Reviewed, UniProtKB/Swiss-Prot P04959 (PELB_ERWCH)

Names and origin

Protein names

Recommended name:
    Pectate lyase B
    EC=4.2.2.2

Gene names

Name:

pelB

Organism

Erwinia chrysanthemi

Taxonomic identifier

556 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	375 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	Involved in maceration and soft-rotting of plant tissue.
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-gluconic acid from pectin: step 2/5.
Subcellular location	Secreted.
Sequence similarities	Belongs to the polysaccharide lyase 1 family. PLADES subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Disulfide bond
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 – 22	22
	Chain	23 – 375	353	Pectate lyase B		PRO_0000024853
Sites
	Active site	240	1	Potential
	Metal binding	150	1	Calcium By similarity
	Metal binding	152	1	Calcium By similarity
	Metal binding	187	1	Calcium By similarity
	Metal binding	191	1	Calcium By similarity
Amino acid modifications
	Disulfide bond	93 ↔ 176		By similarity
	Disulfide bond	351 ↔ 374		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P04959-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: F3FE75D507B8F883	FASTA	375	40,234
	10 20 30 40 50 60 MKSLITPIAA GLLLAFSQYS LAADTGGYTK TDGGDVSGAV KKTASSMQDI VNIIEAAKVD 70 80 90 100 110 120 ANGKKVKGGA YPLVITYTGN EDSLINAAAA NICGQWSKDA RGVEIKDFTK GLTIIGANGS 130 140 150 160 170 180 SANFGIWIVN SSDIVVRNMR IGYLPGGAQD GDMFRIDNSP NVWLDHNELF AANHECDGTK 190 200 210 220 230 240 DGDTTFESAI DIKKGATYVT ISYNYIHGVK KVGLSGFSSS DTAERNITYH HNIYSDVNAR 250 260 270 280 290 300 LPLQRGGNVH AYNNLYTGIT SSGLNVRQNG KALIENNWFE NAVSPVTSRY DGSNFGTWVL 310 320 330 340 350 360 KGNNITKPAD FATYNITWTP DTKEYRNADT WTSTGTYPTV PYSYSPVSAQ CVKDKLANYA 370 GVGKNLATLA SSACK

References

[1]	"Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high-level expression in Escherichia coli." Keen N.T., Tamaki S. J. Bacteriol. 168:595-606(1986) [PubMed: 3536853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EC16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M14510 Genomic DNA. Translation: AAA24847.1.
PIR	WZWCPB. B25158.
3D structure databases
HSSP	HSSP built from PDB template 1AIR based on UniProtKB P11073.
SMR	P04959. Positions 22-374.
ModBase	Search...
Protein family/group databases
CAZy	PL1. Polysaccharide Lyase Family 1.
Enzyme and pathway databases
BRENDA	4.2.2.2. 1459.
Family and domain databases
InterPro	IPR002022. Amb_allergen. 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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PELB_ERWCH

Accession

Primary (citable) accession number: P04959

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	June 16, 2009
This is version 61 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)