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P55333 (XYNB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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 B

Short name=Xylanase B
EC=3.2.1.8
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 names
Name:xlnB
Synonyms:xynB, xynG1
ORF Names:AN9365
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.1.

Induction

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. Ref.4 Ref.5 Ref.6

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from direct assay Ref.1. Source: ASPGD

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay Ref.1. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 221203Endo-1,4-beta-xylanase B
PRO_0000008005

Sites

Active site1171Nucleophile By similarity
Active site2081Proton donor By similarity

Experimental info

Sequence conflict731N → K in CAA90074. Ref.1
Sequence conflict981N → I in CAA90074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P55333 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: B762F0BB4B3F77C3

FASTA22123,504
        10         20         30         40         50         60 
MVSFSSLLLA CSAVTAFAAP SDQSIAERSL SERSTPSSTG TSGGYYYSFW TDGGGDVTYT 

        70         80         90        100        110        120 
NGDGGSYTVE WTNVGNFVGG KGWNPGSSQT ISYSGSFNPS GNGYLSVYGW TQNPLIEYYI 

       130        140        150        160        170        180 
VESYGDYNPG TAGTHQGTLE SDGSTYDIYT ATRENAPSIE GTATFTQFWS VRQSKRTSGS 

       190        200        210        220 
VTTQNHFDAW SQLGMTLGTH NYQIVAVEGY QSSGSASITV S 

« Hide

References

« Hide 'large scale' references
[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]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49893 Genomic DNA. Translation: CAA90074.1.
AACD01000172 Genomic DNA. Translation: EAA66432.1.
BN001308 Genomic DNA. Translation: CBF87481.1.
PIRS57469.
RefSeqXP_682634.1. XM_677542.1.

3D structure databases

ProteinModelPortalP55333.
SMRP55333. Positions 39-221.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11B_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00001152; CADANIAP00001152; CADANIAG00001152.
GeneID2867930.
KEGGani:AN9365.2.

Phylogenomic databases

eggNOGNOG05353.
HOGENOMHOG000179135.
KOK01181.
OMAEYYIVET.
OrthoDBEOG7VQJQX.

Enzyme and pathway databases

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 nameXYNB_EMENI
AccessionPrimary (citable) accession number: P55333
Secondary accession number(s): C8VR70, Q00176, Q5AQR5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: May 14, 2014
This is version 90 of the entry and version 2 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