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P45796 (XYND_PAEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. 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:
Arabinoxylan arabinofuranohydrolase

Short name=AXH
EC=3.2.1.55
Alternative name(s):
AXH-m2,3
Short name=AXH-m23
Alpha-L-arabinofuranosidase
Short name=AF
Gene names
Name:xynD
OrganismPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifier1406 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length635 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves arabinose units from O-2- or O-3-monosubstituted xylose residues, thereby assisting in arabinoxylan (AX) and short-chain arabinoxylo-oligosaccharide (AXOS) degradation By similarity. Preferres wheat flour xylan over oat spelt xylan as substrate. Does not display endoxylanase activity. Ref.2

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Enzyme regulation

Activated by calcium and magnesium. Inhibited by copper. Ref.2

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Domain

The C-terminal CBM6 domain shows calcium-dependent xylo-oligosaccharide and xylan binding. It binds, next to the structural calcium ion, a second calcium ion that, in addition to its coordination sites on the protein, completes its heptacoordination through coordination to the bound xylose moiety.

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

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

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5. Ref.2

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 635609Arabinoxylan arabinofuranohydrolase
PRO_0000012202

Regions

Domain379 – 508130CBM6 1
Domain517 – 634118CBM6 2

Sites

Active site491Proton acceptor By similarity
Active site2481Proton donor By similarity
Metal binding3821Calcium 1; structural By similarity
Metal binding3841Calcium 1; structural By similarity
Metal binding4061Calcium 1; structural By similarity
Metal binding4071Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding5031Calcium 1; structural By similarity
Metal binding5031Calcium 1; via carbonyl oxygen; structural By similarity
Metal binding5201Calcium 2; structural
Metal binding5221Calcium 2; structural
Metal binding5391Calcium 2; via carbonyl oxygen; structural
Metal binding5441Calcium 3; via carbonyl oxygen; structural
Metal binding6201Calcium 3
Metal binding6241Calcium 3; via carbonyl oxygen; structural
Metal binding6251Calcium 3
Metal binding6291Calcium 2; structural
Metal binding6291Calcium 2; via carbonyl oxygen; structural
Binding site3111Substrate By similarity
Site1881Important for catalytic activity By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P45796 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343 / NRRL B-4317 / VKM B-514.
[2]"Purification and characterization of an arabinofuranosidase from Bacillus polymyxa expressed in Bacillus subtilis."
Morales P., Sendra J.M., Perez-Gonzalez J.A.
Appl. Microbiol. Biotechnol. 44:112-117(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-46, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
Strain: CECT 153 / NCTC 4747 / NRRL NRS-1237.
[3]"Ab initio structure determination and functional characterization of CBM36; a new family of calcium-dependent carbohydrate binding modules."
Jamal-Talabani S., Boraston A.B., Turkenburg J.P., Tarbouriech N., Ducros V.M.-A., Davies G.J.
Structure 12:1177-1187(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.8 ANGSTROMS) OF 505-635 IN COMPLEX WITH XYLOTRIOSE.
Strain: ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343 / NRRL B-4317 / VKM B-514.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57094 Genomic DNA. Translation: CAA40378.1.
PIRS19011.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UX7X-ray1.50A516-635[»]
1W0NX-ray0.80A505-635[»]
ProteinModelPortalP45796.
SMRP45796. Positions 516-635.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM36. Carbohydrate-Binding Module Family 36.
CBM6. Carbohydrate-Binding Module Family 6.
GH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.8. 7322.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
2.60.120.260. 2 hits.
InterProIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERPTHR22925. PTHR22925. 1 hit.
PfamPF03422. CBM_6. 2 hits.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SMARTSM00606. CBD_IV. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF75005. SSF75005. 1 hit.
PROSITEPS51175. CBM6. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP45796.

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: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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