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Q00177 (XYNC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
34 kDa xylanase
Xylanase X34
Gene names
Name:xlnC
ORF Names:AN1818
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 length327 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 Ref.2

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Induction

Expressed in presence of xylan and repressed by glucose. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.9. Ref.2

Temperature dependence:

Optimum temperature is 52 degrees Celsius.

Sequence caution

The sequence CBF85620.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAA64983.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 327303Endo-1,4-beta-xylanase C
PRO_0000007974

Sites

Active site1541Proton donor By similarity
Active site2621Nucleophile By similarity

Amino acid modifications

Modified residue251Pyrrolidone carboxylic acid By similarity
Disulfide bond280 ↔ 286 Ref.5

Secondary structure

....................................................... 327
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00177 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B59CF4DE435F6F20

FASTA32735,441
        10         20         30         40         50         60 
MVHLKTLAGS AVFASLATAA VLPRQSASLN DLFVAAGKSY FGTCSDQALL QNSQNEAIVA 

        70         80         90        100        110        120 
SQFGVITPEN SMKWDALEPS QGNFGWSGAD YLVDYATQHN KKVRGHTLVW HSQLPSWVSS 

       130        140        150        160        170        180 
IGDANTLRSV MTNHINEVVG RYKGKIMHWD VVNEIFNEDG TFRNSVFYNL LGEDFVRIAF 

       190        200        210        220        230        240 
ETARAADPDA KLYINDYNLD SASYAKTQAM ASYVKKWLAE GVPIDGIGSQ AHYSSSHWSS 

       250        260        270        280        290        300 
TEAAGALSSL ANTGVSEVAI TELDIAGAAS SDYLNLLNAC LNEQKCVGIT VWGVSDKDSW 

       310        320 
RASDSPLLFD GNYQPKDAYN AIVNALS 

« Hide

References

« Hide 'large scale' references
[1]"Identification, isolation and sequence of the Aspergillus nidulans xlnC gene encoding the 34-kDa xylanase."
Maccabe A.P., Fernandez-Espinar M.-T., de Graaff L.H., Visser J., Ramon D.
Gene 175:29-33(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
[2]"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"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.
[4]"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.
[5]"The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases."
Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G., Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.
J. Biol. Chem. 279:36029-36037(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-327 IN COMPLEX WITH WHEAT XIP-1, DISULFIDE BOND.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49894 Genomic DNA. Translation: CAA90075.1.
DQ490475 mRNA. Translation: ABF50851.1.
AACD01000029 Genomic DNA. Translation: EAA64983.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF85620.1. Sequence problems.
PIRJC5034.
RefSeqXP_659422.1. XM_654330.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TA3X-ray1.70B25-327[»]
ProteinModelPortalQ00177.
SMRQ00177. Positions 27-327.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00008467; CADANIAP00008467; CADANIAG00008467.
GeneID2874673.
KEGGani:AN1818.2.

Phylogenomic databases

eggNOGCOG3693.
HOGENOMHOG000019847.
KOK01181.
OrthoDBEOG7GJ6PM.

Enzyme and pathway databases

BRENDA3.2.1.8. 9578.
UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ00177.

Entry information

Entry nameXYNC_EMENI
AccessionPrimary (citable) accession number: Q00177
Secondary accession number(s): C8VPM8, Q1HFU9, Q5BCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 99 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries