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P29126 (XYNA_RUMFL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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:
Bifunctional endo-1,4-beta-xylanase XylA

EC=3.2.1.8
Gene names
Name:xynA
OrganismRuminococcus flavefaciens
Taxonomic identifier1265 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminococcus

Protein attributes

Sequence length954 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Xylanase domain 1 releases more xylo-oligosaccharides and domain 2 more xylose.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

In the N-terminal section; belongs to the glycosyl hydrolase 11 (cellulase G) family.

In the C-terminal section; belongs to the glycosyl hydrolase 10 (cellulase F) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionendo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727Or 28, or 29 Potential
Chain28 – 954927Bifunctional endo-1,4-beta-xylanase XylA
PRO_0000008015

Regions

Region28 – 244217Xylanase domain 1
Region623 – 954332Xylanase domain 2
Compositional bias245 – 622378Asn/Gln/Trp-rich (linker)

Sites

Active site1221Nucleophile By similarity
Active site2231Proton donor By similarity
Active site7741Proton donor By similarity
Active site8841Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P29126 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 1033567D4B526EBD

FASTA954111,362
        10         20         30         40         50         60 
MKLSKIKKVL SGTVSALMIA SAAPVVASAA DQQTRGNVGG YDYEMWNQNG QGQASMNPGA 

        70         80         90        100        110        120 
GSFTCSWSNI ENFLARMGKN YDSQKKNYKA FGNIVLTYDV EYTPRGNSYM CVYGWTRNPL 

       130        140        150        160        170        180 
MEYYIVEGWG DWRPPGNDGE VKGTVSANGN TYDIRKTMRY NQPSLDGTAT FPQYWSVRQT 

       190        200        210        220        230        240 
SGSANNQTNY MKGTIDVTKH FDAWSAAGLD MSGTLYEVSL NIEGYRSNGS ANVKSVSVTQ 

       250        260        270        280        290        300 
GGSSDNGGQQ QNNDWNQQNN NQQQNNDWNN WGQQNNDWNQ WNNQGQQNND WNNWGQQNND 

       310        320        330        340        350        360 
WNQWNNQGQQ QNNDWNNWGQ QNNDWNQWNN QGQQQNNDWN NWGQQNNDWN QWNNQGQQQN 

       370        380        390        400        410        420 
NDWNNWGQQN NDWNQWNNQN NNQQNAWNGW DNNNNWNQNN QQQNNWDWNN QNNWNNNQQQ 

       430        440        450        460        470        480 
NNDWNQWNNQ NNWNNNQQQN NDWNQWNNQG QQNNDWNQWN NQNNWNQNNN QQNAWNGWDN 

       490        500        510        520        530        540 
NNNWNQWDQN NQWNNQQQNN TWDWNNQNNW NNNQQNNDWN QWNNQGQQQN NDWNQWNNQN 

       550        560        570        580        590        600 
NNQNNGWDWN NQNNWNQNNN QQNAWNGWDN NNNWNQWGGQ NNDWNNQQQN NDWNQWNNQG 

       610        620        630        640        650        660 
QQQNNDWNNQ NNWNQGQQNN NNSAGSSDSL KGAFSKYFKI GTSVSPHELN SGADFLKKHY 

       670        680        690        700        710        720 
NSITPENELK PESILDQGAC QQKGNNVNTQ ISLSRAAQTL KFCEQNGIAL RGHTFVWYSQ 

       730        740        750        760        770        780 
TPDWFFRENF SQNGAYVSKD IMNQRLESMI KNTFAALKSQ YPNLDVYSYD VCNELFLNNG 

       790        800        810        820        830        840 
GGMRGADNSN WVKIYGDDSF VINAFKYARQ YAPAGCKLYL NDYNEYIPAK TNDIYNMAMK 

       850        860        870        880        890        900 
LKQLGYIDGI GMQSHLATNY PDANTYETAL KKFLSTGLEV QITELDITCT NSAEQADLYE 

       910        920        930        940        950 
KIFKLAMQNS AQIPAVTIWG TQDTVSWRSS QNPLLFSAGY QPKPAYDRVM ALAK 

« Hide

References

[1]"A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence."
Zhang J.-X., Flint H.J.
Mol. Microbiol. 6:1013-1023(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 17.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11127 Genomic DNA. Translation: CAA77476.1.
PIRS20907.

3D structure databases

ProteinModelPortalP29126.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.
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.
3.20.20.80. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001000. Glyco_hydro_10.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00331. Glyco_hydro_10. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_RUMFL
AccessionPrimary (citable) accession number: P29126
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 13, 2013
This is version 76 of the entry and version 1 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