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O94163 (XYNF1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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 F1

Short name=Xylanase F1
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase F1
Gene names
Name:xynF1
Synonyms:xlnF1
ORF Names:AO090103000423
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length327 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.3

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.3.

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Ref.3

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence caution

The sequence BAE65852.1 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.3. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.3. Source: ASPGD

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 327308Endo-1,4-beta-xylanase F1
PRO_0000393191

Sites

Active site1551Proton donor By similarity
Active site2631Nucleophile By similarity

Amino acid modifications

Disulfide bond281 ↔ 287 By similarity

Experimental info

Sequence conflict1901N → D in BAE65852. Ref.2
Sequence conflict2091K → Q in BAE65852. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O94163 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 38B2F6374BAD3D0A

FASTA32735,402
        10         20         30         40         50         60 
MVHLKALASG TLFASLASSA VISRQAAASI NDAFVAHGKK YFGTCSDQAL LQNSQNEAIV 

        70         80         90        100        110        120 
RADFGQLTPE NSMKWDALEP SQGSFSFAGA DFLADYAKTN NKLVRGHTLV WHSQLPSWVQ 

       130        140        150        160        170        180 
GITDKDTLTE VIKNHITTIM QRYKGQIYAW DVVNEIFDED GTLRDSVFSQ VLGEDFVRIA 

       190        200        210        220        230        240 
FETAREADPN AKLYINDYNL DSADYAKTKG MVSYVKKWLD AGVPIDGIGS QSHYSANGFP 

       250        260        270        280        290        300 
VSGAKGALTA LASTGVSEVA VTELDIEGAS SESYLEVVNA CLDVSSCVGI TVWGVSDKDS 

       310        320 
WRSSTSPLLF DSNYQAKDAY NAIIDAL 

« Hide

References

« Hide 'large scale' references
[1]"Repression of the expression of genes encoding xylanolytic enzymes in Aspergillus oryzae by introduction of multiple copies of the xynF1 promoter."
Kitamoto N., Yoshino S., Ito M., Kimura T., Ohmiya K., Tsukagoshi N.
Appl. Microbiol. Biotechnol. 50:558-563(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KBN616.
[2]"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.
[3]"Purification and characterization of the overexpressed Aspergillus oryzae xylanase, XynF1."
Kitamoto N., Yoshino S., Ohmiya K., Tsukagoshi N.
Biosci. Biotechnol. Biochem. 63:1791-1794(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011212 Genomic DNA. Translation: BAA75475.1.
AP007174 Genomic DNA. Translation: BAE65852.1. Sequence problems.

3D structure databases

ProteinModelPortalO94163.
SMRO94163. Positions 28-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00010097.

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10F_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3693.
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 nameXYNF1_ASPOR
AccessionPrimary (citable) accession number: O94163
Secondary accession number(s): Q2TY21
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 63 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