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Protein

Pectate lyase 2

Gene
N/A
Organism
Ambrosia artemisiifolia (Short ragweed)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has pectate lyase activity.By similarity

Catalytic activityi

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.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Pathway:ipectin degradation

This protein is involved in step 2 of the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Pectate lyase 4, Pectate lyase 1, Pectate lyase 2, Pectate lyase (amba1.3), Pectate lyase (amba1.3), Pectate lyase (amba1.2), Pectate lyase (amba1.3), Pectate lyase (amba1.4), Pectate lyase (amba1.3), Pectate lyase (amba1.3), Pectate lyase (amba1), Pectate lyase (amba2.01), Pectate lyase (amba2.01), Pectate lyase 5, Pectate lyase 3
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway pectin degradation, which is itself part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-dehydro-3-deoxy-D-gluconate from pectin, the pathway pectin degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941CalciumBy similarity
Metal bindingi218 – 2181CalciumBy similarity
Metal bindingi222 – 2221CalciumBy similarity
Active sitei274 – 2741Sequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectate lyase 2 (EC:4.2.2.2)
Alternative name(s):
Antigen Amb a I
Antigen E
Short name:
AgE
Pollen allergen Amb a 1.3
Allergen: Amb a 1.3
OrganismiAmbrosia artemisiifolia (Short ragweed)
Taxonomic identifieri4212 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceHeliantheaeAmbrosia

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. This is one of the major allergens of the ragweed pollen.1 Publication

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei24. Amb a 1.
789. Amb a 1.0301.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 397372Pectate lyase 2PRO_0000024903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi54 ↔ 71By similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Pollen and flowers.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP27761.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIKQCCYIL YFTLALVALL QPVRSAEGVG EILPSVNETR SLQACEALNI
60 70 80 90 100
IDKCWRGKAD WENNRQALAD CAQGFAKGTY GGKWGDVYTV TSNLDDDVAN
110 120 130 140 150
PKEGTLRFAA AQNRPLWIIF KNDMVINLNQ ELVVNSDKTI DGRGVKVEII
160 170 180 190 200
NGGLTLMNVK NIIIHNINIH DVKVLPGGMI KSNDGPPILR QASDGDTINV
210 220 230 240 250
AGSSQIWIDH CSLSKSFDGL VDVTLGSTHV TISNCKFTQQ SKAILLGADD
260 270 280 290 300
THVQDKGMLA TVAFNMFTDN VDQRMPRCRF GFFQVVNNNY DRWGTYAIGG
310 320 330 340 350
SSAPTILCQG NRFLAPDDQI KKNVLARTGT GAAESMAWNW RSDKDLLENG
360 370 380 390
AIFVTSGSDP VLTPVQSAGM IPAEPGEAAI KLTSSAGVFS CHPGAPC
Length:397
Mass (Da):42,928
Last modified:August 1, 1992 - v1
Checksum:iC8DB41257590DD0A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481L → Y.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62961 mRNA. Translation: AAA32668.1.
M80560 mRNA. Translation: AAA32669.1. Sequence problems.
PIRiC39099.
C53240.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62961 mRNA. Translation: AAA32668.1.
M80560 mRNA. Translation: AAA32669.1. Sequence problems.
PIRiC39099.
C53240.

3D structure databases

ProteinModelPortaliP27761.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei24. Amb a 1.
789. Amb a 1.0301.
CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR018082. AmbAllergen.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
PRINTSiPR00807. AMBALLERGEN.
SMARTiSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning of Amb a I (antigen E), the major allergen family of short ragweed pollen."
    Rafnar T., Griffith I.J., Kuo M.-C., Bond J.F., Rogers B.L., Klapper D.G.
    J. Biol. Chem. 266:1229-1236(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.
    Tissue: Pollen.
  2. "Sequence polymorphism of Amb a I and Amb a II, the major allergens in Ambrosia artemisiifolia (short ragweed)."
    Griffith I.J., Pollock J., Klapper D.G., Rogers B.L., Nault A.K.
    Int. Arch. Allergy Appl. Immunol. 96:296-304(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS.
    Tissue: Pollen.

Entry informationi

Entry nameiPLY2_AMBAR
AccessioniPrimary (citable) accession number: P27761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.