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Protein

Probable endo-1,4-beta-xylanase B

Gene

xlnB

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei117 – 1171NucleophilePROSITE-ProRule annotation
Active sitei208 – 2081Proton donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. 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

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11G_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Endo-1,4-beta-xylanase G1
Short name:
Xylanase G1
Gene namesi
Name:xlnB
Synonyms:xynB, xynG, xynG1
ORF Names:AO090001000111
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 2

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 221202Probable endo-1,4-beta-xylanase BPRO_0000393169Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00000098.

Structurei

3D structure databases

ProteinModelPortaliP87037.
SMRiP87037. Positions 32-220.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
OMAiVTTKNHF.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P87037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFSSLLLA VSAVSGALAA PGDSTLVELA KRAITSSETG TNNGYYYSFW
60 70 80 90 100
TNGGGDVEYT NGNGGQYSVK WTNCDNFVAG KGWNPGSAKT VTYSGEWESN
110 120 130 140 150
SNSYVSLYGW TQNPLVEYYI VDKYGDYDPS TGATELGTVE SDGGTYKIYK
160 170 180 190 200
TTRENAPSIE GTSTFNQYWS VRQSGRVGGT ITAQNHFDAW ANVGLQLGTH
210 220
NYMILATEGY KSSGSATITV E
Length:221
Mass (Da):23,746
Last modified:June 30, 1997 - v1
Checksum:iC010E11E5F53C77E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU586113 mRNA. Translation: ACB97629.1.
AB003085 Genomic DNA. Translation: BAA19744.1.
AP007154 Genomic DNA. Translation: BAE56664.1.
RefSeqiXP_001818666.1. XM_001818614.2.

Genome annotation databases

EnsemblFungiiCADAORAT00000099; CADAORAP00000098; CADAORAG00000099.
GeneIDi5990637.
KEGGiaor:AOR_1_174164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU586113 mRNA. Translation: ACB97629.1.
AB003085 Genomic DNA. Translation: BAA19744.1.
AP007154 Genomic DNA. Translation: BAE56664.1.
RefSeqiXP_001818666.1. XM_001818614.2.

3D structure databases

ProteinModelPortaliP87037.
SMRiP87037. Positions 32-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00000098.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11G_ASPOR.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00000099; CADAORAP00000098; CADAORAG00000099.
GeneIDi5990637.
KEGGiaor:AOR_1_174164.

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
OMAiVTTKNHF.
OrthoDBiEOG7VQJQX.

Enzyme and pathway databases

UniPathwayiUPA00114.

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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (MAR-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 (FEB-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.
    , 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(2004) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiXYNB_ASPOR
AccessioniPrimary (citable) accession number: P87037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 22, 2010
Last sequence update: June 30, 1997
Last modified: January 6, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.