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Protein

Endopolygalacturonase II

Gene

pgaII

Organism
Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
Status
Reviewed-Annotation score: -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 Publication1
Active sitei2231 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCell 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
ORF Names:ASPNIDRAFT_182156
OrganismiAspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)
Taxonomic identifieri380704 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000009038 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 – 271 Publication6
ChainiPRO_000002477128 – 362Endopolygalacturonase IIAdd BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 45Combined sources1 Publication
Disulfide bondi203 ↔ 219Combined sources1 Publication
GlycosylationiCAR_000232240N-linked (GlcNAc...) (high mannose) asparagine2 Publications1
Disulfide bondi329 ↔ 334Combined sources1 Publication
Disulfide bondi353 ↔ 362Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

PTM databases

GlyConnecti126
UniCarbKBiP26214

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 1Sequence analysisAdd BLAST31
Repeati209 – 229PbH1 2Sequence analysisAdd BLAST21
Repeati238 – 259PbH1 3Sequence analysisAdd BLAST22
Repeati267 – 289PbH1 4Sequence analysisAdd BLAST23
Repeati301 – 322PbH1 5Sequence analysisAdd BLAST22

Sequence similaritiesi

Belongs to the glycosyl hydrolase 28 family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5434 LUCA
OrthoDBiEOG092C33Y3

Family and domain databases

Gene3Di2.160.20.10, 1 hit
InterProiView protein in InterPro
IPR000743 Glyco_hydro_28
IPR006626 PbH1
IPR012334 Pectin_lyas_fold
IPR011050 Pectin_lyase_fold/virulence
PfamiView protein in Pfam
PF00295 Glyco_hydro_28, 1 hit
SMARTiView protein in SMART
SM00710 PbH1, 5 hits
SUPFAMiSSF51126 SSF51126, 1 hit
PROSITEiView protein in PROSITE
PS00502 POLYGALACTURONASE, 1 hit

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
ACJE01000008 Genomic DNA Translation: EHA24775.1
PIRiS12895

Genome annotation databases

EnsemblFungiiEHA24775; EHA24775; ASPNIDRAFT_182156

Similar proteinsi

Entry informationi

Entry nameiPGLR2_ASPNA
AccessioniPrimary (citable) accession number: P26214
Secondary accession number(s): G3XYE5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 25, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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