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Reviewed, UniProtKB/Swiss-Prot Q00177 (XYNC_EMENI)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Aspergillus nidulans)
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

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Protein attributes

Sequence length327 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Sequence similarities

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

Sequence caution

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

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Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical term3D-structure
Gene Ontology (GO)
   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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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.4

Secondary structure

1 ....................................................... 327
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q00177-1 [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

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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: 8917072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 16844780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FGSC A4 Glasgow.
[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: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC 4.
[4]"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: 15181003] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-327 IN COMPLEX WITH WHEAT XIP-1, DISULFIDE BOND.

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Cross-references

Sequence databases

Z49894 Genomic DNA. Translation: CAA90075.1.
DQ490475 mRNA. Translation: ABF50851.1.
AACD01000029 Genomic DNA. Translation: EAA64983.1.
PIRJC5034.
RefSeqXP_659422.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TA3X-ray1.70B25-327[»]
ModBaseSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Genome annotation databases

GeneID2874673.
KEGGani:AN1818.2.

Enzyme and pathway databases

BRENDA3.2.1.8. 3859.

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYNC_EMENI
AccessionPrimary (citable) accession number: Q00177
Secondary accession number(s): Q1HFU9, Q5BCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents