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Q9C2Z0

- PLYA_ASPNG

UniProt

Q9C2Z0 - PLYA_ASPNG

Protein

Pectate lyase A

Gene

plyA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Pectinolytic enzyme 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. Favors pectate, the anion, over pectin, the methyl ester.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.

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi136 – 1361CalciumBy similarity
    Metal bindingi165 – 1651CalciumBy similarity
    Metal bindingi169 – 1691CalciumBy similarity
    Active sitei222 – 2221Sequence Analysis

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. pectate lyase activity Source: UniProtKB

    GO - Biological processi

    1. pectin catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiPL1. Polysaccharide Lyase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pectate lyase A (EC:4.2.2.2)
    Gene namesi
    Name:plyA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 323292Pectate lyase APRO_5000066020Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C2Z0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3866.

    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.

    Q9C2Z0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNFKWIVAA AGLLFGQVLA APTATSTHAK RATVSDAAFG YASLNGGTTG    50
    GAGGTTTTVS SYAAFTSAVS GDDAKVVYVD GTIKQTADQV KIGSNTSIIG 100
    KDANAILEGF GVLVKEKENV IIRNLGVSKV LADNGDAIGV QYSNNVWIDH 150
    CDVSSDRDHD KDYYDGLIDI THGSDYVTVS NTFIHDHWKA SLVGHSDSNE 200
    DEDSGHLTVT YANNYWYNVN SRAPSFRFGT GHVYNSYYLD VSDGINTRDG 250
    AQLLVESNQF VDSKKALYST DDGYAVSNDN DFGDSENTAE EGTLTSMPYD 300
    YTLLGSANVK AAVVGTAGQT LTF 323
    Length:323
    Mass (Da):34,369
    Last modified:June 1, 2001 - v1
    Checksum:iE7F438D307B816F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ276331 Genomic DNA. Translation: CAC33162.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ276331 Genomic DNA. Translation: CAC33162.1 .

    3D structure databases

    ProteinModelPortali Q9C2Z0.
    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 COG3866.

    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. "Characterization of Aspergillus niger pectate lyase A."
      Benen J.A., Kester H.C., Parenicova L., Visser J.
      Biochemistry 39:15563-15569(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GLYCOSYLATION, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

    Entry informationi

    Entry nameiPLYA_ASPNG
    AccessioniPrimary (citable) accession number: Q9C2Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3