Q9C2Z0 (PLYA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pectate lyase A
EC=4.2.2.2

Gene names

Name:

plyA

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Pectinolytic enzyme consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectine 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. Ref.1
Catalytic activity	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.
Cofactor	Binds 1 calcium ion per subunit. Ref.1
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the polysaccharide lyase 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Glycoprotein
Gene Ontology (GO)
Biological_process	pectin catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pectate lyase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31
	Chain	32 – 323	292	Pectate lyase A		PRO_5000066020
Sites
	Active site	222	1	Potential
	Metal binding	136	1	Calcium By similarity
	Metal binding	165	1	Calcium By similarity
	Metal binding	169	1	Calcium By similarity
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9C2Z0 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: E7F438D307B816F2	FASTA	323	34,369
	10 20 30 40 50 60 MTNFKWIVAA AGLLFGQVLA APTATSTHAK RATVSDAAFG YASLNGGTTG GAGGTTTTVS 70 80 90 100 110 120 SYAAFTSAVS GDDAKVVYVD GTIKQTADQV KIGSNTSIIG KDANAILEGF GVLVKEKENV 130 140 150 160 170 180 IIRNLGVSKV LADNGDAIGV QYSNNVWIDH CDVSSDRDHD KDYYDGLIDI THGSDYVTVS 190 200 210 220 230 240 NTFIHDHWKA SLVGHSDSNE DEDSGHLTVT YANNYWYNVN SRAPSFRFGT GHVYNSYYLD 250 260 270 280 290 300 VSDGINTRDG AQLLVESNQF VDSKKALYST DDGYAVSNDN DFGDSENTAE EGTLTSMPYD 310 320 YTLLGSANVK AAVVGTAGQT LTF

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ276331 Genomic DNA. Translation: CAC33162.1.
3D structure databases
HSSP	HSSP built from PDB template 1JRG based on UniProtKB P29155.
ProteinModelPortal	Q9C2Z0.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG3866.
Family and domain databases
Gene3D	2.160.20.10. 1 hit.
InterPro	IPR002022. Amb_allergen_dom. IPR012334. Pectin_lyas_fold. IPR011050. Pectin_lyase_fold/virulence. [Graphical view]
Pfam	PF00544. Pec_lyase_C. 1 hit. [Graphical view]
SMART	SM00656. Amb_all. 1 hit. [Graphical view]
SUPFAM	SSF51126. Pectin_lyas_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLYA_ASPNG

Accession

Primary (citable) accession number: Q9C2Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program