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Protein

Pectate lyase 1

Gene
N/A
Organism
Juniperus ashei (Ozark white cedar)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has low pectate lyase activity.1 Publication

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.1 Publication

Cofactori

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

Pathwayi: pectin 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 1
  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)DescriptionActionsGraphical viewLength
Metal bindingi170CalciumBy similarity1
Metal bindingi194CalciumBy similarity1
Metal bindingi198CalciumBy similarity1
Active sitei250Sequence analysis1

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 1 (EC:4.2.2.2)
Alternative name(s):
Major pollen allergen Jun a 1
Allergen: Jun a 1
OrganismiJuniperus ashei (Ozark white cedar)
Taxonomic identifieri13101 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaeCupressalesCupressaceaeJuniperus

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Binds to IgE. Causes seasonal allergic rhinitis in North America.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi224H → A: Reduced pectate lyase activity. 1 Publication1

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3337. Jun a 1.0101.
3338. Jun a 1.0102.
427. Jun a 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000002490822 – 367Pectate lyase 1Add BLAST346

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 451 Publication
Disulfide bondi128 ↔ 1471 Publication
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi178N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi306 ↔ 3121 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 30Combined sources5
Turni35 – 37Combined sources3
Helixi39 – 44Combined sources6
Helixi48 – 50Combined sources3
Turni55 – 58Combined sources4
Beta strandi59 – 64Combined sources6
Helixi79 – 84Combined sources6
Beta strandi89 – 95Combined sources7
Beta strandi97 – 99Combined sources3
Beta strandi109 – 114Combined sources6
Beta strandi120 – 123Combined sources4
Beta strandi129 – 133Combined sources5
Beta strandi135 – 141Combined sources7
Beta strandi143 – 145Combined sources3
Beta strandi152 – 158Combined sources7
Turni159 – 161Combined sources3
Beta strandi162 – 166Combined sources5
Beta strandi173 – 178Combined sources6
Beta strandi180 – 186Combined sources7
Beta strandi188 – 190Combined sources3
Beta strandi193 – 202Combined sources10
Beta strandi204 – 210Combined sources7
Beta strandi212 – 223Combined sources12
Helixi229 – 233Combined sources5
Beta strandi235 – 240Combined sources6
Beta strandi245 – 249Combined sources5
Beta strandi253 – 263Combined sources11
Beta strandi273 – 278Combined sources6
Beta strandi281 – 286Combined sources6
Beta strandi288 – 290Combined sources3
Helixi295 – 297Combined sources3
Beta strandi299 – 303Combined sources5
Helixi309 – 312Combined sources4
Beta strandi317 – 321Combined sources5
Beta strandi323 – 325Combined sources3
Turni344 – 346Combined sources3
Helixi353 – 355Combined sources3
Helixi356 – 359Combined sources4
Turni360 – 362Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PXZX-ray1.70A/B22-367[»]
ProteinModelPortaliP81294.
SMRiP81294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81294.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 305Beta-helixAdd BLAST268

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.

P81294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPCLIAVL VFLCAIVSCY SDNPIDSCWR GDSNWDQNRM KLADCAVGFG
60 70 80 90 100
SSTMGGKGGD FYTVTSTDDN PVNPTPGTLR YGATREKALW IIFSQNMNIK
110 120 130 140 150
LKMPLYVAGH KTIDGRGADV HLGNGGPCLF MRKVSHVILH SLHIHGCNTS
160 170 180 190 200
VLGDVLVSES IGVEPVHAQD GDAITMRNVT NAWIDHNSLS DCSDGLIDVT
210 220 230 240 250
LGSTGITISN NHFFNHHKVM LLGHDDTYDD DKSMKVTVAF NQFGPNAGQR
260 270 280 290 300
MPRARYGLVH VANNNYDPWN IYAIGGSSNP TILSEGNSFT APSESYKKEV
310 320 330 340 350
TKRIGCESPS ACANWVWRST RDAFINGAYF VSSGKTEETN IYNSNEAFKV
360
ENGNAAPQLT KNAGVVT
Length:367
Mass (Da):39,825
Last modified:December 1, 2000 - v1
Checksum:iFC9B81E675662E49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106663 mRNA. Translation: AAD03609.1.
AF106662 mRNA. Translation: AAD03608.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106663 mRNA. Translation: AAD03609.1.
AF106662 mRNA. Translation: AAD03608.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PXZX-ray1.70A/B22-367[»]
ProteinModelPortaliP81294.
SMRiP81294.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3337. Jun a 1.0101.
3338. Jun a 1.0102.
427. Jun a 1.
CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00545; UER00824.

Miscellaneous databases

EvolutionaryTraceiP81294.

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...

Entry informationi

Entry nameiPLY1_JUNAS
AccessioniPrimary (citable) accession number: P81294
Secondary accession number(s): Q9ZNU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 2, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.