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Protein

Endo-1,4-beta-xylanase B

Gene

xlnB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

Pathway: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

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

GO - Molecular functioni

GO - Biological processi

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.

Names & Taxonomyi

Protein namesi
Recommended name:
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
24 kDa xylanase
Endo-1,4-beta-xylanase G1
Short name:
Xylanase G1
Xylanase X24
Gene namesi
Name:xlnB
Synonyms:xynB, xynG1
ORF Names:AN9365
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VIII

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 221203Endo-1,4-beta-xylanase BPRO_0000008005Add
BLAST

Expressioni

Inductioni

Expressed in the presence of D-xylose under conditions of acidic ambient pH, probably under the regulation of the pacC transcription factor. Repressed in presence of glucose through the action of the creA transcription repressor.3 Publications

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00001152.

Structurei

3D structure databases

ProteinModelPortaliP55333.
SMRiP55333. Positions 39-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
InParanoidiP55333.
KOiK01181.
OMAiSEGYHNG.
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.

P55333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFSSLLLA CSAVTAFAAP SDQSIAERSL SERSTPSSTG TSGGYYYSFW
60 70 80 90 100
TDGGGDVTYT NGDGGSYTVE WTNVGNFVGG KGWNPGSSQT ISYSGSFNPS
110 120 130 140 150
GNGYLSVYGW TQNPLIEYYI VESYGDYNPG TAGTHQGTLE SDGSTYDIYT
160 170 180 190 200
ATRENAPSIE GTATFTQFWS VRQSKRTSGS VTTQNHFDAW SQLGMTLGTH
210 220
NYQIVAVEGY QSSGSASITV S
Length:221
Mass (Da):23,504
Last modified:May 1, 2007 - v2
Checksum:iB762F0BB4B3F77C3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731N → K in CAA90074 (PubMed:8787417).Curated
Sequence conflicti98 – 981N → I in CAA90074 (PubMed:8787417).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49893 Genomic DNA. Translation: CAA90074.1.
AACD01000172 Genomic DNA. Translation: EAA66432.1.
BN001308 Genomic DNA. Translation: CBF87481.1.
PIRiS57469.
RefSeqiXP_682634.1. XM_677542.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001152; CADANIAP00001152; CADANIAG00001152.
GeneIDi2867930.
KEGGiani:AN9365.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49893 Genomic DNA. Translation: CAA90074.1.
AACD01000172 Genomic DNA. Translation: EAA66432.1.
BN001308 Genomic DNA. Translation: CBF87481.1.
PIRiS57469.
RefSeqiXP_682634.1. XM_677542.1.

3D structure databases

ProteinModelPortaliP55333.
SMRiP55333. Positions 39-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00001152.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00001152; CADANIAP00001152; CADANIAG00001152.
GeneIDi2867930.
KEGGiani:AN9365.2.

Phylogenomic databases

eggNOGiNOG05353.
HOGENOMiHOG000179135.
InParanoidiP55333.
KOiK01181.
OMAiSEGYHNG.
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.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes."
    Perez-Gonzalez J.A., de Graaff L.H., Visser J., Ramon D.
    Appl. Environ. Microbiol. 62:2179-2182(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "Opposite patterns of expression of two Aspergillus nidulans xylanase genes with respect to ambient pH."
    MacCabe A.P., Orejas M., Perez-Gonzalez J.A., Ramon D.
    J. Bacteriol. 180:1331-1333(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "The wide-domain carbon catabolite repressor CreA indirectly controls expression of the Aspergillus nidulans xlnB gene, encoding the acidic endo-beta-(1,4)-xylanase X(24)."
    Orejas M., MacCabe A.P., Perez-Gonzalez J.A., Kumar S., Ramon D.
    J. Bacteriol. 183:1517-1523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "CreA mediates repression of the regulatory gene xlnR which controls the production of xylanolytic enzymes in Aspergillus nidulans."
    Tamayo E.N., Villanueva A., Hasper A.A., de Graaff L.H., Ramon D., Orejas M.
    Fungal Genet. Biol. 45:984-993(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiXYNB_EMENI
AccessioniPrimary (citable) accession number: P55333
Secondary accession number(s): C8VR70, Q00176, Q5AQR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: June 24, 2015
This is version 96 of the entry and version 2 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.