Reviewed, UniProtKB/Swiss-Prot P26509 (PGLR2_PECCC)

Names and origin

Protein names

Recommended name:
    Endo-polygalacturonase
    EC=3.2.1.15

Gene names

Name:

pehA

Organism

Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora)

Taxonomic identifier

555 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	402 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	Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 28 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	polygalacturonase 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 – 23

23

Chain

24 – 402

379

Endo-polygalacturonase

PRO_0000024759

Sites

Active site

249

1

Proton donor By similarity

Active site

277

1

Probable

Amino acid modifications

Disulfide bond

41 ↔ 62

Disulfide bond

115 ↔ 125

Secondary structure

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402

Helix Strand Turn

Details...

Beta strand

40 – 45

6

Beta strand

48 – 50

3

Helix

52 – 59

8

Beta strand

67 – 71

5

Beta strand

73 – 81

9

Beta strand

90 – 93

4

Beta strand

98 – 101

4

Helix

106 – 108

3

Beta strand

109 – 111

3

Beta strand

118 – 120

3

Beta strand

128 – 133

6

Beta strand

138 – 140

3

Beta strand

142 – 146

5

Beta strand

154 – 158

5

Helix

162 – 170

9

Beta strand

179 – 184

6

Beta strand

186 – 196

11

Beta strand

202 – 207

6

Beta strand

209 – 219

11

Beta strand

229 – 234

6

Beta strand

236 – 242

7

Beta strand

244 – 246

3

Beta strand

251 – 256

6

Beta strand

263 – 273

11

Beta strand

275 – 277

3

Beta strand

279 – 300

22

Beta strand

302 – 308

7

Turn

311 – 313

3

Beta strand

316 – 329

14

Beta strand

331 – 337

7

Beta strand

350 – 361

12

Beta strand

366 – 370

5

Beta strand

378 – 386

9

Beta strand

392 – 401

10

Sequences

	Sequence		Length	Mass (Da)
	P26509-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: C1902D8C5388B6B5	FASTA	402	42,853
	10 20 30 40 50 60 MEYQSGKRVL SLSLGLIGLF SASAWASDSR TVSEPKTPSS CTTLKADSST ATSTIQKALN 70 80 90 100 110 120 NCDQGKAVRL SAGSTSVFLS GPLSLPSGVS LLIDKGVTLR AVNNAKSFEN APSSCGVVDK 130 140 150 160 170 180 NGKGCDAFIT AVSTTNSGIY GPGTIDGQGG VKLQDKKVSW WELAADAKVK KLKQNTPRLI 190 200 210 220 230 240 QINKSKNFTL YNVSLINSPN FHVVFSDGDG FTAWKTTIKT PSTARNTDGI DPMSSKNITI 250 260 270 280 290 300 AYSNIATGDD NVAIKAYKGR AETRNISILH NDFGTGHGMS IGSETMGVYN VTVDDLKMNG 310 320 330 340 350 360 TTNGLRIKSD KSAAGVVNGV RYSNVVMKNV AKPIVIDTVY EKKEGSNVPD WSDITFKDVT 370 380 390 400 SETKGVVVLN GENAKKPIEV TMKNVKLTSD STWQIKNVNV KK

References

[1]	"Structural analysis of the pehA gene and characterization of its protein product, endopolygalacturonase, of Erwinia carotovora subspecies carotovora." Saarilahti H.T., Heino P., Pakkanen R., Kalkkinen N., Palva I., Palva E.T. Mol. Microbiol. 4:1037-1044(1990) [PubMed: 2215212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SCC3193.
[2]	"Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora." Pickersgill R., Smith D., Worboys K., Jenkins J. J. Biol. Chem. 273:24660-24664(1998) [PubMed: 9733763] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51701 Genomic DNA. Translation: CAA35998.1.

PIR

S11772.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BHE	X-ray	1.90	A	27-402	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH28. Glycoside Hydrolase Family 28.

Enzyme and pathway databases

BRENDA

3.2.1.15. 290410.

Family and domain databases

InterPro

IPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.

Pfam

PF00295. Glyco_hydro_28. 1 hit.
[Graphical view]

SMART

SM00710. PbH1. 5 hits.
[Graphical view]

PROSITE

PS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PGLR2_PECCC

Accession

Primary (citable) accession number: P26509

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	January 19, 2010
This is version 68 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)