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Protein

Endopolygalacturonase II

Gene

pgaII

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei201Proton donor1
Active sitei2231

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BRENDAi3.2.1.15. 518.
SABIO-RKP26214.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28II_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Endopolygalacturonase II (EC:3.2.1.15)
Short name:
EPG-II
Alternative name(s):
Pectinase 2
Polygalacturonase II
Short name:
PG-II
Polygalacturonase X2
Gene namesi
Name:pgaII
Synonyms:pg2
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication1
Mutagenesisi201D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication1
Mutagenesisi202D → E: Reduces activity by 99.4%. No effect on Km for substrate. 1 Publication1
Mutagenesisi202D → N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication1
Mutagenesisi223H → A: Reduces activity by 99.5%. No effect on Km for substrate. 1 Publication1
Mutagenesisi256R → N: Reduces activity by 86%. Reduces Km for substrate 10-fold. 1 Publication1
Mutagenesisi258K → N: Reduces activity by 99.2%. Reduces Km for substrate 10-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002477022 – 27Sequence analysis6
ChainiPRO_000002477128 – 362Endopolygalacturonase IIAdd BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 45
Disulfide bondi203 ↔ 219
GlycosylationiCAR_000232240N-linked (GlcNAc...) (high mannose)1
Disulfide bondi329 ↔ 334
Disulfide bondi353 ↔ 362

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP26214.

PTM databases

UniCarbKBiP26214.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00011984.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Helixi35 – 41Combined sources7
Helixi42 – 44Combined sources3
Beta strandi46 – 52Combined sources7
Beta strandi61 – 63Combined sources3
Beta strandi71 – 80Combined sources10
Beta strandi89 – 96Combined sources8
Beta strandi98 – 101Combined sources4
Beta strandi106 – 108Combined sources3
Helixi111 – 113Combined sources3
Beta strandi121 – 123Combined sources3
Beta strandi129 – 135Combined sources7
Beta strandi137 – 141Combined sources5
Beta strandi143 – 145Combined sources3
Beta strandi152 – 155Combined sources4
Beta strandi157 – 163Combined sources7
Beta strandi165 – 167Combined sources3
Helixi169 – 172Combined sources4
Turni173 – 175Combined sources3
Beta strandi181 – 184Combined sources4
Beta strandi188 – 194Combined sources7
Beta strandi196 – 198Combined sources3
Beta strandi203 – 216Combined sources14
Beta strandi218 – 222Combined sources5
Beta strandi225 – 230Combined sources6
Beta strandi232 – 234Combined sources3
Beta strandi237 – 260Combined sources24
Beta strandi265 – 292Combined sources28
Beta strandi302 – 318Combined sources17
Beta strandi322 – 328Combined sources7
Turni331 – 333Combined sources3
Beta strandi334 – 348Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CZFX-ray1.68A/B1-362[»]
ProteinModelPortaliP26214.
SMRiP26214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati156 – 186PbH1 1Add BLAST31
Repeati209 – 229PbH1 2Add BLAST21
Repeati238 – 259PbH1 3Add BLAST22
Repeati267 – 289PbH1 4Add BLAST23
Repeati301 – 322PbH1 5Add BLAST22

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated
Contains 5 PbH1 repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5434. LUCA.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSFASLLAY GLVAGATFAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL
60 70 80 90 100
NNIEVPAGTT LDLTGLTSGT KVIFEGTTTF QYEEWAGPLI SMSGEHITVT
110 120 130 140 150
GASGHLINCD GARWWDGKGT SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM
160 170 180 190 200
AFSVQANDIT FTDVTINNAD GDTQGGHNTD AFDVGNSVGV NIIKPWVHNQ
210 220 230 240 250
DDCLAVNSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN VTIEHSTVSN
260 270 280 290 300
SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP
310 320 330 340 350
TNGVTIQDVK LESVTGSVDS GATEIYLLCG SGSCSDWTWD DVKVTGGKKS
360
TACKNFPSVA SC
Length:362
Mass (Da):37,684
Last modified:May 1, 1992 - v1
Checksum:i952A79F612BC8000
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58893 Genomic DNA. Translation: CAA41694.1.
PIRiS12895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58893 Genomic DNA. Translation: CAA41694.1.
PIRiS12895.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CZFX-ray1.68A/B1-362[»]
ProteinModelPortaliP26214.
SMRiP26214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00011984.

Protein family/group databases

CAZyiGH28. Glycoside Hydrolase Family 28.
mycoCLAPiPGA28II_ASPNG.

PTM databases

UniCarbKBiP26214.

Proteomic databases

PaxDbiP26214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5434. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.15. 518.
SABIO-RKP26214.

Miscellaneous databases

EvolutionaryTraceiP26214.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTiSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
PROSITEiPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGLR2_ASPNG
AccessioniPrimary (citable) accession number: P26214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.