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P29127 (XYNA_NEOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 97. 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:
Bifunctional endo-1,4-beta-xylanase A

Short name=XYLA
EC=3.2.1.8
Gene names
Name:XYNA
OrganismNeocallimastix patriciarum (Rumen fungus)
Taxonomic identifier4758 [NCBI]
Taxonomic lineageEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeNeocallimastix

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes xylans into xylobiose and xylose.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

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
   Technical term3D-structure
Multifunctional enzyme
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 – 1818 Potential
Chain19 – 607589Bifunctional endo-1,4-beta-xylanase A
PRO_0000008016

Regions

Domain524 – 56239CBM10 1
Domain566 – 60540CBM10 2
Region30 – 255226Catalytic 1
Region275 – 499225Catalytic 2
Compositional bias256 – 27419Ser/Thr-rich (linker)
Compositional bias500 – 52324Ser/Thr-rich (linker)

Sites

Active site1411Nucleophile By similarity
Active site2231Proton donor By similarity
Active site3861Nucleophile By similarity
Active site4741Proton donor By similarity

Secondary structure

.............................. 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29127 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 9C5B73A67D0CC780

FASTA60766,175
        10         20         30         40         50         60 
MRTIKFFFAV AIATVAKAQW GGGGASAGQR LTVGNGQTQH KGVADGYSYE IWLDNTGGSG 

        70         80         90        100        110        120 
SMTLGSGATF KAEWNASVNR GNFLARRGLD FGSQKKATDY SYIGLDYTAT YRQTGSASGN 

       130        140        150        160        170        180 
SRLCVYGWFQ NRGVQGVPLV EYYIIEDWVD WVSDAQGRMV TIDGAQYKIF QMDHTGPTIN 

       190        200        210        220        230        240 
GGSETFKQYF SVRQQKRTSG HITVSDHFKE WAKQGWGIGN LYEVALNAEG WQSSGIADVT 

       250        260        270        280        290        300 
KLDVYTTQKG SNPAPTSTGT VPSSSAGGST ANGKKFTVGN GQNQHKGVND GFSYEIWLDN 

       310        320        330        340        350        360 
TGGNGSMTLG SGATFKAEWN AAVNRGNFLA RRGLDFGSQK KATDYDYIGL DYAATYKQTA 

       370        380        390        400        410        420 
SASGNSRLCV YGWFQNRGLN GVPLVEYYII EDWVDWVPDA QGKMVTIDGA QYKIFQMDHT 

       430        440        450        460        470        480 
GPTINGGSET FKQYFSVRQQ KRTSGHITVS DHFKEWAKQG WGIGNLYEVA LNAEGWQSSG 

       490        500        510        520        530        540 
VADVTLLDVY TTPKGSSPAT SAAPRTTTRT TTRTKSLPTN YNKCSARITA QGYKCCSDPN 

       550        560        570        580        590        600 
CVVYYTDEDG TWGVENNDWC GCGVEQCSSK ITSQGYKCCS DPNCVVFYTD DDGKWGVENN 


DWCGCGF 

« Hide

References

[1]"Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin."
Gilbert H.J., Hazlewood G.P., Laurie J.I., Orpin C.G., Xue G.P.
Mol. Microbiol. 6:2065-2072(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65526 mRNA. Translation: CAA46498.1.
PIRS24754.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C1FX-ray2.10A275-499[»]
2VG9X-ray2.00A275-492[»]
ProteinModelPortalP29127.
SMRP29127. Positions 30-247, 275-492, 529-562, 572-605.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH11. Glycoside Hydrolase Family 11.
mycoCLAPXYN11A_NEOPA.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.8. 6834.
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. 2 hits.
PS00777. GLYCOSYL_HYDROL_F11_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29127.

Entry information

Entry nameXYNA_NEOPA
AccessionPrimary (citable) accession number: P29127
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 11, 2013
This is version 97 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