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Reviewed, UniProtKB/Swiss-Prot P07528 (XYNA_BACHD)

Last modified June 16, 2009. Version 72. 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

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 [Complete proteome] [HAMAP]
Taxonomic identifier86665 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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 processXylan 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-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Chain29 – 396368Endo-1,4-beta-xylanase A
PRO_0000007967

Sites

Active site1951Proton donor By similarity
Active site3011Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P07528-1 [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 1-11.
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.
[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: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases

D00087 Genomic DNA. Translation: BAA00055.1.
BA000004 Genomic DNA. Translation: BAB05839.1.
PIRH83914.
JD0003.
RefSeqNP_242986.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2UWFX-ray2.10A47-396[»]
SMRP07528. Positions 48-396.
ModBaseSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Genome annotation databases

GeneID891394.
GenomeReviewsGene locus BH2120 in contig BA000004_GR.
KEGGbha:BH2120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP07528.
OMAP07528. GAAVEPY.

Enzyme and pathway databases

BioCycBHAL272558:BH2120-MON.
BRENDA3.2.1.8. 191865.

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 72 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)

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