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Protein

Pectate lyase 1

Gene
N/A
Organism
Juniperus ashei (Ozark white cedar)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionLyase
LigandCalcium, Metal-binding

Enzyme and pathway databases

UniPathwayi
UPA00545;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...) asparagineSequence analysis1
Glycosylationi178N-linked (GlcNAc...) asparagineSequence 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

3D structure databases

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
InterProiView protein in InterPro
IPR018082 AmbAllergen
IPR002022 Pec_lyase
IPR012334 Pectin_lyas_fold
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF00544 Pec_lyase_C, 1 hit
PRINTSiPR00807 AMBALLERGEN
SMARTiView protein in SMART
SM00656 Amb_all, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiPLY1_JUNAS
AccessioniPrimary (citable) accession number: P81294
Secondary accession number(s): Q9ZNU7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: August 30, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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