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P83513 (XY11A_PSEXY) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 65. 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 xylanase/deacetylase

Including the following 2 domains:

  1. Endo-1,4-beta-xylanase 11A
    EC=3.2.1.8
    Alternative name(s):
    Xylanase XynT
    Xylanase xyn11A
  2. Acetylated xylan deacetylase
    EC=3.5.1.-
Gene names
Name:xyn11A
Synonyms:xynT
OrganismPseudobutyrivibrio xylanivorans
Taxonomic identifier185007 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesLachnospiraceaePseudobutyrivibrio

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is also probably able, via its C-terminal domain, to remove acetyl groups from acetylated xylan, and thus it is probably capable of hydrolyzing acetylated xylan. Ref.2

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.2

Pathway

Glycan degradation; xylan degradation.

Subcellular location

Secreted Ref.2.

Domain

Consists of three domains: two complementary catalytic domains and one substrate-binding module. Ref.1

Post-translational modification

In the later growth phases, seems to undergo a proteolytic cleavage into a 30 kDa protein possessing xylanolytic activity.

Biotechnological use

Could be used as a feed additive for animals in order to diminish health problems due to undigested plant fiber and enhance proliferation of beneficial microflora. Ref.2

Sequence similarities

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

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Contains 1 NodB homology domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.6. Active from pH 4.0 to 8.0.

Temperature dependence:

Optimum temperature is 38 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Ref.2
Chain15 – 602588Bifunctional xylanase/deacetylase
PRO_0000184070

Regions

Domain249 – 366118CBM6
Domain402 – 578177NodB homology
Region24 – 210187Endoglucanase

Sites

Active site1081Nucleophile By similarity
Active site1981Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P83513 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: F3D7AE32EF7A3CF0

FASTA60265,923
        10         20         30         40         50         60 
MSATLLVPSM TVKAADTIYN NKTGNQDGYD YELWKDTGNT SMTLNAGGTF DCSWSNINNA 

        70         80         90        100        110        120 
LFRKGKKFDS TQTYQQIGNI TFDYGCDYRP NGNSYLCVYG WTVDPLVEYY IVDSWGTWRP 

       130        140        150        160        170        180 
PGGTPKGQIQ VDGGTYDVYE TTRYNAPSIQ GDTTFKQYFS VRTSKRTSGT ISVSEHFKAW 

       190        200        210        220        230        240 
ERMGMRCGNF MKPALNIEGY QSSGSASVYK NNMTIGGSSS SSGNQGGNQG GNTGNENAGN 

       250        260        270        280        290        300 
NLVTVADADK IQCETMTKSG QYTGNISSPF NGVALYANND AVKYTQYFAS GTHDFTLRGC 

       310        320        330        340        350        360 
SNNNKMARVD LKIGGQNKGT FYYGDSYPAE YTIKNVSHGT GNQTIELVVT ADDGQWDAYL 

       370        380        390        400        410        420 
DYFNNSVEPG CSLVPGAVVV LVALGSSSNT GNNSGTNTQN QKLIALTFDD GPSSTTSQVL 

       430        440        450        460        470        480 
DMLEKYNVKA TFFLIGQNVN SNTASIVQRQ VKMGCELACH SYTHEDMTKM NASQIRNQID 

       490        500        510        520        530        540 
WTASAIKNTA GVDVKFFRPP YISVNNTMYQ NIDLPFIQGS MHNDWESSTS ASQRVNSVLS 

       550        560        570        580        590        600 
SAKDGDIILL HDFQGNSQTV SALPQIIEGL KNQGYTFVTV SELFEMKGVN PNVEYKIWSN 


VK 

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References

[1]"Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorcans Mz5T."
Cepeljnik T., Rincon M.T., Flint H.J., Marinsek-Logar R.
Folia Microbiol. (Praha) 51:263-267(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN ORGANIZATION.
Strain: Mz5T.
[2]"Isolation and characterization of the Pseudobutyrivibrio xylanivorans Mz5T xylanase XynT -- the first family 11 endoxylanase from rumen Butyrivibrio-related bacteria."
Cepeljnik T., Krizaj I., Marinsek-Logar R.
Enzyme Microb. Technol. 34:219-227(2004)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-193, PROTEIN SEQUENCE OF 15-39, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, BIOTECHNOLOGY.
Strain: Mz5T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ543424 Genomic DNA. Translation: CAD65888.2.

3D structure databases

ProteinModelPortalP83513.
SMRP83513. Positions 18-363.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM36. Carbohydrate-Binding Module Family 36.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17647.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
3.20.20.370. 1 hit.
InterProIPR005084. CMB_fam6.
IPR008985. ConA-like_lec_gl_sf.
IPR008979. Galactose-bd-like.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamPF03422. CBM_6. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEPS51175. CBM6. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXY11A_PSEXY
AccessionPrimary (citable) accession number: P83513
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: May 30, 2006
Last modified: March 19, 2014
This is version 65 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