PNG1_KLULA
ID PNG1_KLULA Reviewed; 353 AA.
AC Q6CLZ6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE EC=3.5.1.52;
DE AltName: Full=Peptide:N-glycanase 1;
GN Name=PNG1; OrderedLocusNames=KLLA0E24266g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC glycoproteins in the cytoplasm and assists their proteasome-mediated
CC degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the
CC glycan and the amide side chain of Asn, converting Asn to Asp. Prefers
CC proteins containing high-mannose over those bearing complex type
CC oligosaccharides. Can recognize misfolded proteins in the endoplasmic
CC reticulum that are exported to the cytosol to be destroyed and
CC deglycosylate them, while it has no activity toward native proteins.
CC Deglycosylation is a prerequisite for subsequent proteasome-mediated
CC degradation of some, but not all, misfolded glycoproteins (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000305}.
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DR EMBL; CR382125; CAH00130.1; -; Genomic_DNA.
DR RefSeq; XP_455043.1; XM_455043.1.
DR AlphaFoldDB; Q6CLZ6; -.
DR SMR; Q6CLZ6; -.
DR STRING; 28985.XP_455043.1; -.
DR EnsemblFungi; CAH00130; CAH00130; KLLA0_E24223g.
DR GeneID; 2894341; -.
DR KEGG; kla:KLLA0_E24223g; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_031058_0_1_1; -.
DR InParanoid; Q6CLZ6; -.
DR OMA; WIHVDAC; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0120125; C:PNGase complex; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0035977; P:protein deglycosylation involved in glycoprotein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IEA:EnsemblFungi.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..353
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248992"
FT REGION 316..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 353 AA; 41408 MW; F7BBD091FEF8C130 CRC64;
MTDFQETLSS VSKRFLELYR SKILSQWRGT NGSSEEEKRF NSLIQQNGFA RQIFGLYKSL
CFRYENDAWY SVVLDILDLD LIYSNVDKAV QDNNASDIEY QDYLVKELLR YFKRDFFSWC
NKPNCSKCGT DEHLEWVGTD RANSEEAKYQ CGNVEVYRCT LTGDITRFPR YNDPIKLLQT
RTGRCGEWCN VFTLILKSFG LNARYIWNKE DHVWCEYYSP NLKRWVHLDC CEQSFDEPHI
YSKNWNKKMS YVLAFSNDIV ADVSGRYILQ NNLPRNAISE NELNFMCTYL TKTLRKDFND
DQIYALACRD EQERLSLEKT KPSKDTSTTT LTGTKGRESG STAWKQQRGE DGS
