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Protein

Pectate lyase A

Gene

plyA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: 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

Ca2+1 PublicationNote: Binds 1 Ca2+ 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

  • metal ion binding Source: UniProtKB-KW
  • pectate lyase activity Source: UniProtKB

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • 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

Enzyme and pathway databases

BRENDAi4.2.2.2. 518.

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

GO - Cellular componenti

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

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

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00008167.

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

        10         20         30         40         50
MTNFKWIVAA AGLLFGQVLA APTATSTHAK RATVSDAAFG YASLNGGTTG
60 70 80 90 100
GAGGTTTTVS SYAAFTSAVS GDDAKVVYVD GTIKQTADQV KIGSNTSIIG
110 120 130 140 150
KDANAILEGF GVLVKEKENV IIRNLGVSKV LADNGDAIGV QYSNNVWIDH
160 170 180 190 200
CDVSSDRDHD KDYYDGLIDI THGSDYVTVS NTFIHDHWKA SLVGHSDSNE
210 220 230 240 250
DEDSGHLTVT YANNYWYNVN SRAPSFRFGT GHVYNSYYLD VSDGINTRDG
260 270 280 290 300
AQLLVESNQF VDSKKALYST DDGYAVSNDN DFGDSENTAE EGTLTSMPYD
310 320
YTLLGSANVK AAVVGTAGQT LTF
Length:323
Mass (Da):34,369
Last modified:June 1, 2001 - v1
Checksum:iE7F438D307B816F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276331 Genomic DNA. Translation: CAC33162.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ276331 Genomic DNA. Translation: CAC33162.1.

3D structure databases

ProteinModelPortaliQ9C2Z0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00008167.

Protein family/group databases

CAZyiPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG3866.

Enzyme and pathway databases

BRENDAi4.2.2.2. 518.

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.
ProtoNetiSearch...

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: June 24, 2015
This is version 52 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.