Reviewed, UniProtKB/Swiss-Prot Q9X6Z2 (PELA_PAEBA)

Names and origin

Protein names

Recommended name:
    Pectate lyase A
    EC=4.2.2.2
Alternative name(s):
    Pectin lyase
    EC=4.2.2.10

Gene names

Name:

pelA

Organism

Paenibacillus barcinonensis

Taxonomic identifier

198119 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	222 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	Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is not able to cleave trigalacturonate. Does not degrade xylans and carboxymethylcellulose (CMC). Ref.1 Ref.2
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. 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.
Cofactor	Binds 1 calcium ion per subunit. Ref.1 Ref.2
Enzyme regulation	Strongly inhibited by Ba2+. To a lesser extent, is also inhibited by Sn2+, Mg2+ and Ag+. Inhibited by EDTA in vitro. Ref.1
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconic acid from pectin: step 2/5.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the polysaccharide lyase 3 family.
biophysicochemical properties	Kinetic parameters: Vmax=102.4 µmol/min/mg enzyme with 22% esterified pectin as substrate Vmax=95.4 µmol/min/mg enzyme with polygalacturonic acid as substrate pH dependence: Optimum pH is 10. Is stable for 1 hour at 40 degrees Celsius in the pH range 4.0-8.0. Temperature dependence: Optimum temperature is 50-55 degrees Celsius. More than 50% of maximum activity is found in the temperature range 40-60 degrees Celsius. Retains more than 50% of the initial activity after 4 hours incubation at 40 degrees Celsius at pH 10, while at 50 degrees Celsius only 1% of the initial activity is found after the same treatment.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW pectate lyase activity Inferred from electronic annotation. Source: EC pectin lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 222	197	Pectate lyase A		PRO_5000065163

Sequences

	Sequence		Length	Mass (Da)
	Q9X6Z2-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 7F29F585791C9682	FASTA	222	23,233
	10 20 30 40 50 60 MKKMLTLLLS AGLVASIFGV MPAAAAPTVV NSTIVVPKGT TYDGQGKTFV ANPSTLGDGS 70 80 90 100 110 120 QAENQKPVFR LEAGATLKNV IIGAPAADGV HCYGSCNISN VVWEDVGEDA LTLKSSGTVN 130 140 150 160 170 180 ITGGAAYKAY DKVFQMNASG TINIKNFRAD DIGKLVRQNG GTSYAVNMTL DNSNISNVKD 190 200 210 220 SIMRTDSSVS QGKITNTRYS KVPTLFKGFA SGKTSQSGNT QY

References

[1]	"An unusual pectate lyase from a Bacillus sp. with high activity on pectin: cloning and characterization." Soriano M., Blanco A., Diaz P., Pastor F.I.J. Microbiology 146:89-95(2000) [PubMed: 10658655] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 15478 / CECT 7022 / BP-23.
[2]	"Pectate lyase C from Bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin." Soriano M., Diaz P., Pastor F.I.J. Microbiology 152:617-625(2006) [PubMed: 16514142] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ237980 Genomic DNA. Translation: CAB40884.1.
3D structure databases
HSSP	HSSP built from PDB template 1EE6 based on UniProtKB Q9RHW0.
ModBase	Search...
Protein family/group databases
CAZy	PL3. Polysaccharide Lyase Family 3.
Enzyme and pathway databases
BRENDA	4.2.2.2. 1000.
Family and domain databases
InterPro	IPR004898. Pectate_lyase_cat. IPR012334. Pectin_lyas_fold. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF03211. Pectate_lyase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PELA_PAEBA

Accession

Primary (citable) accession number: Q9X6Z2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)