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P33558 (XYNA2_CLOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 92. 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 A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xynA
OrganismClostridium stercorarium
Taxonomic identifier1510 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeunclassified Ruminococcaceae

Protein attributes

Sequence length512 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.

Domain

XynA is a modular enzyme. The number of CBM6 (carbohydrate binding type-6) domains varies between strains. The polymeric substrate can interact with several of these CBM6 domains By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 11 (cellulase G) family.

Contains 2 CBM6 (carbohydrate binding type-6) domains.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 70 degrees Celsius. Thermostable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 512482Endo-1,4-beta-xylanase A
PRO_0000008002

Regions

Domain251 – 371121CBM6 1
Repeat279 – 340621
Domain388 – 508121CBM6 2
Repeat416 – 477622
Region279 – 4771992 X 61 AA approximate repeats
Compositional bias236 – 2449Pro-rich

Sites

Active site1241Nucleophile By similarity
Active site2151Proton donor By similarity
Metal binding2541Calcium 1 By similarity
Metal binding2561Calcium 1 By similarity
Metal binding2761Calcium 1; via carbonyl oxygen By similarity
Metal binding3661Calcium 1 By similarity
Metal binding3911Calcium 2 By similarity
Metal binding3931Calcium 2 By similarity
Metal binding4131Calcium 2; via carbonyl oxygen By similarity
Metal binding5031Calcium 2 By similarity
Binding site2711Substrate 1; via carbonyl oxygen By similarity
Binding site2801Substrate 1; via amide nitrogen By similarity
Binding site3371Substrate 1 By similarity
Binding site3641Substrate 1 By similarity
Binding site4171Substrate 2; via amide nitrogen By similarity
Binding site4741Substrate 2 By similarity
Binding site5011Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P33558 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 1E133CBF4C139305

FASTA51255,843
        10         20         30         40         50         60 
MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW KDYGNTIMEL 

        70         80         90        100        110        120 
NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY GCDYNPNGNS YLCVYGWTRN 

       130        140        150        160        170        180 
PLVEYYIVES WGSWRPPGAT PKGTITQWMA GTYEIYETTR VNQPSIDGTA TFQQYWSVRT 

       190        200        210        220        230        240 
SKRTSGTISV TEHFKQWERM GMRMGKMYEV ALTVEGYQSS GYANVYKNEI RIGANPTPAP 

       250        260        270        280        290        300 
SQSPIRRDAF SIIEAEEYNS TNSSTLQVIG TPNNGRGIGY IENGNTVTYS NIDFGSGATG 

       310        320        330        340        350        360 
FSATVATEVN TSIQIRSDSP TGTLLGTLYV SSTGSWNTYQ TVSTNISKIT GVHDIVLVFS 

       370        380        390        400        410        420 
GPVNVDNFIF SRSSPVPAPG DNTRDAYSII QAEDYDSSYG PNLQIFSLPG GGSAIGYIEN 

       430        440        450        460        470        480 
GYSTTYKNID FGDGATSVTA RVATQNATTI QVRLGSPSGT LLGTIYVGST GSFDTYRDVS 

       490        500        510 
ATISNTAGVK DIVLVFSGPV NVDWFVFSKS GT 

« Hide

References

[1]"Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xylanase A: identification of catalytic and cellulose binding domains."
Sakka K., Kojima Y., Kondo T., Karita S., Ohmiya K., Shimada K.
Biosci. Biotechnol. Biochem. 57:273-277(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-40.
Strain: F-9.
[2]Sakka K.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13325 Genomic DNA. Translation: BAA02584.1.

3D structure databases

ProteinModelPortalP33558.
SMRP33558. Positions 33-374, 379-509.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM6. Carbohydrate-Binding Module Family 6.
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.
2.60.120.260. 2 hits.
InterProIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR008985. ConA-like_lec_gl_sf.
IPR008979. Galactose-bd-like.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamPF03422. CBM_6. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00606. CBD_IV. 2 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEPS51175. CBM6. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA2_CLOSR
AccessionPrimary (citable) accession number: P33558
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: October 16, 2013
This is version 92 of the entry and version 2 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