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Unreviewed, UniProtKB/TrEMBL Q59675 (Q59675_9GAMM)

Last modified November 25, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Endo-beta-1,4-xylanase EMBL CAA88764.2
    EC=3.2.1.8
OrganismCellvibrio japonicus EMBL CAA88764.2
Taxonomic identifier155077 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Ontologies

Keywords

   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase RuleBase RU003432V0
Hydrolase

Gene Ontology (GO)

   Biological processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential EMBL CAA88764.2
Chain20 – 606587 Potential EMBL CAA88764.2
PRO_5000147609

Sequences

Sequence LengthMass (Da)Tools
Q59675-1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 56E149954CE6BFEE

FASTA60664,884
        10         20         30         40         50         60 
MKKIQQLLML SLISSTLIAC GGGGGGGSTP TTSSSPQSSS PASTPSSASS SSIISSSSLS 

        70         80         90        100        110        120 
SSLSSSSLSS SSLSSSSASS VSSSSVAASE GNVVIEVDMA NGWRGNASGS TSHSGITYSA 

       130        140        150        160        170        180 
DGVTFAALGD GVGAVFDIAR PTTLEDAVIA MVVNVSAEFK ASEANLQIFA QLKEDWSKGE 

       190        200        210        220        230        240 
WDCLAASSEL TADTDLTLTC TIDEDDDKFN QTARDVQVGI QAKGTPAGTI TIKSVTITLA 

       250        260        270        280        290        300 
QEAYSANVDH LRDLAPSDFP IGVAVSNTDS ATYNLLTNSR EQAVVKKHFN HLTAGNIMKM 

       310        320        330        340        350        360 
SYMQPTEGNF NFTNADAFVD WATENNMTVH GHALVWHSDY QVPNFMKNWA GSAEDFLAAL 

       370        380        390        400        410        420 
DTHITTIVDH YEAKGNLVSW DVVNEAIDDN SPANFRTTDS AFYVKSGNSS VYIERAFQTA 

       430        440        450        460        470        480 
RAADPAVILY YNDYNIEQNN AKTTKMVDMV KDFQARSIPI DGVGFQMHVC MNYPSIANIS 

       490        500        510        520        530        540 
AAMKKVVDLG LLVKITELDV AVNQPHCDAY PANKINPLTE AAQLAQKKRY CDVVKAYLDT 

       550        560        570        580        590        600 
VPVNQRGGIS VWGTTDANTW LDGLYREQFE DEKISWPLLF DNNYNDKPAL RGFADALIGT 


QCTNTH 

« Hide

References

[1]"Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus."
Millward-Sadler S.J., Davidson K., Hazlewood G.P., Black G.W., Gilbert H.J., Clarke J.H.
Biochem. J. 312:39-48(1995) [PubMed: 7492333] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]Gilbert H.J.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Structure of a family 15 carbohydrate-binding module in complex with xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation."
Szabo L., Jamal S., Xie H., Charnock S.J., Bolam D.N., Gilbert H.J., Davies G.J.
J. Biol. Chem. 276:49061-49065(2001) [PubMed: 11598143] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 91-243.
[4]"Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases."
Pell G., Szabo L., Charnock S.J., Xie H., Gloster T.M., Davies G.J., Gilbert H.J.
J. Biol. Chem. 279:11777-11788(2004) [PubMed: 14670951] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 86-606.

Cross-references

Sequence databases

Z48928 Genomic DNA. Translation: CAA88764.2.
PIRS59634.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GNYX-ray1.63A91-243[»]
ModBaseSearch...

Family and domain databases

InterProIPR005088. CBM_15.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sub_cat.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF03426. CBM_15. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Entry information

Entry nameQ59675_9GAMM
AccessionPrimary (citable) accession number: Q59675
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: March 1, 2004
Last modified: November 25, 2008
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information