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Q45071 (XYND_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
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
Ordered Locus Names:BSU18160
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length513 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. Is more active on wheat bran AXOS than on wheat water-extractable AX and rye water-extractable AX. Does not display endoxylanase, xylosidase or arabinanase activity. Ref.3

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.2.

Domain

The CBM6 domain lost its carbohydrate binding capacity.

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.6. Stable from pH 4.4 to 7.6. Ref.3

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Thermostable for 40 min from 4 to 45 degrees Celsius.

Mass spectrometry

Molecular mass is 52080 Da from positions 27 - 513. Determined by MALDI. Ref.3

Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
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-N-arabinofuranosidase activity

Inferred from electronic annotation. Source: 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 – 513487Arabinoxylan arabinofuranohydrolase
PRO_0000360828

Regions

Domain382 – 511130CBM6

Sites

Active site501Proton acceptor
Active site2511Proton donor
Metal binding3851Calcium; structural
Metal binding3871Calcium; structural
Metal binding4091Calcium; structural
Metal binding4101Calcium; via carbonyl oxygen; structural
Metal binding5061Calcium; structural
Metal binding5061Calcium; via carbonyl oxygen; structural
Binding site3141Substrate
Site1891Important for catalytic activity

Secondary structure

1 ........................................................................... 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q45071 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 1EBC94AB6CE1490F

FASTA51354,498
        10         20         30         40         50         60 
MRKKCSVCLW ILVLLLSCLS GKSAYAATST TIAKHIGNSN PLIDHHLGAD PVALTYNGRV 

        70         80         90        100        110        120 
YIYMSSDDYE YNSNGTIKDN SFANLNRVFV ISSADMVNWT DHGAIPVAGA NGANGGRGIA 

       130        140        150        160        170        180 
KWAGASWAPS IAVKKINGKD KFFLYFANSG GGIGVLTADS PIGPWTDPIG KPLVTPSTPG 

       190        200        210        220        230        240 
MSGVVWLFDP AVFVDDDGTG YLYAGGGVPG VSNPTQGQWA NPKTARVIKL GPDMTSVVGS 

       250        260        270        280        290        300 
ASTIDAPFMF EDSGLHKYNG TYYYSYCINF GGTHPADKPP GEIGYMTSSS PMGPFTYRGH 

       310        320        330        340        350        360 
FLKNPGAFFG GGGNNHHAVF NFKNEWYVVY HAQTVSSALF GAGKGYRSPH INKLVHNADG 

       370        380        390        400        410        420 
SIQEVAANYA GVTQISNLNP YNRVEAETFA WNGRILTEKS TAPGGPVNNQ HVTSIQNGDW 

       430        440        450        460        470        480 
IAVGNADFGA GGARSFKANV ASTLGGKIEV RLDSADGKLV GTLNVPSTGG AQTWREIETA 

       490        500        510 
VSGATGVHKV FFVFTGTGTG NLFNFDYWQF TQR

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-37, SUBCELLULAR LOCATION.
Strain: 168.
[3]"Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase."
Bourgois T.M., Van Craeyveld V., Van Campenhout S., Courtin C.M., Delcour J.A., Robben J., Volckaert G.
Appl. Microbiol. Biotechnol. 75:1309-1317(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[4]"Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family."
Vandermarliere E., Bourgois T.M., Winn M.D., van Campenhout S., Volckaert G., Delcour J.A., Strelkov S.V., Rabijns A., Courtin C.M.
Biochem. J. 418:39-47(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 27-513 IN COMPLEXES WITH XYLOTRIOSE; XYLOTETRAOSE; ARABINOXYLO-OLIGOSACCHARIDES AND CELLOTETRAOSE.
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13699.1.
PIRH69735.
RefSeqNP_389698.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3C7EX-ray2.00A27-513[»]
3C7FX-ray1.55A27-513[»]
3C7GX-ray2.02A27-513[»]
3C7HX-ray2.00A27-513[»]
3C7OX-ray1.80A27-513[»]
ProteinModelPortalQ45071.
SMRQ45071. Positions 27-513.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU18160.

Protein family/group databases

CAZyCBM6. Carbohydrate-Binding Module Family 6.
GH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbQ45071.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13699; CAB13699; BSU18160.
GeneID936433.
KEGGbsu:BSU18160.
PATRIC18975467. VBIBacSub10457_1925.

Organism-specific databases

GenoListBSU18160. [Micado]

Phylogenomic databases

eggNOGCOG5498.
HOGENOMHOG000292007.
KOK15921.
OMASPHINKL.
ProtClustDBCLSK865478.

Enzyme and pathway databases

BioCycBSUB:BSU18160-MONOMER.
BRENDA3.2.1.55. 700.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
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. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SMARTSM00606. CBD_IV. 1 hit.
[Graphical view]
SUPFAMSSF49785. Gal_bind_like. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITEPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ45071.

Entry information

Entry nameXYND_BACSU
AccessionPrimary (citable) accession number: Q45071
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents