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Protein

Endo-1,4-beta-xylanase A

Gene

xlnA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=242.8 µM for birch wood xylan1 Publication
  1. Vmax=123 µmol/min/mg enzyme1 Publication

pH dependencei

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 8.0.1 Publication

Temperature dependencei

Optimum temperature is 58 degrees Celsius. Has complete stability at 60 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei128 – 1281NucleophilePROSITE-ProRule annotation
Active sitei219 – 2191Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  • endo-1,4-beta-xylanase activity Source: UniProtKB

GO - Biological processi

  • xylan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16226.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Endo-1,4-beta-xylanase G2
Short name:
Xylanase G2
Gene namesi
Name:xlnA
Synonyms:xlnG2, xynG2
ORF Names:AO090120000026
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 232213Endo-1,4-beta-xylanase APRO_0000393162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00010980.

Structurei

3D structure databases

ProteinModelPortaliQ9HFA4.
SMRiQ9HFA4. Positions 46-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
OMAiYDILQTT.
OrthoDBiEOG7VQJQX.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9HFA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFSSILLA CSAAIGALAT PIEPLADHPN EAFNETAFND LVGRSTPSST
60 70 80 90 100
GYNNGYYYSF WTDGGGDVTY TNGNGGSYSV QWSNVGNFVG GKGWNPGSSR
110 120 130 140 150
AITYSGSFNP SGNGYLAVYG WTTDPLIEYY IVESYGTYNP GSGGTYKGQV
160 170 180 190 200
TSDGGTYNIY TSVRTNAPSI IGTATFTQFW SVRTSKRVGG TVTTGNHFNA
210 220 230
WAKYGLTLGT HNYQIVATEG YQSSGSSAIT VY
Length:232
Mass (Da):24,605
Last modified:March 1, 2001 - v1
Checksum:i1F73104751EA561C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU848307 mRNA. Translation: ACJ26384.1.
AB044941 Genomic DNA. Translation: BAB20794.1.
AP007166 Genomic DNA. Translation: BAE62665.1.
PIRiJC7577.
RefSeqiXP_001823798.1. XM_001823746.2.

Genome annotation databases

EnsemblFungiiCADAORAT00011206; CADAORAP00010980; CADAORAG00011206.
GeneIDi5996057.
KEGGiaor:AOR_1_38094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU848307 mRNA. Translation: ACJ26384.1.
AB044941 Genomic DNA. Translation: BAB20794.1.
AP007166 Genomic DNA. Translation: BAE62665.1.
PIRiJC7577.
RefSeqiXP_001823798.1. XM_001823746.2.

3D structure databases

ProteinModelPortaliQ9HFA4.
SMRiQ9HFA4. Positions 46-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00010980.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_ASPOR.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00011206; CADAORAP00010980; CADAORAG00011206.
GeneIDi5996057.
KEGGiaor:AOR_1_38094.

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
OMAiYDILQTT.
OrthoDBiEOG7VQJQX.

Enzyme and pathway databases

UniPathwayiUPA00114.
BioCyciMetaCyc:MONOMER-16226.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiXYNA_ASPOR
AccessioniPrimary (citable) accession number: Q9HFA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.