SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P26214

- PGLR2_ASPNG

UniProt

P26214 - PGLR2_ASPNG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Endopolygalacturonase II
Gene
pgaII, pg2
Organism
Aspergillus niger
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei201 – 2011Proton donor
Active sitei223 – 2231

GO - Molecular functioni

  1. polygalacturonase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

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

Secreted Inferred

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication
Mutagenesisi201 – 2011D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication
Mutagenesisi202 – 2021D → E: Reduces activity by 99.4%. No effect on Km for substrate. 1 Publication
Mutagenesisi202 – 2021D → N: Reduces activity by 99.9%. No effect on Km for substrate. 1 Publication
Mutagenesisi223 – 2231H → A: Reduces activity by 99.5%. No effect on Km for substrate. 1 Publication
Mutagenesisi256 – 2561R → N: Reduces activity by 86%. Reduces Km for substrate 10-fold. 1 Publication
Mutagenesisi258 – 2581K → N: Reduces activity by 99.2%. Reduces Km for substrate 10-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Propeptidei22 – 276 Reviewed prediction
PRO_0000024770
Chaini28 – 362335Endopolygalacturonase II
PRO_0000024771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 45
Disulfide bondi203 ↔ 219
Glycosylationi240 – 2401N-linked (GlcNAc...) (high mannose)
CAR_000232
Disulfide bondi329 ↔ 334
Disulfide bondi353 ↔ 362

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

PTM databases

UniCarbKBiP26214.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 346
Helixi35 – 417
Helixi42 – 443
Beta strandi46 – 527
Beta strandi61 – 633
Beta strandi71 – 8010
Beta strandi89 – 968
Beta strandi98 – 1014
Beta strandi106 – 1083
Helixi111 – 1133
Beta strandi121 – 1233
Beta strandi129 – 1357
Beta strandi137 – 1415
Beta strandi143 – 1453
Beta strandi152 – 1554
Beta strandi157 – 1637
Beta strandi165 – 1673
Helixi169 – 1724
Turni173 – 1753
Beta strandi181 – 1844
Beta strandi188 – 1947
Beta strandi196 – 1983
Beta strandi203 – 21614
Beta strandi218 – 2225
Beta strandi225 – 2306
Beta strandi232 – 2343
Beta strandi237 – 26024
Beta strandi265 – 29228
Beta strandi302 – 31817
Beta strandi322 – 3287
Turni331 – 3333
Beta strandi334 – 34815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZFX-ray1.68A/B1-362[»]
ProteinModelPortaliP26214.
SMRiP26214. Positions 28-362.

Miscellaneous databases

EvolutionaryTraceiP26214.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati156 – 18631PbH1 1
Add
BLAST
Repeati209 – 22921PbH1 2
Add
BLAST
Repeati238 – 25922PbH1 3
Add
BLAST
Repeati267 – 28923PbH1 4
Add
BLAST
Repeati301 – 32222PbH1 5
Add
BLAST

Sequence similaritiesi

Contains 5 PbH1 repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG5434.

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

MHSFASLLAY GLVAGATFAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL    50
NNIEVPAGTT LDLTGLTSGT KVIFEGTTTF QYEEWAGPLI SMSGEHITVT 100
GASGHLINCD GARWWDGKGT SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM 150
AFSVQANDIT FTDVTINNAD GDTQGGHNTD AFDVGNSVGV NIIKPWVHNQ 200
DDCLAVNSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN VTIEHSTVSN 250
SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP 300
TNGVTIQDVK LESVTGSVDS GATEIYLLCG SGSCSDWTWD DVKVTGGKKS 350
TACKNFPSVA SC 362
Length:362
Mass (Da):37,684
Last modified:May 1, 1992 - v1
Checksum:i952A79F612BC8000
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58893 Genomic DNA. Translation: CAA41694.1.
PIRiS12895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58893 Genomic DNA. Translation: CAA41694.1 .
PIRi S12895.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CZF X-ray 1.68 A/B 1-362 [» ]
ProteinModelPortali P26214.
SMRi P26214. Positions 28-362.
ModBasei Search...

Protein family/group databases

CAZyi GH28. Glycoside Hydrolase Family 28.
mycoCLAPi PGA28II_ASPNG.

PTM databases

UniCarbKBi P26214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5434.

Enzyme and pathway databases

SABIO-RK P26214.

Miscellaneous databases

EvolutionaryTracei P26214.

Family and domain databases

Gene3Di 2.160.20.10. 1 hit.
InterProi IPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view ]
Pfami PF00295. Glyco_hydro_28. 1 hit.
[Graphical view ]
SMARTi SM00710. PbH1. 5 hits.
[Graphical view ]
SUPFAMi SSF51126. SSF51126. 1 hit.
PROSITEi PS00502. POLYGALACTURONASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning, nucleotide sequence and expression of the gene encoding prepro-polygalacturonase II of Aspergillus niger."
    Bussink H.J.D., Kester H.C.M., Visser J.
    FEBS Lett. 273:127-130(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-40 AND 151-161.
    Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
  2. "Identification of the glycosylation site and glycan structures of recombinant endopolygalacturonase II by mass spectrometry."
    Yang Y., Bergmann C., Benen J., Orlando R.
    Rapid Commun. Mass Spectrom. 11:1257-1262(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATE ON ASN-240, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis."
    van Santen Y., Benen J.A.E., Schroeter K.-H., Kalk K.H., Armand S., Visser J., Dijkstra B.W.
    J. Biol. Chem. 274:30474-30480(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), MUTAGENESIS OF ASP-180; ASP-201; ASP-202; HIS-223; ARG-256 AND LYS-258.

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: April 16, 2014
This is version 90 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

External Data

Dasty 3

Similar proteinsi