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Q8GJ44 (XYNA1_CLOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 67. 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

EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Xylanase 11A
Short name=Xyn11A
Gene names
Name:xynA
OrganismClostridium stercorarium
Taxonomic identifier1510 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeunclassified Ruminococcaceae

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoxylanase that degrades arabinoxylan and glucuronoxylan to xylobiose and xylotriose (in vitro). Ref.1 Ref.2

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.1.

Induction

Up-regulated by growth on xylan. Ref.1

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.

Sequence similarities

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

Contains 3 CBM6 (carbohydrate binding type-6) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5-7.0. Ref.1

Temperature dependence:

Optimum temperature is 75 degrees Celsius. Thermostable.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
Xylan degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

xylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 651621Endo-1,4-beta-xylanase A
PRO_0000236809

Regions

Domain250 – 370121CBM6 1
Repeat278 – 339621
Domain387 – 507121CBM6 2
Repeat415 – 476622
Domain527 – 647121CBM6 3
Repeat555 – 616623
Region278 – 6163393 X 61 AA approximate repeats

Sites

Active site1241Nucleophile By similarity
Active site2141Proton donor By similarity
Metal binding2531Calcium 1
Metal binding2551Calcium 1
Metal binding2751Calcium 1; via carbonyl oxygen
Metal binding3651Calcium 1
Metal binding5301Calcium 2
Metal binding5321Calcium 2
Metal binding5521Calcium 2; via carbonyl oxygen
Metal binding6421Calcium 2
Binding site2701Substrate 1; via carbonyl oxygen
Binding site2791Substrate 1; via amide nitrogen
Binding site3361Substrate 1
Binding site3631Substrate 1
Binding site5561Substrate 2; via amide nitrogen
Binding site6131Substrate 2
Binding site6401Substrate 2

Experimental info

Sequence conflict649 – 6513SGT → FRNLRV in CAD48307. Ref.1

Secondary structure

........................................... 651
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8GJ44 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 52E501A16F9D1423

FASTA65170,151
        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 PKGTITVDGG TYEIYETTRV NQPSIDGTAT FQQYWSVRTS 

       190        200        210        220        230        240 
KRTSGTISVT EHFKQWERMG MRMGKMYEVA LTVEGYQSSG YANVYKNEIR IGANPTPAPS 

       250        260        270        280        290        300 
QSPIRRDAFS IIEAEEYNST NSSTLQVIGT PNNGRGIGYI ENGNTVTYSN IDFGSGATGF 

       310        320        330        340        350        360 
SATVATEVNT SIQIRSDSPT GTLLGTLYVS STGSWNTYQT VSTNISKITG VHDIVLVFSG 

       370        380        390        400        410        420 
PVNVDNFIFS RSSPVPAPGD NTRDAYSIIQ AEDYDSSYGP NLQIFSLPGG GSAIGYIENG 

       430        440        450        460        470        480 
YSTTYNNVNF ANGLSSITAR VATQISTSIQ VRAGGATGTL LGTIYVPSTN SWDSYQNVTA 

       490        500        510        520        530        540 
NLSNITGVHD ITLVFSGPVN VDYFVFTPAN VNSGPTSPVG GTRSAFSNIQ AEDYDSSYGP 

       550        560        570        580        590        600 
NLQIFSLPGG GSAIGYIENG YSTTYKNIDF GDGATSVTAR VATQNATTIQ VRLGSPSGTL 

       610        620        630        640        650 
LGTIYVGSTG SFDTYRDVSA TISNTAGVKD IVLVFSGPVN VDWFVFSKSG T 

« Hide

References

[1]"Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes."
Adelsberger H., Hertel C., Glawischnig E., Zverlov V.V., Schwarz W.H.
Microbiology 150:2257-2266(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: NCIB 11745.
[2]"Co-operative binding of triplicate carbohydrate-binding modules from a thermophilic xylanase."
Boraston A.B., McLean B.W., Chen G., Li A., Warren R.A.J., Kilburn D.G.
Mol. Microbiol. 43:187-194(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-651, FUNCTION.
Strain: NCIB 11745.
[3]"Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and 'galactose-binding' domains."
Boraston A.B., Notenboom V., Warren R.A.J., Kilburn D.G., Rose D.R., Davies G.
J. Mol. Biol. 327:659-669(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 507-651 IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS.
[4]"Binding sub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration."
Van Bueren A.L., Boraston A.B.
Submitted (JUN-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 235-373 IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ508403 Genomic DNA. Translation: CAD48307.1.
AF417638 Genomic DNA. Translation: AAL14106.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NAEX-ray2.05A507-651[»]
1O8PX-ray2.00A507-651[»]
1O8SX-ray1.15A507-651[»]
1OD3X-ray1.00A507-651[»]
1UY1X-ray1.80A235-373[»]
1UY2X-ray1.70A235-373[»]
1UY3X-ray1.89A235-373[»]
1UY4X-ray1.69A235-373[»]
ProteinModelPortalQ8GJ44.
SMRQ8GJ44. Positions 33-373, 378-507, 518-648.
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

BRENDA3.2.1.8. 1520.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
2.60.120.260. 3 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. 3 hits.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00606. CBD_IV. 3 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 3 hits.
SSF49899. SSF49899. 1 hit.
PROSITEPS51175. CBM6. 3 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8GJ44.

Entry information

Entry nameXYNA1_CLOSR
AccessionPrimary (citable) accession number: Q8GJ44
Secondary accession number(s): Q93AQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: October 16, 2013
This is version 67 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

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