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P0C1A6 (PLYL_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Pectate lyase L

EC=4.2.2.2
Alternative name(s):
Pectate transeliminase
Gene names
Name:pelL
OrganismErwinia chrysanthemi
Taxonomic identifier556 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processpectin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Sites

Active site2731Proton acceptor By similarity
Metal binding2091Calcium 1 By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2341Calcium 1 By similarity
Metal binding2371Calcium 1 By similarity
Metal binding4021Calcium 2 By similarity
Metal binding4131Calcium 2; via carbonyl oxygen By similarity
Metal binding4161Calcium 2; via carbonyl oxygen By similarity
Metal binding4181Calcium 2 By similarity
Metal binding4231Calcium 2 By similarity

Amino acid modifications

Disulfide bond28 ↔ 114 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C1A6 [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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EC16.

Cross-references

Sequence databases

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

3D structure databases

ProteinModelPortalP0C1A6.
SMRP0C1A6. Positions 26-425.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyPL9. Polysaccharide Lyase Family 9.

Proteomic databases

PRIDEP0C1A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00545; UER00824.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SMARTSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMSSF51126. SSF51126. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLYL_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: October 16, 2013
This is version 37 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

PATHWAY comments

Index of metabolic and biosynthesis pathways