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P51584 (XYNY_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. 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 Y

Short name=Xylanase Y
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase Y
Short name=XylY
Gene names
Name:xynY
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1077 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.

Domain

A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.8.

Temperature dependence:

Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcellulosome

Inferred from direct assay Ref.1. Source: MENGO

   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 – 2626 Potential
Chain27 – 10771051Endo-1,4-beta-xylanase Y
PRO_0000007972

Regions

Domain33 – 180148CBM-cenC 1
Domain565 – 714150CBM-cenC 2
Repeat734 – 757241
Repeat768 – 791242
Region255 – 512258Catalytic Potential
Region734 – 791582 X 24 AA approximate repeats
Compositional bias552 – 5576Poly-Gly

Sites

Active site3371Proton donor By similarity
Active site4601Nucleophile By similarity

Secondary structure

.................................................................................................................................................................................... 1077
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51584 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BFC8D2D22C5726A0

FASTA1,077119,673
        10         20         30         40         50         60 
MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN LGVDTYLTAV 

        70         80         90        100        110        120 
ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS VFVKHNGTGT ETFKLSVSYL 

       130        140        150        160        170        180 
DSETEEENKE VIATKDVVAG EWTEISAKYK APKTAVNITL SITTDSTVDF IFDDVTITRK 

       190        200        210        220        230        240 
GMAEANTVYA ANAVLKDMYA NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA 

       250        260        270        280        290        300 
TLVQSGSTNT NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV 

       310        320        330        340        350        360 
SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG GAREPGYGNG 

       370        380        390        400        410        420 
RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW DHKRDCIASI CANLYNKGLL 

       430        440        450        460        470        480 
DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI NIGCDVQITE LDISTENGKF SLQQQADKYK 

       490        500        510        520        530        540 
AVFQAAVDIN RTSSKGKVTA VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP 

       550        560        570        580        590        600 
QSEWGDGNNP AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE 

       610        620        630        640        650        660 
SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL QYVDGSGTQR 

       670        680        690        700        710        720 
YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD TINFYIDEAI GAVAGTVIEG 

       730        740        750        760        770        780 
PAPQPTQPPV LLGDVNGDGT INSTDLTMLK RSVLRAITLT DDAKARADVD KNGSINSTDV 

       790        800        810        820        830        840 
LLLSRYLLRV IDKFPVAENP SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT 

       850        860        870        880        890        900 
KSLNVYLPYG YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT 

       910        920        930        940        950        960 
PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF GGFSMGGLTT 

       970        980        990       1000       1010       1020 
WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR SGLSKREYFV FAATGSDHIA 

      1030       1040       1050       1060       1070 
YANMNPQIEA MKALPHFDYT SDFSKGNFYF LVAPGATHWW GYVRHYIYDA LPYFFHE 

« Hide

References

[1]"Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria."
Fontes C.M.G.A., Hazelwood G.P., Morag E., Hall J., Hirst B.H., Gilbert H.J.
Biochem. J. 307:151-158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83269 Genomic DNA. Translation: CAA58242.1.
PIRS54975.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYOX-ray2.10A/B558-718[»]
1GKKX-ray1.60A/B792-1077[»]
1GKLX-ray1.40A/B792-1077[»]
1H6XX-ray2.23A560-720[»]
1H6YX-ray2.12A/B560-720[»]
1OHZX-ray2.20B733-791[»]
1WB4X-ray1.40A/B792-1077[»]
1WB5X-ray1.40A/B792-1077[»]
1WB6X-ray1.40A/B792-1077[»]
2CCLX-ray2.03B/D730-791[»]
2W5FX-ray1.90A/B32-551[»]
2WYSX-ray2.75A/B33-551[»]
2WZEX-ray2.50A/B33-551[»]
3ZI7X-ray2.30A/B792-1077[»]
4BAGX-ray1.90A/B792-1077[»]
4H35X-ray1.90A/B792-1077[»]
ProteinModelPortalP51584.
SMRP51584. Positions 561-719, 733-788, 803-1075.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP51584. 1 interaction.

Protein family/group databases

CAZyCBM22. Carbohydrate-Binding Module Family 22.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.1330.10. 1 hit.
2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProIPR016134. Cellulos_enz_dockerin_1.
IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
IPR003305. CenC_carb-bd.
IPR018242. Dockerin_1.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02018. CBM_4_9. 2 hits.
PF00404. Dockerin_1. 2 hits.
PF00756. Esterase. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
SSF63446. SSF63446. 1 hit.
PROSITEPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
PS00018. EF_HAND_1. 2 hits.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51584.

Entry information

Entry nameXYNY_CLOTM
AccessionPrimary (citable) accession number: P51584
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 101 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries