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Reviewed, UniProtKB/Swiss-Prot P45796 (XYND_PAEPO)

Last modified November 25, 2008. Version 54. 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 D
      Short name=Xylanase D
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase D
Gene names
Name: xynD
OrganismPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

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Protein attributes

Sequence length635 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)

Function

Shows xylanase activity as well as alpha-L-arabinofuranosidase activity.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

Contains 2 CBM6 (carbohydrate binding type-6) domains.

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Ontologies

Keywords

   Biological processXylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure

Gene Ontology (GO)

   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncarbohydrate 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 – 2626 Potential
Chain27 – 635609Endo-1,4-beta-xylanase D
PRO_0000012202

Regions

Domain379 – 508130CBM6 1
Domain517 – 634118CBM6 2

Secondary structure

1 ..................... 635
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P45796-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F9DEC69967323316

FASTA63567,914
        10         20         30         40         50         60 
MIRKCLVLFL SFALLLSVFP MLNVDAANRP LAKIPGNSNP LMDHKLGADP YSLVYDGRVY 

        70         80         90        100        110        120 
IFMSSDTYVY NKDGSIKEND FSALDRIQVI SSTDMVNWTD HGTIPVAGAN NKNSGRGIAK 

       130        140        150        160        170        180 
WASNSWAPAV AHKKINGRDK FFLYFANGGA GIGVLTADTP IGPWTDPLGK ALVTHSTPGM 

       190        200        210        220        230        240 
AGVTWLFDPA VLVDDDGTGY LYSGGGIPNE SDPASIANPK TARVIKLGAD MTSVIGSATT 

       250        260        270        280        290        300 
IDAPYLFEDS GIHKYNGKYY YSYCINFAGT HPQQYPAGEI GYMVSDNPMG PFTYKGHFLK 

       310        320        330        340        350        360 
NPYTFFGVGG NNHHAVFNFK NEWYVVYHAQ TVSKAQIGAG KGYRSPHINK LVHKEDGSIS 

       370        380        390        400        410        420 
EVQGNMTGIA QLSNMNPYTR VEAETIAWQA GVTTEPTQAS GGPISNLNVT NIHNGDWIAV 

       430        440        450        460        470        480 
GKADFGSAGA KTFKANVATN VGGNIEVRLD SETGPLVGSL KVPSTGGMQT WREVETTINN 

       490        500        510        520        530        540 
ATGVHNIYLV FTGSGSGNLL NLDAWQFTPN TGGNTITKVE AENMKIGGTY AGKISAPFDG 

       550        560        570        580        590        600 
VALYANADYV SYSQYFANST HNISVRGASS NAGTAKVDLV IGGVTVGSFN FTGKTPTVQT 

       610        620        630 
LSNITHATGD QEIKLALTSD DGTWDAYVDF IEFSL

« Hide

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References

[1]"Two beta-glycanase genes are clustered in Bacillus polymyxa: molecular cloning, expression, and sequence analysis of genes encoding a xylanase and an endo-beta-(1,3)-(1,4)-glucanase."
Gosalbes M.J., Perez-Gonzalez J.A., Gonzalez R., Navarro A.
J. Bacteriol. 173:7705-7710(1991) [PubMed: 1938968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 842 / DSM 36 / IFO 15309 / NCIB 8158 / NCTC 10343.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X57094 Genomic DNA. Translation: CAA40378.1.
PIRS19011.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UX7X-ray1.50A516-635[»]
1W0NX-ray0.80A505-635[»]
ModBaseSearch...

Family and domain databases

InterProIPR005084. CBM_6.
IPR006584. Cellulose_bd_IV.
IPR006710. Glyco_hydro_43.
[Graphical view]
PANTHERPTHR22925. Glyco_hydro_43. 1 hit.
PfamPF03422. CBM_6. 2 hits.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SMARTSM00606. CBD_IV. 1 hit.
[Graphical view]
PROSITEPS51175. CBM6. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYND_PAEPO
AccessionPrimary (citable) accession number: P45796
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 25, 2008
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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