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Q53317 (XYND_RUMFL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Xylanase/beta-glucanase

Including the following 2 domains:

  1. Endo-1,4-beta-xylanase
    Short name=Xylanase
    EC=3.2.1.8
  2. Endo-beta-1,3-1,4 glucanase
    EC=3.2.1.73
    Alternative name(s):
    1,3-1,4-beta-D-glucan 4-glucanohydrolase
    Lichenase
Gene names
Name:xynD
OrganismRuminococcus flavefaciens
Taxonomic identifier1265 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminococcus

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Contains two catalytic domains with xylanase and endo-beta-1,3-1,4 glucanase activities.

Catalytic activity

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

Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

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 16 family.

Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainSignal
   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

licheninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 802771Xylanase/beta-glucanase
PRO_0000008009

Regions

Domain258 – 404147CBM-cenC
Region32 – 244213A (xylanase)
Region245 – 523279B
Region524 – 55532Linker
Region556 – 802247C (beta-glucanase)
Compositional bias524 – 5296Poly-Thr
Compositional bias532 – 54312Poly-Thr
Compositional bias546 – 5538Poly-Thr

Sites

Active site1241Nucleophile By similarity
Active site2261Proton donor By similarity
Active site6841Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q53317 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2880A689647284AF

FASTA80289,091
        10         20         30         40         50         60 
MKKSIFKRYA AAVGLMASVL MFTAVPTTSN AADDQKTGKV GGFDWEMWNQ NYTGTVSMNP 

        70         80         90        100        110        120 
GAGSFTCSWS GIENFLARMG KNYDDQKKNY KAFGDIVLTY DVEYTPRGNS YMCIYGWTRN 

       130        140        150        160        170        180 
PLMEYYIVEG WGDWEPPGND GVDNFGTTTI DGKTYKIRKS MRYNQPSIEG TKTFPQYWSV 

       190        200        210        220        230        240 
RTTSGSRNNT TNYMKDQVSV TKHFDAWSKA GLDMSGTLYE VSLNIEGYRS NGSANVKSIS 

       250        260        270        280        290        300 
FDGGIDIPDP EPIKPDENGY YLKENFESGE GNWSGRGSAK VKSSSGYDGT KGIFVSGRED 

       310        320        330        340        350        360 
TWNGASINLD ELTFKAGETY SLGTAVMQDF ESSVDFKLTL QYTDADGKEN YDEVKTVTAA 

       370        380        390        400        410        420 
KGQWVDLSNS SYTIPSGATG LVLYVEVPES KTDFYMDGAY AGVKGTKPLI SISSQSVDPP 

       430        440        450        460        470        480 
VTEPTNPTNP TGPSVTKWGD ANCDGGVDLS DAIFIMQFLA NPNKYGLTGT ETNHMTNQGK 

       490        500        510        520        530        540 
VNGDVCEHGS GLTEDDAVSI QKYLIRAISE LPESYLEGHD PSKTTTTTTR ITTTTTTTTT 

       550        560        570        580        590        600 
TTTSKTTTTT TTTSPAMHGG YRDLGTPMNT SATMISDFRT GKAGDFFASD GWTNGKPFDC 

       610        620        630        640        650        660 
WWYKRNAVIN DGCLQLSIDQ KWTNDKNPDW DPRYSGGEFR TNNFYHYGYY ECSMQAMKND 

       670        680        690        700        710        720 
GVVSSFFTYT GPSDDNPWDE IDIEILGKNT TQVQFNYYTN GQGKHEKLYD LGFDSSEAYH 

       730        740        750        760        770        780 
TYGFDWQPNY IAWYVDGREV YRATQDIPKT PGKIMMNAWP GLTVDDWLKA FNGRTPLTAH 

       790        800 
YQWVTYNKNG VQHSSQGQNP WG 

« Hide

References

[1]"A bifunctional enzyme, with separate xylanase and beta(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens."
Flint H.J., Martin J., McPherson C.A., Daniel A.S., Zhang J.-X.
J. Bacteriol. 175:2943-2951(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 17.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S61204 Genomic DNA. Translation: AAB26620.1.

3D structure databases

ProteinModelPortalQ53317.
SMRQ53317. Positions 575-790.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM22. Carbohydrate-Binding Module Family 22.
GH11. Glycoside Hydrolase Family 11.
GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
2.60.120.180. 1 hit.
2.60.120.200. 1 hit.
2.60.120.260. 1 hit.
InterProIPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR003305. CenC_carb-bd.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR008979. Galactose-bd-like.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamPF02018. CBM_4_9. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSPR00737. GLHYDRLASE16.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF63446. SSF63446. 1 hit.
PROSITEPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYND_RUMFL
AccessionPrimary (citable) accession number: Q53317
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 13, 2013
This is version 79 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