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P23360 (XYNA_THEAU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 92. 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

Short name=Xylanase
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
TAXI
Gene names
Name:XYNA
OrganismThermoascus aurantiacus
Taxonomic identifier5087 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeThermoascus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

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

Caution

Ref.2, Ref.3 and Ref.5 N-terminal modification was incorrect. X-ray structure has cyclic pyroglutamic acid.

Sequence caution

The sequence described in Ref.2 differs from that shown. Reason: Sequencing errors.

The sequence described in Ref.3 differs from that shown. Reason: Sequencing errors.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2 Ref.3 Ref.4
Chain27 – 329303Endo-1,4-beta-xylanase
PRO_0000007985

Sites

Active site1571Proton donor
Active site2631Nucleophile

Amino acid modifications

Modified residue271Pyrrolidone carboxylic acid
Disulfide bond281 ↔ 287

Experimental info

Sequence conflict2431G → S in CAB65468. Ref.1
Sequence conflict2431G → S in AAF24127. Ref.1
Sequence conflict2711P → S in CAB65468. Ref.1
Sequence conflict2711P → S in AAF24127. Ref.1

Secondary structure

........................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23360 [UniParc].

Last modified April 27, 2001. Version 4.
Checksum: 8FE2F3D1A9F89815

FASTA32935,686
        10         20         30         40         50         60 
MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ NRLTTGKNAA 

        70         80         90        100        110        120 
IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ QNGKLIRGHT LVWHSQLPSW 

       130        140        150        160        170        180 
VSSITDKNTL TNVMKNHITT LMTRYKGKIR AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP 

       190        200        210        220        230        240 
IAFQTARAAD PNAKLYINDY NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ 

       250        260        270        280        290        300 
GAGVLQALPL LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS 

       310        320 
WRASTTPLLF DGNFNPKPAY NAIVQDLQQ 

« Hide

References

[1]"Cloning, sequencing and overexpression of Thermoascus aurantiacus xylanase A (xynA)."
Bousson J.-C., Parriche M.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Significance of structural homology of Thermoascus aurantiacus xylanase with the exoglucanase of Cellulomonas fimi."
Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R.
J. Protein Chem. 9:337-338(1990)
Cited for: PROTEIN SEQUENCE OF 27-328.
[3]"The primary structure of xylanase from Thermoascus aurantiacus."
Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K., Vithayathil P.J.
Protein Seq. Data Anal. 4:15-20(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-328.
[4]"Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I."
Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C.
Acta Crystallogr. D 57:385-392(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-328, X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
Strain: IMI 216529.
[5]"High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture."
Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W.
Proteins 36:295-306(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
Strain: IMI 216529.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132635 Genomic DNA. Translation: CAB65468.1.
AF127529 Genomic DNA. Translation: AAF24127.1.
PIRA59381.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GOKX-ray1.14A28-329[»]
1GOMX-ray1.92A28-329[»]
1GOOX-ray1.87A28-329[»]
1GOQX-ray1.80A28-329[»]
1GORX-ray1.70A28-329[»]
1I1WX-ray0.89A28-329[»]
1I1XX-ray1.11A28-329[»]
1K6AX-ray1.14A27-329[»]
1TUXX-ray1.80A28-325[»]
2BNJX-ray1.60A28-329[»]
3NYDX-ray1.23A/B28-329[»]
3O2LX-ray2.00A28-329[»]
4BS0X-ray1.09A/B28-329[»]
ProteinModelPortalP23360.
SMRP23360. Positions 27-328.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
mycoCLAPXYN10A_THEAU.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23360.

Entry information

Entry nameXYNA_THEAU
AccessionPrimary (citable) accession number: P23360
Secondary accession number(s): Q9UQZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 27, 2001
Last modified: January 22, 2014
This is version 92 of the entry and version 4 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries