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Q01172

- PELA_ASPNG

UniProt

Q01172 - PELA_ASPNG

Protein

Pectin lyase A

Gene

pelA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    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. polysaccharide catabolic process Source: UniProtKB-KW

    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-SubCell

    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

    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: October 1, 2014
    This is version 91 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