Reviewed, UniProtKB/Swiss-Prot Q59671 (PEL_PSEFL)

Names and origin

Protein names

Recommended name:
    Pectate lyase
      Short name=PL
    EC=4.2.2.2

Gene names

Name:

pel

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Plays a role in bacterial invasion of plants.
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 By similarity.
Pathway	Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
Subcellular location	Secreted.
Sequence similarities	Belongs to the polysaccharide lyase 1 family.

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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 380	352	Pectate lyase		PRO_0000024860
Sites
	Active site	265	1	Potential
	Metal binding	170	1	Calcium By similarity
	Metal binding	209	1	Calcium By similarity
	Metal binding	213	1	Calcium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59671-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: ACDA387D0BC5DD95	FASTA	380	40,624
	10 20 30 40 50 60 MTNPSTFTAS KLASAVIGAL LLSSVPAHAA DIWLDSATTG WATQNGGTKG GSRAAANNIY 70 80 90 100 110 120 TAKNAAELKT ALKASVGANG RIIKITGIID ISEGKAYTTT ADMKVRGRLD IPGKTTIVGT 130 140 150 160 170 180 TSNAEIREGF LYAKENDVII RNITIENPWD PEPKWDPTDG SAGNWNSEYD GLTIEGANNV 190 200 210 220 230 240 WVDHVTFTDG RRTDDQNGTA NGRPKQHHDG ALDVKNGANY VTISYSAFKS HEKNNLIGSS 250 260 270 280 290 300 DSRTTDDGKL KVTIHNTLFE NISARAPRVR FGQVHLYNNY HVGSTSHKVY PFSYAHGMGK 310 320 330 340 350 360 NSKIFSERNA FEISGISGCD KIAGDYGGNV YRDTGSTVNG TALTCPWSTN IGWTPPYSYT 370 380 PLAADKVAAD VKAKAGAGKL

References

[1]

"Cloning of a pectate lyase gene from Xanthomonas campestris pv. malvacearum and comparison of its sequence relationship with pel genes of soft-rot Erwinia and Pseudomonas." Liao C.H., Gaffney T.D., Bradley S.P., Wong L.C. Mol. Plant Microbe Interact. 9:14-21(1996) [PubMed: 8589419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CY091 / Biovar 2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L38902 Genomic DNA. Translation: AAB46399.1. L41673 Genomic DNA. Translation: AAA93535.1.
3D structure databases
HSSP	HSSP built from PDB template 1JRG based on UniProtKB P29155.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Enzyme and pathway databases
BRENDA	4.2.2.2. 329.
Family and domain databases
InterPro	IPR002022. Amb_allergen. IPR006626. PbH1. IPR012334. Pectin_lyas_fold. [Graphical view]
Gene3D	G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
Pfam	PF00544. Pec_lyase_C. 1 hit. [Graphical view]
SMART	SM00656. Amb_all. 1 hit. SM00710. PbH1. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PEL_PSEFL

Accession

Primary (citable) accession number: Q59671
Secondary accession number(s): Q51784

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	September 22, 2009
This is version 53 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)