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P54865 (XYND_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. 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:
Bifunctional xylanase/deacetylase

Including the following 2 domains:

  1. Endo-1,4-beta-xylanase D
    Short name=XYLD
    Short name=Xylanase D
    EC=3.2.1.8
  2. Acetylated xylan deacetylase
    EC=3.5.1.-
Gene names
Name:xynD
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length644 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 displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Sequence similarities

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

Contains 2 CBM2 (carbohydrate binding type-2) domains.

Contains 1 NodB homology domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343 Potential
Chain44 – 644601Bifunctional xylanase/deacetylase
PRO_0000008000

Regions

Domain246 – 33388CBM2 1
Domain356 – 532177NodB homology
Domain557 – 64488CBM2 2
Region44 – 230187Endoglucanase
Region231 – 24515Linker ("hinge") (Gly-rich box)
Region337 – 35014Linker ("hinge") (Pro-Thr box)
Region548 – 5569Linker ("hinge") (Gly-rich box)
Compositional bias231 – 2388Poly-Gly

Sites

Active site1261Nucleophile By similarity
Active site2161Proton donor By similarity

Secondary structure

................................. 644
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54865 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 56B045CC6E0E1820

FASTA64466,582
        10         20         30         40         50         60 
MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG THDGYFYSFW 

        70         80         90        100        110        120 
TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV SYSGQFNPSR NAYLTLYGWT 

       130        140        150        160        170        180 
QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG GTYDIYRTQR VNKPSIEGDS STFYQYWSVR 

       190        200        210        220        230        240 
QQKRTGGTIT SGNHFDAWAS KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT 

       250        260        270        280        290        300 
GGGGGSTGCS VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS 

       310        320        330        340        350        360 
TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP QSCSAGYVGL 

       370        380        390        400        410        420 
TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL MQAYKNAGVQ IGNHSWDHPH 

       430        440        450        460        470        480 
LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL FRPPYGESNA TLRQVESSLG LREIIWDVDS 

       490        500        510        520        530        540 
QDWNNASASQ IRQAASRLTN GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR 

       550        560        570        580        590        600 
AVAPSSAGGG GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS 

       610        620        630        640 
SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG 

« Hide

References

[1]"Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases."
Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P., Clarke J.H., Gilbert H.J.
Mol. Microbiol. 11:375-382(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 221.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76729 Genomic DNA. Translation: CAA54145.1.
PIRI40712.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5BNMR-A247-333[»]
1E5CNMR-A247-333[»]
1HEHNMR-C557-644[»]
1HEJNMR-C557-644[»]
1XBDNMR-A247-333[»]
2XBDNMR-A247-333[»]
ProteinModelPortalP54865.
SMRP54865. Positions 15-235, 247-333, 356-544, 557-644.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM2. Carbohydrate-Binding Module Family 2.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.8. 1233.
UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.180. 1 hit.
2.60.40.290. 2 hits.
3.20.20.370. 1 hit.
InterProIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR008985. ConA-like_lec_gl_sf.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR002509. Polysac_deacetylase.
IPR006311. TAT_signal.
[Graphical view]
PfamPF00553. CBM_2. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSPR00911. GLHYDRLASE11.
SMARTSM00637. CBD_II. 2 hits.
[Graphical view]
SUPFAMSSF49384. SSF49384. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEPS51173. CBM2. 2 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS51677. NODB. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54865.

Entry information

Entry nameXYND_CELFI
AccessionPrimary (citable) accession number: P54865
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 96 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries