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

Q96VB6 (XYNF3_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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 F3

Short name=Xylanase F3
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F3
Gene names
Name:xynF3
Synonyms:xlnF3
ORF Names:AO090001000208
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length323 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. Ref.1

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.1 Ref.4.

Miscellaneous

The promoter does not contain any 5'-GGCTAAA-3' sequence identified as binding sites for the xylanolytic transcriptional activator xlnR.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=200 µM for birch wood xylan Ref.1

Vmax=435 µmol/min/mg enzyme

pH dependence:

Optimum pH is 5.5. Retain 85 percent of its activity in the pH range from 6.0 to 7.0 after a 12 h incubation at 25 degrees Celsius.

Temperature dependence:

Optimum temperature is 58 degrees Celsius. The purified enzyme showed complete stability under 60 degrees Celsius.

Sequence caution

The sequence BAE56751.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 323300Endo-1,4-beta-xylanase F3
PRO_0000393192

Sites

Active site1531Proton donor By similarity
Active site2591Nucleophile By similarity

Amino acid modifications

Disulfide bond277 ↔ 283 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96VB6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 474B2F7E130AD465

FASTA32334,696
        10         20         30         40         50         60 
MVHLKSLAGI LLYTSLCIAS SQQAPASINN AFVAKGKKYF GTCADQGTLS DGTNSGIIKA 

        70         80         90        100        110        120 
DFGQLTPENS MKWDATEPSQ GKFSFSGADY LVNYAATNNK LIRGHTLVWH SQLPSWVQGI 

       130        140        150        160        170        180 
TDKNTLTSVL KNHITTVMNR YKGKVYAWDV VNEIFNEDGT LRSSVFYNVL GEDFVRIAFE 

       190        200        210        220        230        240 
TARAADPQAK LYINDYNLDS ANYGKTTGLA NHVKKWIAQG IPIDGIGSQT HLSAGGSSGV 

       250        260        270        280        290        300 
KGALNTLAAS GVSEVAITEL DIAGASSNDY VNVVEACLEV SKCVGITVWG VSDKNSWRSA 

       310        320 
ESPLLFDGNY QPKSAYNAIL NAL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, characterization, and expression analysis of the xynF3 gene from Aspergillus oryzae."
Kimura T., Suzuki H., Furuhashi H., Aburatani T., Morimoto K., Sakka K., Ohmiya K.
Biosci. Biotechnol. Biochem. 66:285-292(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Gene cloning, sequencing, expression and characterization of a xylanase gene from Aspergillus niger DMS1957."
Quyen D.T., Nguyen S.L.T.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VTCC-F-187.
[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
EU848306 mRNA. Translation: ACJ26383.1.
AB066176 Genomic DNA. Translation: BAB69073.1.
AP007154 Genomic DNA. Translation: BAE56751.1. Sequence problems.
PIRJC7813.

3D structure databases

ProteinModelPortalQ96VB6.
SMRQ96VB6. Positions 23-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000185.

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10C_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000019847.
OrthoDBEOG7GJ6PM.

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.
ProtoNetSearch...

Entry information

Entry nameXYNF3_ASPOR
AccessionPrimary (citable) accession number: Q96VB6
Secondary accession number(s): Q2UNW4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 64 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