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Q9C2Z0

- PLYA_ASPNG

UniProt

Q9C2Z0 - PLYA_ASPNG

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Protein
Pectate lyase A
Gene
plyA
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 – 1361Calcium By similarity
Metal bindingi165 – 1651Calcium By similarity
Metal bindingi169 – 1691Calcium By similarity
Active sitei222 – 2221 Reviewed prediction

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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131
Add
BLAST
Chaini32 – 323292Pectate lyase A
PRO_5000066020Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9C2Z0.

Family & Domainsi

Sequence similaritiesi

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

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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: November 13, 2013
This is version 47 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

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