PNG1_DEBHA
ID PNG1_DEBHA Reviewed; 375 AA.
AC Q6BNI6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=DEHA2E21384g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88507.2; -; Genomic_DNA.
DR RefSeq; XP_460234.2; XM_460234.1.
DR AlphaFoldDB; Q6BNI6; -.
DR SMR; Q6BNI6; -.
DR STRING; 4959.XP_460234.2; -.
DR EnsemblFungi; CAG88507; CAG88507; DEHA2E21384g.
DR GeneID; 2902821; -.
DR KEGG; dha:DEHA2E21384g; -.
DR VEuPathDB; FungiDB:DEHA2E21384g; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_031058_0_1_1; -.
DR InParanoid; Q6BNI6; -.
DR OMA; PRYNSAI; -.
DR OrthoDB; 917526at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006950; P:response to stress; IEA:UniProt.
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..375
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248988"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 219
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 43898 MW; 26B568D485083038 CRC64;
MSSQGNKYEY GELADKLILA YSKRRLFKAI GTKRDRQQQF SRLDNKDKRF ISKLIDVSNS
NEKHKIPSEL DIALDCIDLA KIYEGVDKRE YERESKAKDP NLIYEDFIVL ELLHYFKHDF
FKWVNKPECS RCKQSSNNIV PTGNSGPPSI NPSEISIIEN YKCTKCNIAV SFPRYNNPIK
LLETKSGRCG EWVNCFIFIL RALLGSQSQI RYVWNHEDHV WCEYYSLGLK RWIHLDPCEG
VFDEPNLYCE NWGKKMSWCF AFGETYIMDV SDKYITKSDK QINKLESVSS LKNIKEFIDT
LNDDKLVRYY SNMALTASDE NRNLMRLYQE VILIHNSEKF NKENKIEVSR THNIPTGRQT
GDAEWTKSRG EDGNE
