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Q9HFA4 (XYNA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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 A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase G2
Short name=Xylanase G2
Gene names
Name:xlnA
Synonyms:xlnG2, xynG2
ORF Names:AO090120000026
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length232 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.4.

Miscellaneous

The promoter contains two 5'-GGCTAAA-3' sequences identified as binding sites for the xylanolytic transcriptional activator xlnR.

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=242.8 µM for birch wood xylan Ref.1

Vmax=123 µmol/min/mg enzyme

pH dependence:

Optimum pH is 6.0. Retains over 95 percent activity in the pH range from 5.0 to 7.0, and 70 percent activity in the pH range from 4.0 to 8.0.

Temperature dependence:

Optimum temperature is 58 degrees Celsius. Has complete stability at 60 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
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: ASPGD

   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 – 1919 Potential
Chain20 – 232213Endo-1,4-beta-xylanase A
PRO_0000393162

Sites

Active site1281Nucleophile By similarity
Active site2191Proton donor By similarity

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9HFA4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 1F73104751EA561C

FASTA23224,605
        10         20         30         40         50         60 
MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST GYNNGYYYSF 

        70         80         90        100        110        120 
WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR AITYSGSFNP SGNGYLAVYG 

       130        140        150        160        170        180 
WTTDPLIEYY IVESYGTYNP GSGGTYKGQV TSDGGTYNIY TSVRTNAPSI IGTATFTQFW 

       190        200        210        220        230 
SVRTSKRVGG TVTTGNHFNA WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, overexpression, and purification of a major xylanase from Aspergillus oryzae."
Kimura T., Suzuki H., Furuhashi H., Aburatani T., Morimoto K., Karita S., Sakka K., Ohmiya K.
Biosci. Biotechnol. Biochem. 64:2734-2738(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-64, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Gene cloning, sequencing, expression and characterization of a beta-xylanase gene from Aspergillus oryzae VTCC-F187."
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
EU848307 mRNA. Translation: ACJ26384.1.
AB044941 Genomic DNA. Translation: BAB20794.1.
AP007166 Genomic DNA. Translation: BAE62665.1.
PIRJC7577.
RefSeqXP_001823798.1. XM_001823746.2.

3D structure databases

ProteinModelPortalQ9HFA4.
SMRQ9HFA4. Positions 46-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00010980.

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_ASPOR.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00011206; CADAORAP00010980; CADAORAG00011206.
GeneID5996057.
KEGGaor:AOR_1_38094.

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
OMANETALHE.
OrthoDBEOG7VQJQX.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16226.
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.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_ASPOR
AccessionPrimary (citable) accession number: Q9HFA4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 75 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