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P26214

- PGLR2_ASPNG

UniProt

P26214 - PGLR2_ASPNG

Protein

Endopolygalacturonase II

Gene

pgaII

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    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 Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 276Sequence AnalysisPRO_0000024770
    Chaini28 – 362335Endopolygalacturonase IIPRO_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

    1
    362
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26214.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

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

    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...
    MobiDBi 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: October 1, 2014
    This is version 91 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