SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01172

- PELA_ASPNG

UniProt

Q01172 - PELA_ASPNG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 2561 Reviewed prediction

GO - Molecular functioni

  1. pectin lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. 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 Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
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...) Inferred
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. 1 Publication 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.

Miscellaneous databases

EvolutionaryTraceiQ01172.

Family & Domainsi

Sequence similaritiesi

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

MKYSTIFSAA AAVFAGSAAA VGVSGSAEGF AEGVTGGGDA TPVYPDTIDE    50
LVSYLGDDEA RVIVLTKTFD FTDSEGTTTG TGCAPWGTAS ACQVAIDQDD 100
WCENYEPDAP SVSVEYYNAG VLGITVTSNK SLIGEGSSGA IKGKGLRIVS 150
GAENIIIQNI AVTDINPKYV WGGDAITLDD CDLVWIDHVT TARIGRQHYV 200
LGTSADNRVS LTNNYIDGVS DYSATCDGYH YWGIYLDGDA DLVTMKGNYI 250
YHTSGRSPKV QDNTLLHCVN NYFYDISGHA FEIGEGGYVL AEGNVFQNVD 300
TVLETYEGAA FTVPSTTAGE VCSTYLGRDC VINGFGCSGT FSEDSTSFLS 350
DFEGKNIASA SAYTSVASRV VANAGQGNL 379
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: November 13, 2013
This is version 90 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

Similar proteinsi