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Reviewed, UniProtKB/Swiss-Prot O24554 (PEL_ZINEL)

Last modified September 22, 2009. Version 56. 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 lyase
    EC=4.2.2.2
Alternative name(s):
    ZePel
OrganismZinnia elegans (Zinnia)
Taxonomic identifier34245 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheaeZinnia

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the degradation of pectin. May assist in the removal and modification of an existing pectin matrix in order to allow the deposition of newly synthesized walls polymers for a specialized function or to create an architecture that is extensible.

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

Binds 1 calcium ion. Required for its activity.

Pathway

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

Tissue specificity

Expressed in sites of vascular differentiation and in new primordia on the flank of the shoot meristem.

Induction

Up-regulated by auxin.

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

Biophysicochemical properties

Kinetic parameters:

Vmax=0.12 µmol/min/mg enzyme

pH dependence:

Optimum pH is 10.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein
Gene Ontology (GO)
   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 401381Pectate lyase
PRO_0000024893

Sites

Active site2791 Potential
Metal binding1991Calcium By similarity
Metal binding2231Calcium By similarity
Metal binding2271Calcium By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O24554-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B5EA3B57A9830F02

FASTA40144,407
        10         20         30         40         50         60 
MATTILPLIL FISSLAIASS SPSRTPHAIV NEVHKSINAS RRNLGYLSCG TGNPIDDCWR 

        70         80         90        100        110        120 
CDPNWANNRQ RLADCAIGFG KNAMGGRNGR IYVVTDPGND DPVNPVPGTL RYAVIQDEPL 

       130        140        150        160        170        180 
WIIFKRDMVI QLRQELVMNS HKTIDGRGVN VHIGNGPCIT IHYASNIIIH GIHIHDCKQA 

       190        200        210        220        230        240 
GNGNIRNSPH HSGWWTQSDG DGISIFASKD IWIDHNSLSN CHDGLIDAIH GSTAITISNN 

       250        260        270        280        290        300 
YMTHHDKVML LGHSDSYTQD KNMQVTIAFN HFGEGLVQRM PRCRHGYFHV VNNDYTHWEM 

       310        320        330        340        350        360 
YAIGGSASPT IYSQGNRFLA PNTRFDKEVT KHENAPESEW KNWNWRSEGD LMLNGAYFRE 

       370        380        390        400 
SGGRAASSFA RASSLSGRPS TLVASMTRSA GALVCRKGSR C 

« Hide

References

[1]"A pectate lyase from Zinnia elegans is auxin inducible."
Domingo C., Roberts K., Stacey N.J., Connerton I., Ruiz-Teran F., McCann M.C.
Plant J. 13:17-28(1998) [PubMed: 9680962] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Envy.

Cross-references

Sequence databases

Y09541 mRNA. Translation: CAA70735.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Enzyme and pathway databases

BRENDA4.2.2.2. 228834.

Family and domain databases

InterProIPR002022. Amb_allergen.
IPR018082. AmbAllergen.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSPR00807. AMBALLERGEN.
SMARTSM00656. Amb_all. 1 hit.
SM00710. PbH1. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEL_ZINEL
AccessionPrimary (citable) accession number: O24554
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: January 1, 1998
Last modified: September 22, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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