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Reviewed, UniProtKB/Swiss-Prot P49942 (XYNA_BACOV)

Last modified June 16, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 · Relevant documents

Names and origin

Protein namesRecommended name:
    Endo-1,4-beta-xylanase A
      Short name=Xylanase A
    EC=3.2.1.8
Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
Gene names
Name: xylI
OrganismBacteroides ovatus
Taxonomic identifier28116 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Induction

By xylan.

Sequence similarities

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

Ontologies

Keywords
   Biological processXylan degradation
   DomainSignal
   Molecular functionGlycosidase
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 – 2424 Potential
Chain25 – 376352Endo-1,4-beta-xylanase A
PRO_0000007966

Sites

Active site1601Proton donor By similarity
Active site2651Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P49942-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 40C3B36E2DAA3499

FASTA37642,980
        10         20         30         40         50         60 
MKLKRIILLL LTVMFSFSYG EVFAKDGSSL KKALKNKFLI GVSVNTHQSS GKDVAAVEIV 

        70         80         90        100        110        120 
KKNFNSIVAE NCMKSSVIHP KENKYNFAQA DEFVSFGESN QMAIIGHCLI WHSQLAPWFC 

       130        140        150        160        170        180 
VDKDGNNVSP EVLKKRMKDH ITTIVKRYKG RIKGWDVVNE AIEDNGAYRK TKFYEILGEE 

       190        200        210        220        230        240 
YIPLAFQYAH EADPDAELYY NDYSMAQPGR REAVVKMVND LKKRGIRIDA IGMQGHIGMD 

       250        260        270        280        290        300 
YPKISEFEKS MLAFAGTGVK IMITELDLTV IPSPNPNVGA EVSASFEYKK EMNPYPDGLP 

       310        320        330        340        350        360 
EEVSKAWTER MNDFFRLFLK HHNLITRVTL WGVADQNSWR NDWPMRGRTD YPLLFDRNYQ 

       370 
PKPVVGLIIK EAEKTK 

« Hide

References

[1]"Nucleotide sequences of xylan-inducible xylanase and xylosidase/arabinosidase genes from Bacteroides ovatus V975."
Whitehead T.R.
Biochim. Biophys. Acta 1244:239-241(1995) [PubMed: 7766665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: V975.

Cross-references

Sequence databases

U04957 Genomic DNA. Translation: AAB08023.1.
PIRS55892.

3D structure databases

HSSPHSSP built from PDB template 1HIZ based on UniProtKB P40943.
ModBaseSearch...

Protein family/group databases

CAZyGH10. Glycoside Hydrolase Family 10.

Enzyme and pathway databases

BRENDA3.2.1.8. 97613.

Family and domain databases

InterProIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_BACOV
AccessionPrimary (citable) accession number: P49942
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents