPS TGATELGTVE SDGGTYKIYK TTRENAPSIE GTSTFNQYWS VRQSGRVGGT 

       190        200        210        220 
ITAQNHFDAW ANVGLQLGTH NYMILATEGY KSSGSATITV E 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence of xylanase G1 gene from Aspergillus oryzae KBN616."
Kimura T., Kitamoto N., Kito Y., Karita S., Sakka K., Ohmiya K.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KBN616.
[2]"Cloning and sequence analysis of the gene encoding xylanase from Aspergillus oryzae."
Han W., Su Y., Chen G.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: AS 3.4382.
[3]"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. expand/collapse author list , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[4]"Proteomic analysis of extracellular proteins from Aspergillus oryzae grown under submerged and solid-state culture conditions."
Oda K., Kakizono D., Yamada O., Iefuji H., Akita O., Iwashita K.
Appl. Environ. Microbiol. 72:3448-3457(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU586113 mRNA. Translation: ACB97629.1.
AB003085 Genomic DNA. Translation: BAA19744.1.
AP007154 Genomic DNA. Translation: BAE56664.1.
RefSeqXP_001818666.1. XM_001818614.2.

3D structure databases

ProteinModelPortalP87037.
SMRP87037. Positions 32-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000098.

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11G_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00000099; CADAORAP00000098; CADAORAG00000099.
GeneID5990637.
KEGGaor:AOR_1_174164.

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
OMATVTTKNH.
OrthoDBEOG7VQJQX.

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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_ASPOR
AccessionPrimary (citable) accession number: P87037
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: July 1, 1997
Last modified: February 19, 2014
This is version 85 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