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Reviewed, UniProtKB/Swiss-Prot P26514 (XYNA_STRLI)

Last modified June 16, 2009. Version 80. 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 A
      Short name=Xylanase A
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
Gene names
Name: xlnA
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

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Protein attributes

Sequence length477 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

Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.

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.

Contains 1 ricin B-type lectin domain.

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Ontologies

Keywords
   Biological processXylan degradation
   Cellular componentSecreted
   DomainSignal
   LigandLectin
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
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

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Ref.1
Chain42 – 477436Endo-1,4-beta-xylanase A
PRO_0000007979

Regions

Domain361 – 477117Ricin B-type lectin

Sites

Active site1691Proton donor
Active site2771Nucleophile

Amino acid modifications

Disulfide bond364 ↔ 383 Ref.4
Disulfide bond406 ↔ 423 Ref.4
Disulfide bond447 ↔ 466 Ref.4

Secondary structure

1 .......................................................................................... 477
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P26514-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: E14A7FE37BDC68CC

FASTA47751,163
        10         20         30         40         50         60 
MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA AQSGRYFGTA 

        70         80         90        100        110        120 
IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF NFSSADRVYN WAVQNGKQVR 

       130        140        150        160        170        180 
GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI NGVMAHYKGK IVQWDVVNEA FADGSSGARR 

       190        200        210        220        230        240 
DSNLQRSGND WIEVAFRTAR AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI 

       250        260        270        280        290        300 
DCVGFQSHFN SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR 

       310        320        330        340        350        360 
CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP ADGGQIKGVG 

       370        380        390        400        410        420 
SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR VYGDKCLDAA GTSNGSKVQI 

       430        440        450        460        470 
YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA VGNGTANGTL IQLYTCSNGS NQRWTRT

« Hide

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References

[1]"Sequences of three genes specifying xylanases in Streptomyces lividans."
Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.
Gene 107:75-82(1991) [PubMed: 1743521] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 42-92.
Strain: 66 / 1326.
[2]Shareck F.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 20 AND 140-141.
[3]"Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases."
Derewenda U., Swenson L., Green R., Wei Y.Y., Morosoli R., Shareck F., Kluepfel D., Derewenda Z.S.
J. Biol. Chem. 269:20811-20814(1994) [PubMed: 8063693] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 42-340.
[4]"High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding."
Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R.
Biochemistry 41:4246-4254(2002) [PubMed: 11914070] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 348-477, DISULFIDE BONDS.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M64551 Genomic DNA. Translation: AAC26525.1.
PIRJS0589.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E0VX-ray1.70A42-343[»]
1E0WX-ray1.20A42-343[»]
1E0XX-ray1.65A/B42-350[»]
1KNLX-ray1.20A348-477[»]
1KNMX-ray1.20A348-477[»]
1MC9X-ray1.70A348-477[»]
1OD8X-ray1.05A42-354[»]
1V0KX-ray1.03A42-354[»]
1V0LX-ray0.98A42-354[»]
1V0MX-ray1.07A42-354[»]
1V0NX-ray1.10A42-354[»]
1XASX-ray2.60A42-340[»]
SMRP26514. Positions 42-477.
ModBaseSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA3.2.1.8. 15238.

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameXYNA_STRLI
AccessionPrimary (citable) accession number: P26514
Secondary accession number(s): P96464
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: June 16, 2009
This is version 80 of the entry and version 2 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