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P07528 (XYNA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. 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:
Endo-1,4-beta-xylanase A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xynA
Ordered Locus Names:BH2120
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Biophysicochemical properties

pH dependence:

Active over a very broad pH range.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
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_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 – 2828 Ref.1
Chain29 – 396368Endo-1,4-beta-xylanase A
PRO_0000007967

Sites

Active site1951Proton donor By similarity
Active site3011Nucleophile By similarity

Secondary structure

.................................................................. 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07528 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 29C1F46BE00E180C

FASTA39645,294
        10         20         30         40         50         60 
MITLFRKPFV AGLAISLLVG GGIGNVAAAQ GGPPKSGVFG ENEKRNDQPF AWQVASLSER 

        70         80         90        100        110        120 
YQEQFDIGAA VEPYQLEGRQ AQILKHHYNS LVAENAMKPE SLQPREGEWN WEGADKIVEF 

       130        140        150        160        170        180 
ARKHNMELRF HTLVWHSQVP EWFFIDEDGN RMVDETDPDK REANKQLLLE RMENHIKTVV 

       190        200        210        220        230        240 
ERYKDDVTSW DVVNEVIDDG GGLRESEWYQ ITGTDYIKVA FETARKYGGE EAKLYINDYN 

       250        260        270        280        290        300 
TEVPSKRDDL YNLVKDLLEQ GVPIDGVGHQ SHIQIGWPSI EDTRASFEKF TSLGLDNQVT 

       310        320        330        340        350        360 
ELDMSLYGWP PTGAYTSYDD IPAELLQAQA DRYDQLFELY EELAADISSV TFWGIADNHT 

       370        380        390 
WLDGRAREYN NGVGIDAPFV FDHNYRVKPA YWRIID 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the xylanase A gene of alkalophilic Bacillus sp. strain C-125."
Hamamoto T., Honda H., Kudo T., Horikoshi K.
Agric. Biol. Chem. 51:953-955(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS.
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
[2]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00087 Genomic DNA. Translation: BAA00055.1.
BA000004 Genomic DNA. Translation: BAB05839.1.
PIRH83914.
JD0003.
RefSeqNP_242986.1. NC_002570.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UWFX-ray2.10A48-396[»]
ProteinModelPortalP07528.
SMRP07528. Positions 47-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH2120.

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB05839; BAB05839; BAB05839.
GeneID891394.
KEGGbha:BH2120.
PATRIC18941396. VBIBacHal18977_2211.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3693.
HOGENOMHOG000019847.
KOK01181.
OMAGAAVEPY.
OrthoDBEOG6B363F.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-2204-MONOMER.
UniPathwayUPA00114.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07528.

Entry information

Entry nameXYNA_BACHD
AccessionPrimary (citable) accession number: P07528
Secondary accession number(s): Q9JPV5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 14, 2014
This is version 105 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