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Reviewed, UniProtKB/Swiss-Prot P0C1A6 (PELL_ERWCH)

Last modified November 24, 2009. Version 22. 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

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Names and origin

Protein namesRecommended name:
    Pectate lyase L
    EC=4.2.2.2
Alternative name(s):
    Pectate transeliminase
Gene names
Name: pelL
OrganismErwinia chrysanthemi
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

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Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Presents an endo-cleaving activity on polygalacturonate or partially methylated pectin By similarity.

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Cofactor

Calcium By similarity.

Pathway

Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the polysaccharide lyase 9 family.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 425400Pectate lyase L
PRO_0000024936

Secondary structure

1 .................................................................................. 425
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P0C1A6-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: BE2557332CFF91F7

FASTA42545,537
        10         20         30         40         50         60 
MKYLNCFIST GLAAFFLVNS TSVLAADCSS DLTSGISTKR IYYVAPNGSS SNNGNSFNSP 

        70         80         90        100        110        120 
MSFTAAMAAA NPGELILLKP GTYTIPYTQG KGNTITFNKS GKEGSPIYVA AANCGRAVFD 

       130        140        150        160        170        180 
FSFPDSQWVQ ASYGFYVTGD YWYFKGIEVT RAGYQGAYVT GSHNTFENTA FHHNRNTGLE 

       190        200        210        220        230        240 
INNGGSYNTV INSDAYRNYD PKKNGSMADG FGPKQKQGQG NRFGGCRAWE NSDDGFDLFD 

       250        260        270        280        290        300 
SPQKVVIENS WAFRNGINYW SDSSFAGNGN GFKLGGNQAV GNHRITRSVA FGNVSKGFDQ 

       310        320        330        340        350        360 
NNNAGGVTVI NNTSYKNGIN YGFGSNVKSG QKHYFRNNVS LSGSATVNNA DAKSNSWDTG 

       370        380        390        400        410        420 
PVASASDFVS LDTSLATISR DNDGTLPETA LFRLSTNSKL INAGTKESNI SYSGSAPDLG 


AFERN

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References

[1]"Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine-rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes."
Alfano J.R., Ham J.H., Collmer A.
J. Bacteriol. 177:4553-4556(1995) [PubMed: 7635842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EC16.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42248 Genomic DNA. Translation: AAA99476.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RU4X-ray1.60A26-425[»]
ModBaseSearch...

Protein family/group databases

CAZyPL9. Polysaccharide Lyase Family 9.

Enzyme and pathway databases

BRENDA4.2.2.2. 1459.

Family and domain databases

InterProIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
SMARTSM00710. PbH1. 5 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePELL_ERWCH
AccessionPrimary (citable) accession number: P0C1A6
Secondary accession number(s): Q47473, Q59421
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: April 18, 2006
Last modified: November 24, 2009
This is version 22 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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