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Reviewed, UniProtKB/Swiss-Prot Q05526 (PELW_DICD3)

Last modified January 19, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Pectate disaccharide-lyase
    EC=4.2.2.9
Alternative name(s):
    Exopolygalacturonate lyase
      Short name=ExoPL
Gene names
Name: pelW
Synonyms: kdgC
OrganismDickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Taxonomic identifier198628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the formation of unsaturated digalacturonates from polygalacturonate or short oligogalacturonates.

Catalytic activity

Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate from the reducing end of pectate, i.e. de-esterified pectin.

Cofactor

Copper.

Manganese.

Nickel.

Pathway

Glycan metabolism; pectin degradation.

Subcellular location

Cytoplasm.

Induction

By galacturonate and PGA, and inhibited by EDTA.

Sequence similarities

Belongs to the polysaccharide lyase 2 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Manganese
Nickel
   Molecular functionLyase
Gene Ontology (GO)
   Biological processpectin catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate disaccharide-lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Pectate disaccharide-lyase
PRO_0000212998

Sequences

Sequence LengthMass (Da)Tools
Q05526-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: CC1FF8782E33F1E8

FASTA55364,074
        10         20         30         40         50         60 
MSIFTDLNTS RKWQIDQWLS AVNSHIEKIQ QYGHSVVNPT PLLADGFEIK TQSPVVWQFP 

        70         80         90        100        110        120 
DGHDAPISNF ASQQNWLRLL ISMSVITETE KYRHLAFCQS EYFLNRFVDE NSGLFYWGGH 

       130        140        150        160        170        180 
RFINLDTLAS EGPESKSMVH ELKHHLPYYE FLHQVNPEKT RHFIQGFWNA HVEDWSCLDL 

       190        200        210        220        230        240 
GRHGDYARQR DPDVFLHSRH DVVTPANWPE LPLTKGLTFV NAGTDLIYAA FVYARHTGDA 

       250        260        270        280        290        300 
HAAAWGKHLY RQYVLARNPE TGMPVYQFSS PLQRQPVPAD DNQTQSWFGD RAQRQFGPEF 

       310        320        330        340        350        360 
GAIAREANVL FRDMRPLLID NPLAMLDILR HQPDAEILTW VIAGLKNYYQ YAYDVNSNSL 

       370        380        390        400        410        420 
RPMWNNGQDM TDYCFKRDGY YGKAGTVLKP FPLEGDYLLP LVRAWLLSDD DDLHTLIVTM 

       430        440        450        460        470        480 
LSRLEKQGIH QSASPFLLLA ITELAHAKQS AQWAEYAWQM AEILFKRYFH HGLFVRSEHH 

       490        500        510        520        530        540 
RYVRLDDPFP AILLTLIAAC RNKWSEVPAV LTQGGYIHGD YRINGESRVI YDTGIYLPRK 

       550 
INPLILFLQI HHY 

« Hide

References

[1]"Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation."
Condemine G., Robert-Baudouy J.
Mol. Microbiol. 5:2191-2202(1991) [PubMed: 1766386] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937."
Shevchik V.E., Condemine G., Robert-Baudouy J., Hugouvieux-Cotte-Pattat N.
J. Bacteriol. 181:3912-3919(1999) [PubMed: 10383957] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO C-TERMINUS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62073 Genomic DNA. Translation: CAA43990.1.
PIRS17712.

3D structure databases

SMRQ05526. Positions 17-537.
ModBaseSearch...

Protein family/group databases

CAZyPL2. Polysaccharide Lyase Family 2.

Family and domain databases

InterProIPR010702. Pectate_lyase_2.
[Graphical view]
PfamPF06917. Pectate_lyase_2. 1 hit.
[Graphical view]
PIRSFPIRSF001432. Pect_lyase. 1 hit.
ProtoNetSearch...

Entry information

Entry namePELW_DICD3
AccessionPrimary (citable) accession number: Q05526
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: January 19, 2010
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

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