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Protein

Pectin lyase A

Gene

pelA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.

Catalytic activityi

Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei256Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi4.2.2.10. 518.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Pectin lyase A (EC:4.2.2.10)
Short name:
PLA
Alternative name(s):
Pectin lyase II
Short name:
PLII
Gene namesi
Name:pelA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000002489621 – 379Pectin lyase AAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi83 ↔ 102
Glycosylationi88O-linked (Man)1
Disulfide bondi92 ↔ 226
Glycosylationi129N-linked (GlcNAc...)Curated1
Disulfide bondi322 ↔ 330
Glycosylationi368O-linked (Man); in strain 4M-1471

Post-translational modificationi

N-glycosylated at Asn-129 and O-glycosylated at Thr-88 when expressed in Aspergillus nidulans. The protein from strain 4M-147 is O-glycosylated at Thr-88 and Ser-368. PubMed:9195887 modeled GalNAc at the O-glycosylation site, a glycosylation not observed in fungi. The O-linked saccharide is probably mannose.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ01172.
PRIDEiQ01172.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 31Combined sources3
Turni36 – 39Combined sources4
Helixi48 – 56Combined sources9
Beta strandi57 – 59Combined sources3
Beta strandi61 – 65Combined sources5
Beta strandi67 – 70Combined sources4
Turni72 – 75Combined sources4
Beta strandi77 – 83Combined sources7
Beta strandi94 – 96Combined sources3
Helixi98 – 100Combined sources3
Helixi101 – 105Combined sources5
Beta strandi111 – 119Combined sources9
Beta strandi124 – 126Combined sources3
Beta strandi128 – 134Combined sources7
Turni136 – 138Combined sources3
Beta strandi140 – 143Combined sources4
Beta strandi146 – 148Combined sources3
Beta strandi153 – 159Combined sources7
Beta strandi161 – 165Combined sources5
Beta strandi175 – 178Combined sources4
Beta strandi182 – 188Combined sources7
Beta strandi190 – 196Combined sources7
Beta strandi198 – 201Combined sources4
Beta strandi208 – 213Combined sources6
Beta strandi215 – 217Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi226 – 231Combined sources6
Beta strandi234 – 236Combined sources3
Beta strandi242 – 247Combined sources6
Beta strandi249 – 253Combined sources5
Beta strandi265 – 270Combined sources6
Beta strandi272 – 283Combined sources12
Beta strandi288 – 293Combined sources6
Beta strandi295 – 311Combined sources17
Helixi318 – 322Combined sources5
Helixi323 – 326Combined sources4
Beta strandi334 – 338Combined sources5
Helixi349 – 352Combined sources4
Helixi363 – 365Combined sources3
Helixi366 – 373Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IDJX-ray2.40A/B21-379[»]
1IDKX-ray1.93A21-379[»]
ProteinModelPortaliQ01172.
SMRiQ01172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01172.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 1 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
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.

Q01172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYSTIFSAA AAVFAGSAAA VGVSGSAEGF AEGVTGGGDA TPVYPDTIDE
60 70 80 90 100
LVSYLGDDEA RVIVLTKTFD FTDSEGTTTG TGCAPWGTAS ACQVAIDQDD
110 120 130 140 150
WCENYEPDAP SVSVEYYNAG VLGITVTSNK SLIGEGSSGA IKGKGLRIVS
160 170 180 190 200
GAENIIIQNI AVTDINPKYV WGGDAITLDD CDLVWIDHVT TARIGRQHYV
210 220 230 240 250
LGTSADNRVS LTNNYIDGVS DYSATCDGYH YWGIYLDGDA DLVTMKGNYI
260 270 280 290 300
YHTSGRSPKV QDNTLLHCVN NYFYDISGHA FEIGEGGYVL AEGNVFQNVD
310 320 330 340 350
TVLETYEGAA FTVPSTTAGE VCSTYLGRDC VINGFGCSGT FSEDSTSFLS
360 370
DFEGKNIASA SAYTSVASRV VANAGQGNL
Length:379
Mass (Da):39,855
Last modified:July 1, 1993 - v1
Checksum:i4DF1326BFFCA77B5
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti32E → K in strain: 4M-147. 1 Publication1
Natural varianti39D → S in strain: 4M-147. 1 Publication1
Natural varianti121V → T in strain: 4M-147. 1 Publication1
Natural varianti233G → A in strain: 4M-147. 1 Publication1
Natural varianti268C → A in strain: 4M-147. 1 Publication1
Natural varianti273F → W in strain: 4M-147. 1 Publication1
Natural varianti309A → E in strain: 4M-147. 1 Publication1
Natural varianti316T → S in strain: 4M-147. 1 Publication1
Natural varianti337C → S in strain: 4M-147. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60724 Genomic DNA. Translation: CAA43130.1.
X55784 Genomic DNA. Translation: CAA39305.1.
PIRiS17979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60724 Genomic DNA. Translation: CAA43130.1.
X55784 Genomic DNA. Translation: CAA39305.1.
PIRiS17979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IDJX-ray2.40A/B21-379[»]
1IDKX-ray1.93A21-379[»]
ProteinModelPortaliQ01172.
SMRiQ01172.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Proteomic databases

PaxDbiQ01172.
PRIDEiQ01172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.2.2.10. 518.

Miscellaneous databases

EvolutionaryTraceiQ01172.

Family and domain databases

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

Entry informationi

Entry nameiPELA_ASPNG
AccessioniPrimary (citable) accession number: Q01172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.