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P26515 (XYNB_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 B

Short name=Xylanase B
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene names
Name:xlnB
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 11 (cellulase G) family.

Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect 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

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Ref.1
Chain42 – 335294Endo-1,4-beta-xylanase B
PRO_0000008010

Regions

Domain250 – 33586CBM2
Region42 – 230189Catalytic
Region231 – 24919Linker ("hinge") (Gly-rich box)

Sites

Active site1281Nucleophile By similarity
Active site2181Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P26515 [UniParc].

Last modified August 14, 2001. Version 3.
Checksum: 513B1458BF8FF0CF

FASTA33535,575
        10         20         30         40         50         60 
MNLLVQPRRR RRGPVTLLVR SAWAVALAAL AALMLPGTAQ ADTVVTTNQE GTNNGYYYSF 

        70         80         90        100        110        120 
WTDSQGTVSM NMGSGGQYST SWRNTGNFVA GKGWANGGRR TVQYSGSFNP SGNAYLALYG 

       130        140        150        160        170        180 
WTSNPLVEYY IVDNWGTYRP TGEYKGTVTS DGGTYDIYKT TRVNKPSVEG TRTFDQYWSV 

       190        200        210        220        230        240 
RQSKRTGGTI TTGNHFDAWA RAGMPLGNFS YYMIMATEGY QSSGSSSINV GGTGGGDSGG 

       250        260        270        280        290        300 
GDNGGGGGGC TATVSAGQKW GDRYNLDVSV SGASDWTVTM NVPSPAKVLS NWNVNASYPS 

       310        320        330 
AQTLTARLNG SGNNWGATIQ ANANWTWPSV SCSAG 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 42-72.
Strain: 66 / 1326.
[2]"Analysis of DNA flanking the xlnB locus of Streptomyces lividans reveals genes encoding acetyl xylan esterase and the RNA component of ribonuclease P."
Shareck F., Biely P., Morosoli R., Kluepfel D.
Gene 153:105-109(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 29-32 AND 252-307.
Strain: 66 / 1326.
[3]Shareck F.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 225.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64552 Genomic DNA. Translation: AAC06114.2.
PIRJS0590.

3D structure databases

ProteinModelPortalP26515.
SMRP26515. Positions 45-228.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
2.60.40.290. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMSSF49384. SSF49384. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEPS51173. CBM2. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNB_STRLI
AccessionPrimary (citable) accession number: P26515
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 14, 2001
Last modified: November 13, 2013
This is version 81 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries