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Protein

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Gene

PNG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. Involved in the formation of free oligosaccharide in cytosol.6 Publications

Catalytic activityi

Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by Z-VAD-fmk, a well-known caspase inhibitor. Also inhibited by Man9GlcNAc2-iodoacetoamide. Both molecules inhibit enzyme activity through covalent binding of the carbohydrate to the single Cys-191 residue.3 Publications

Kineticsi

  1. KM=210 µM for asialofetuin1 Publication
  1. Vmax=140 nmol/min/mg enzyme with asialofetuin as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi129Zinc1
Metal bindingi132Zinc1
Metal bindingi165Zinc1
Metal bindingi168Zinc1
Active sitei191Nucleophile1
Active sitei2181
Active sitei2351
Binding sitei238Substrate1

GO - Molecular functioni

GO - Biological processi

  • glycoprotein catabolic process Source: GO_Central
  • glycoprotein ERAD pathway Source: SGD
  • misfolded or incompletely synthesized protein catabolic process Source: SGD
  • protein deglycosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YPL096W-MONOMER.
BRENDAi3.5.1.52. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Alternative name(s):
Peptide:N-glycanase 1
Short name:
yPNG1
Gene namesi
Name:PNG1
Ordered Locus Names:YPL096W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL096W.
SGDiS000006017. PNG1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123W → A: No effect. 1 Publication1
Mutagenesisi129C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi132C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi165C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi168C → A or S: Abolishes enzyme activity. 1 Publication1
Mutagenesisi174F → A: No effect. 1 Publication1
Mutagenesisi177Y → A: No effect. 1 Publication1
Mutagenesisi187R → A: No effect. 1 Publication1
Mutagenesisi189G → A: No effect. 1 Publication1
Mutagenesisi191C → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi194W → A: No effect. 1 Publication1
Mutagenesisi198F → A: No effect. 1 Publication1
Mutagenesisi199T → A: No effect. 1 Publication1
Mutagenesisi203K → A: No effect. 1 Publication1
Mutagenesisi206G → A: No effect. 1 Publication1
Mutagenesisi210R → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi212V → A: No effect. 1 Publication1
Mutagenesisi218H → A: Abolishes enzyme activity. 2 Publications1
Mutagenesisi218H → Y in png1-1; abolishes enzyme activity. 2 Publications1
Mutagenesisi220W → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi220W → F: No effect. 1 Publication1
Mutagenesisi222E → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi224F → A: No effect. 1 Publication1
Mutagenesisi230R → A: No effect. 1 Publication1
Mutagenesisi231W → A: Abolishes enzyme activity. 1
Mutagenesisi231W → F: No effect. 1
Mutagenesisi234V → A: No effect. 1 Publication1
Mutagenesisi235D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi242D → A: No effect. 1 Publication1
Mutagenesisi251W → A: No effect. 1 Publication1
Mutagenesisi253K → A: No effect. 1 Publication1
Mutagenesisi257Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi261F → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi264D → A: No effect. 1 Publication1
Mutagenesisi266V → A: No effect. 1 Publication1
Mutagenesisi268D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi273Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi281R → A: No effect. 1 Publication1
Mutagenesisi347R → A: No effect. 1 Publication1
Mutagenesisi354W → A: No effect. 1 Publication1
Mutagenesisi358R → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002489961 – 363Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidaseAdd BLAST363

Proteomic databases

MaxQBiQ02890.
PRIDEiQ02890.

Interactioni

Subunit structurei

Interacts with RAD23 subunit of 26S proteasome.3 Publications

Protein-protein interaction databases

BioGridi36085. 20 interactors.
DIPiDIP-4008N.
IntActiQ02890. 2 interactors.
MINTiMINT-574235.

