Pectate lyase A precursor - Erwinia chrysanthemi

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Reviewed, UniProtKB/Swiss-Prot P0C1A2 (PELA_ERWCH)

Last modified November 24, 2009. Version 22. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Pectate lyase A
EC=4.2.2.2

Gene names

Name:

pelA

Organism

Erwinia chrysanthemi

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	393 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	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.
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. PLADES subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Lyase
PTM	Disulfide bond
Technical term	3D-structure
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

32

Potential

Chain

361

Pectate lyase A

PRO_0000024852

Sites

Active site

1

Potential

Metal binding

1

Calcium By similarity

Metal binding

1

Calcium By similarity

Metal binding

1

Calcium By similarity

Metal binding

1

Calcium By similarity

Amino acid modifications

Disulfide bond

Secondary structure

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393

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P0C1A2-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 20025C904FD7B345
Show »

393

42,080

        10         20         30         40         50         60 
MMNKASGRSF TRSSKYLLAT LIAGMMASGV SAAELVSDKA LESAPTVGWA SQNGFTTGGA 

        70         80         90        100        110        120 
AATSDNIYIV TNISEFTSAL SAGAEAKIIQ IKGTIDISGG TPYTDFADQK ARSQINIPAN 

       130        140        150        160        170        180 
TTVIGLGTDA KFINGSLIID GTDGTNNVII RNVYIQTPID VEPHYEKGDG WNAEWDAMNI 

       190        200        210        220        230        240 
TNGAHHVWID HVTISDGNFT DDMYTTKDGE TYVQHDGALD IKRGSDYVTI SNSLIDQHDK 

       250        260        270        280        290        300 
TMLIGHNDTN SAQDKGKLHV TLFNNVFNRV TERAPRVRYG SIHSFNNVFK GDAKDPVYRY 

       310        320        330        340        350        360 
QYSFGIGTSG SVLSEGNSFT IANLSASKAC KVVKKFNGSI FSDNGSVLNG SAVDLSGCGF 

       370        380        390 
SAYTSKIPYI YDVQPMTTEL AQSITDNAGS GKL

References

[1]	"Structure and organization of the pel genes from Erwinia chrysanthemi EC16." Tamaki S.J., Gold S., Robeson M., Manulis S., Keen N.T. J. Bacteriol. 170:3468-3478(1988) [PubMed: 3042750] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EC16.
[2]	"Structure of pectate lyase A: comparison to other isoforms." Thomas L.M., Doan C.N., Oliver R.L., Yoder M.D. Acta Crystallogr. D 58:1008-1015(2002) [PubMed: 12037303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-393.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14509 Genomic DNA. Translation: AAA24843.1.

PIR

WZWC6A. B31091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JRG	X-ray	2.10	A/B	33-393	[»]
1JTA	X-ray	1.80	A	33-393	[»]
1OOC	X-ray	2.94	A/B	33-393	[»]
1PE9	X-ray	1.60	A/B	33-393	[»]

ModBase

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.
IPR011050. Pectin_lyase_fold/virulence.
[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

Entry information

Entry name

PELA_ERWCH

Accession

Primary (citable) accession number: P0C1A2
Secondary accession number(s): P29155

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	April 18, 2006
Last modified:	November 24, 2009
This is version 22 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents