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Q01172

- PELA_ASPNG

UniProt

Q01172 - PELA_ASPNG

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Protein

Pectin lyase A

Gene

pelA

Organism
Aspergillus niger
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei256 – 2561Sequence Analysis

GO - Molecular functioni

  1. pectin lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

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

Secreted Curated

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 379359Pectin lyase APRO_0000024896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi83 ↔ 102
Glycosylationi88 – 881O-linked (Man)
Disulfide bondi92 ↔ 226
Glycosylationi129 – 1291N-linked (GlcNAc...)Curated
Disulfide bondi322 ↔ 330
Glycosylationi368 – 3681O-linked (Man); in strain 4M-147

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

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313
Turni36 – 394
Helixi48 – 569
Beta strandi57 – 593
Beta strandi61 – 655
Beta strandi67 – 704
Turni72 – 754
Beta strandi77 – 837
Beta strandi94 – 963
Helixi98 – 1003
Helixi101 – 1055
Beta strandi111 – 1199
Beta strandi124 – 1263
Beta strandi128 – 1347
Turni136 – 1383
Beta strandi140 – 1434
Beta strandi146 – 1483
Beta strandi153 – 1597
Beta strandi161 – 1655
Beta strandi175 – 1784
Beta strandi182 – 1887
Beta strandi190 – 1967
Beta strandi198 – 2014
Beta strandi208 – 2136
Beta strandi215 – 2173
Beta strandi221 – 2233
Beta strandi226 – 2316
Beta strandi234 – 2363
Beta strandi242 – 2476
Beta strandi249 – 2535
Beta strandi265 – 2706
Beta strandi272 – 28312
Beta strandi288 – 2936
Beta strandi295 – 31117
Helixi318 – 3225
Helixi323 – 3264
Beta strandi334 – 3385
Helixi349 – 3524
Helixi363 – 3653
Helixi366 – 3738

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IDJX-ray2.40A/B21-379[»]
1IDKX-ray1.93A21-379[»]
ProteinModelPortaliQ01172.
SMRiQ01172. Positions 21-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01172.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG306793.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321E → K in strain: 4M-147. 1 Publication
Natural varianti39 – 391D → S in strain: 4M-147. 1 Publication
Natural varianti121 – 1211V → T in strain: 4M-147. 1 Publication
Natural varianti233 – 2331G → A in strain: 4M-147. 1 Publication
Natural varianti268 – 2681C → A in strain: 4M-147. 1 Publication
Natural varianti273 – 2731F → W in strain: 4M-147. 1 Publication
Natural varianti309 – 3091A → E in strain: 4M-147. 1 Publication
Natural varianti316 – 3161T → S in strain: 4M-147. 1 Publication
Natural varianti337 – 3371C → S in strain: 4M-147. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60724 Genomic DNA. Translation: CAA43130.1.
X55784 Genomic DNA. Translation: CAA39305.1.
PIRiS17979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60724 Genomic DNA. Translation: CAA43130.1 .
X55784 Genomic DNA. Translation: CAA39305.1 .
PIRi S17979.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IDJ X-ray 2.40 A/B 21-379 [» ]
1IDK X-ray 1.93 A 21-379 [» ]
ProteinModelPortali Q01172.
SMRi Q01172. Positions 21-379.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi PL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG306793.

Miscellaneous databases

EvolutionaryTracei Q01172.

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view ]
Pfami PF00544. Pec_lyase_C. 1 hit.
[Graphical view ]
SMARTi SM00656. Amb_all. 1 hit.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans."
    Kusters-Van Someren M.A., Harmsen J.A.M., Kester H.C.M., Visser J.
    Curr. Genet. 20:293-299(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40 AND 115-125.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. "Cloning and expression of a second Aspergillus niger pectin lyase gene (pelA): indications of a pectin lyase gene family in A. niger."
    Harmsen J.A.M., Kurster-Van Sommeren M.A., Visser J.
    Curr. Genet. 18:161-166(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  3. "Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases."
    Mayans O., Scott M., Connerton I., Gravesen T., Benen J., Visser J., Pickersgill R., Jenkins J.
    Structure 5:677-689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-379 FOR STRAIN N400, X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 21-379 FOR STRAIN 4M-147, VARIANTS LYS-32; SER-39; THR-121; ALA-233; ALA-268; TRP-273; GLU-309; SER-316 AND SER-337.
    Strain: 4M-147 and ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

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: October 29, 2014
This is version 92 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

External Data

Dasty 3