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 30Combined sources18
Beta strandi31 – 33Combined sources3
Helixi36 – 48Combined sources13
Helixi50 – 65Combined sources16
Helixi69 – 78Combined sources10
Helixi81 – 94Combined sources14
Beta strandi97 – 100Combined sources4
Helixi103 – 118Combined sources16
Beta strandi130 – 132Combined sources3
Beta strandi138 – 146Combined sources9
Helixi151 – 153Combined sources3
Beta strandi154 – 165Combined sources12
Turni166 – 168Combined sources3
Beta strandi171 – 177Combined sources7
Helixi180 – 186Combined sources7
Helixi191 – 203Combined sources13
Turni204 – 206Combined sources3
Beta strandi209 – 214Combined sources6
Turni215 – 217Combined sources3
Beta strandi218 – 225Combined sources8
Turni226 – 229Combined sources4
Beta strandi230 – 235Combined sources6
Turni236 – 239Combined sources4
Beta strandi240 – 242Combined sources3
Helixi246 – 250Combined sources5
Beta strandi258 – 262Combined sources5
Beta strandi265 – 268Combined sources4
Helixi270 – 273Combined sources4
Beta strandi275 – 278Combined sources4
Helixi286 – 301Combined sources16
Helixi306 – 324Combined sources19
Beta strandi325 – 327Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3WX-ray3.00A8-342[»]
1X3ZX-ray2.80A8-342[»]
3ESWX-ray3.40A8-341[»]
ProteinModelPortaliQ02890.
SMRiQ02890.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02890.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000006540.
HOGENOMiHOG000183313.
InParanoidiQ02890.
KOiK01456.
OMAiNREDHVW.
OrthoDBiEOG092C0W7W.

Family and domain databases

InterProiIPR018325. Rad4/PNGase_transGLS-fold.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM00460. TGc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEVYEKNNI DFDSIAKMLL IKYKDFILSK FKKAAPVENI RFQNLVHTNQ
60 70 80 90 100
FAQGVLGQSQ HLCTVYDNPS WHSIVLETLD LDLIYKNVDK EFAKDGHAEG
110 120 130 140 150
ENIYTDYLVK ELLRYFKQDF FKWCNKPDCN HCGQNTSENM TPLGSQGPNG
160 170 180 190 200
EESKFNCGTV EIYKCNRCGN ITRFPRYNDP IKLLETRKGR CGEWCNLFTL
210 220 230 240 250
ILKSFGLDVR YVWNREDHVW CEYFSNFLNR WVHVDSCEQS FDQPYIYSIN
260 270 280 290 300
WNKKMSYCIA FGKDGVVDVS KRYILQNELP RDQIKEEDLK FLCQFITKRL
310 320 330 340 350
RYSLNDDEIY QLACRDEQEQ IELIRGKTQE TKSESVSAAS KSSNRGRESG
360
SADWKAQRGE DGK
Length:363
Mass (Da):42,485
Last modified:November 1, 1996 - v1
Checksum:i004F3E3E07C3B954
GO

Mass spectrometryi

Molecular mass is 43208 Da from positions 1 - 363. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68203.1.
BK006949 Genomic DNA. Translation: DAA11337.1.
PIRiS61970.
RefSeqiNP_015229.1. NM_001183910.1.

Genome annotation databases

EnsemblFungiiYPL096W; YPL096W; YPL096W.
GeneIDi856009.
KEGGisce:YPL096W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43281 Genomic DNA. Translation: AAB68203.1.
BK006949 Genomic DNA. Translation: DAA11337.1.
PIRiS61970.
RefSeqiNP_015229.1. NM_001183910.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X3WX-ray3.00A8-342[»]
1X3ZX-ray2.80A8-342[»]
3ESWX-ray3.40A8-341[»]
ProteinModelPortaliQ02890.
SMRiQ02890.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36085. 20 interactors.
DIPiDIP-4008N.
IntActiQ02890. 2 interactors.
MINTiMINT-574235.

Proteomic databases

MaxQBiQ02890.
PRIDEiQ02890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL096W; YPL096W; YPL096W.
GeneIDi856009.
KEGGisce:YPL096W.

Organism-specific databases

EuPathDBiFungiDB:YPL096W.
SGDiS000006017. PNG1.

Phylogenomic databases

GeneTreeiENSGT00390000006540.
HOGENOMiHOG000183313.
InParanoidiQ02890.
KOiK01456.
OMAiNREDHVW.
OrthoDBiEOG092C0W7W.

Enzyme and pathway databases

BioCyciYEAST:YPL096W-MONOMER.
BRENDAi3.5.1.52. 984.

Miscellaneous databases

EvolutionaryTraceiQ02890.
PROiQ02890.

Family and domain databases

InterProiIPR018325. Rad4/PNGase_transGLS-fold.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPNG1_YEAST
AccessioniPrimary (citable) accession number: Q02890
Secondary accession number(s): D6W3S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4850 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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.