Reviewed, UniProtKB/Swiss-Prot P26213 (PGLR1_ASPNG)

Names and origin

Protein names

Recommended name:
    Polygalacturonase-1
    EC=3.2.1.15
Alternative name(s):
    Polygalacturonase I
      Short name=PG-I
    Pectinase 1

Gene names

Name:	pgaA
Synonyms:	pgaI

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	368 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. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Catalytic activity	Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the glycosyl hydrolase 28 family. Contains 6 PbH1 repeats.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro 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 – 18

18

Potential

Propeptide

19 – 31

13

Potential

PRO_0000024768

Chain

32 – 368

337

Polygalacturonase-1

PRO_0000024769

Sites

Active site

207

1

Proton donor By similarity

Active site

229

1

Probable

Amino acid modifications

Glycosylation

44

1

O-linked (Man) Ref.2

Glycosylation

46

1

O-linked (Man) Ref.2

Glycosylation

246

1

N-linked (GlcNAc...) Probable

Disulfide bond

35 ↔ 50

Disulfide bond

209 ↔ 225

Disulfide bond

335 ↔ 340

Disulfide bond

359 ↔ 368

Secondary structure

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368

Helix Strand Turn

Details...

Beta strand

35 – 39

5

Helix

40 – 46

7

Helix

47 – 49

3

Beta strand

51 – 57

7

Beta strand

76 – 85

10

Beta strand

94 – 96

3

Beta strand

99 – 101

3

Beta strand

103 – 106

4

Beta strand

111 – 113

3

Helix

116 – 118

3

Turn

124 – 126

3

Beta strand

127 – 129

3

Beta strand

135 – 147

13

Beta strand

149 – 151

3

Beta strand

158 – 169

12

Beta strand

171 – 173

3

Helix

177 – 180

4

Beta strand

187 – 190

4

Beta strand

194 – 200

7

Beta strand

202 – 222

21

Beta strand

224 – 240

17

Beta strand

243 – 256

14

Beta strand

258 – 266

9

Beta strand

272 – 298

27

Beta strand

308 – 310

3

Beta strand

312 – 324

13

Beta strand

329 – 334

6

Beta strand

340 – 354

15

Sequences

	Sequence		Length	Mass (Da)
	P26213-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: CD9B46A9A99B5102	FASTA	368	38,108
	10 20 30 40 50 60 MHSYQLLGLA AVGSLVSAAP APSRVSEFAK KASTCTFTSA SEASESISSC SDVVLSSIEV 70 80 90 100 110 120 PAGETLDLSD AADGSTITFE GTTSFGYKEW KGPLIRFGGK DLTVTMADGA VIDGDGSRWW 130 140 150 160 170 180 DSKGTNGGKT KPKFMYIHDV EDSTFKGINI KNTPVQAISV QATNVHLNDF TIDNSDGDDN 190 200 210 220 230 240 GGHNTDGFDI SESTGVYISG ATVKNQDDCI AINSGESISF TGGTCSGGHG LSIGSVGGRD 250 260 270 280 290 300 DNTVKNVTIS DSTVSNSANG VRIKTIYKET GDVSEITYSN IQLSGITDYG IVIEQDYENG 310 320 330 340 350 360 SPTGTPSTGI PITDVTVDGV TGTLEDDATQ VYILCGDGSC SDWTWSGVDL SGGKTSDKCE NVPSGASC

References

[1]	"Identification and characterization of a second polygalacturonase gene of Aspergillus niger." Bussink H.J.D., Brouwer K., de Graaff L.H., Kester H.C.M., Visser J. Curr. Genet. 20:301-307(1991) [PubMed: 1934135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-43; 107-117 AND 205-221. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]	"Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger." van Pouderoyen G., Snijder H.J., Benen J.A.E., Dijkstra B.W. FEBS Lett. 554:462-466(2003) [PubMed: 14623112] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-368, GLYCOSYLATION AT SER-44; SER-46 AND ASN-246.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X58892 Genomic DNA. Translation: CAA41693.1.

PIR

S17980.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NHC	X-ray	1.70	A/B/C/D/E/F	33-368	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH28. Glycoside Hydrolase Family 28.

Enzyme and pathway databases

BRENDA

3.2.1.15. 277.

Family and domain databases

InterPro

IPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[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. 6 hits.
[Graphical view]

PROSITE

PS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PGLR1_ASPNG

Accession

Primary (citable) accession number: P26213

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)