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Q12667 (XYNA_PIRSP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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 A

EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Xylanase A
Short name=XYLA
Gene names
Name:XYNA
OrganismPiromyces sp.
Taxonomic identifier45796 [NCBI]
Taxonomic lineageEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Domain

Consists of an N- and C-terminal catalytic domains linked to a middle reiterated domain. Only the C-terminal catalytic domain is active.

Sequence similarities

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

Contains 2 CBM10 (carbohydrate binding type-10) domains.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 625606Endo-1,4-beta-xylanase A
PRO_0000008017

Regions

Repeat259 – 268101
Repeat269 – 278102
Domain286 – 32338CBM10 1
Domain338 – 37033CBM10 2
Region20 – 254235Catalytic 1
Region255 – 27925Linker
Region259 – 278202 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]
Region374 – 40330Linker
Region404 – 625222Catalytic 2

Sites

Active site5101Nucleophile By similarity
Active site6031Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12667 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9DA99B6A17290922

FASTA62568,049
        10         20         30         40         50         60 
MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE QWADGGNNSA 

        70         80         90        100        110        120 
TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA EYRLVKKSAS NVGYSYVGVY 

       130        140        150        160        170        180 
GWTLQSGISG VYEYYIVDNW LSQWRPGDWV GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS 

       190        200        210        220        230        240 
LRKSERTCGT IDVTAHFAQW EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN 

       250        260        270        280        290        300 
GKDQDGKSKG GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS 

       310        320        330        340        350        360 
NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE IVLTDSDGDW 

       370        380        390        400        410        420 
GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST NTNFCSTSKH SGQSVTETSN 

       430        440        450        460        470        480 
KVGSIGGVGY ELWADSGNNS ATFYSDGSFS CSFRNAKDYL CRSGLSFDST KTYQQLGHMY 

       490        500        510        520        530        540 
ADFKLVKQNI QNVDYSYVGI YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA 

       550        560        570        580        590        600 
KYTVYENTRT GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV 

       610        620 
LGEAGSTGSG TSGTADFPYA KVYIK 

« Hide

References

[1]"The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91858 mRNA. Translation: CAA62969.1.

3D structure databases

ProteinModelPortalQ12667.
SMRQ12667. Positions 292-323.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_PIRSP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 2 hits.
3.90.1220.10. 2 hits.
InterProIPR002883. CBM10/Dockerin_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR009034. Dockerin_dom.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF02013. CBM_10. 2 hits.
PF00457. Glyco_hydro_11. 2 hits.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49899. SSF49899. 2 hits.
SSF64571. SSF64571. 2 hits.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_PIRSP
AccessionPrimary (citable) accession number: Q12667
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 79 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries