PNGF_ELIMR
ID PNGF_ELIMR Reviewed; 354 AA.
AC P21163;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F;
DE Short=PNGase F;
DE EC=3.5.1.52;
DE AltName: Full=Glycopeptide N-glycosidase;
DE AltName: Full=N-glycanase;
DE Flags: Precursor;
GN Name=ngl; Synonyms=png;
OS Elizabethkingia miricola (Chryseobacterium miricola).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=172045;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2182634; DOI=10.1016/s0021-9258(19)39244-0;
RA Tarentino A.L., Quinones G., Trumble A., Changchien L.-M., Duceman B.,
RA Maley F., Plummer T.H. Jr.;
RT "Molecular cloning and amino acid sequence of peptide-N4-(N-acetyl-beta-D-
RT glucosaminyl)asparagine amidase from flavobacterium meningosepticum.";
RL J. Biol. Chem. 265:6961-6966(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 41-61.
RC STRAIN=ATCC 33958;
RX PubMed=2182635; DOI=10.1016/s0021-9258(19)39245-2;
RA Barsomian G.D., Johnson T.L., Borowski M., Denman J., Ollington J.F.,
RA Hirani S., McNeilly D.S., Rasmussen J.R.;
RT "Cloning and expression of peptide-N4-(N-acetyl-beta-D-
RT glucosaminyl)asparagine amidase F in Escherichia coli.";
RL J. Biol. Chem. 265:6967-6972(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2203781; DOI=10.1016/s0021-9258(18)55440-5;
RA Lemp D., Haselbeck A., Klebl F.;
RT "Molecular cloning and heterologous expression of N-glycosidase F from
RT Flavobacterium meningosepticum.";
RL J. Biol. Chem. 265:15606-15610(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7918386; DOI=10.1021/bi00205a005;
RA Kuhn P., Tarantino A.L., Plummer T.H. Jr., van Roey P.;
RT "Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine
RT amidase F at 2.2-A resolution.";
RL Biochemistry 33:11699-11706(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7881905; DOI=10.1016/s0969-2126(94)00108-1;
RA Norris G.E., Stillman T.J., Anderson B.F., Baker E.N.;
RT "The three-dimensional structure of PNGase F, a glycosylasparaginase from
RT Flavobacterium meningosepticum.";
RL Structure 2:1049-1059(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS.
RX PubMed=7493989; DOI=10.1074/jbc.270.49.29493;
RA Kuhn P., Guan C., Cui T., Tarentino A.L., Plummer T.H. Jr., van Roey P.;
RT "Active site and oligosaccharide recognition residues of peptide-N4-(N-
RT acetyl-beta-D-glucosaminyl)asparagine amidase F.";
RL J. Biol. Chem. 270:29493-29497(1995).
CC -!- FUNCTION: Cleaves an entire glycan from a glycoprotein. Requires that
CC the glycosylated asparagine moiety (reaction 1) be substituted on its
CC amino (R1) and carboxyl (R2) terminus with a polypeptide chain.
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 -!- SUBUNIT: Monomer.
CC -!- BIOTECHNOLOGY: Widely used for the removal of N-glycans from
CC glycoproteinss and glycopeptides in laboratory.
CC -!- MISCELLANEOUS: PNGase F binds primarily to the polypeptide chain around
CC the glycosamine junction including the inner di-N-acetylchitobiose core
CC on the carbohydrate moiety.
CC -!- CAUTION: Submitted as Flavobacterium meningosepticum ATCC 33958 by the
CC authors and identified as Elizabethkingia miricola by ATCC Catalog.
CC {ECO:0000305}.
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DR EMBL; J05449; AAA85323.1; -; mRNA.
DR EMBL; J05411; AAA24932.1; -; Genomic_DNA.
DR EMBL; M57237; AAA24928.1; ALT_SEQ; Genomic_DNA.
DR PIR; A38365; PNFMGF.
DR RefSeq; WP_034866261.1; NZ_JRFN01000002.1.
DR PDB; 1PGS; X-ray; 1.80 A; A=41-354.
DR PDB; 1PNF; X-ray; 2.00 A; A=41-354.
DR PDB; 1PNG; X-ray; 2.20 A; A=41-354.
DR PDBsum; 1PGS; -.
DR PDBsum; 1PNF; -.
DR PDBsum; 1PNG; -.
DR AlphaFoldDB; P21163; -.
DR SMR; P21163; -.
DR IntAct; P21163; 2.
DR STRING; 172045.KS04_00695; -.
DR PRIDE; P21163; -.
DR eggNOG; ENOG502Z8FK; Bacteria.
DR EvolutionaryTrace; P21163; -.
DR GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.120.230; -; 2.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR015197; PngaseF_C.
DR InterPro; IPR015196; PngaseF_N.
DR Pfam; PF09113; N-glycanase_C; 1.
DR Pfam; PF09112; N-glycanase_N; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:2182635"
FT CHAIN 41..354
FT /note="Peptide-N(4)-(N-acetyl-beta-D-
FT glucosaminyl)asparagine amidase F"
FT /id="PRO_0000022079"
FT ACT_SITE 100
FT ACT_SITE 158
FT ACT_SITE 246
FT DISULFID 91..96
FT /evidence="ECO:0000269|PubMed:7918386"
FT DISULFID 244..248
FT /evidence="ECO:0000269|PubMed:7918386"
FT DISULFID 271..292
FT /evidence="ECO:0000269|PubMed:7918386"
FT MUTAGEN 100
FT /note="D->N: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:7493989"
FT MUTAGEN 158
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7493989"
FT MUTAGEN 246
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7493989"
FT CONFLICT 33
FT /note="R -> G (in Ref. 1; AAA85323)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="W -> C (in Ref. 2; AAA24932)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="N -> I (in Ref. 1; AAA85323)"
FT /evidence="ECO:0000305"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:1PGS"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1PGS"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1PGS"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1PGS"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:1PGS"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 220..231
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1PGS"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:1PGS"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1PGS"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 332..345
FT /evidence="ECO:0007829|PDB:1PGS"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1PGS"
SQ SEQUENCE 354 AA; 39032 MW; 22CF510F77C22539 CRC64;
MRKLLIFSIS AYLMAGIVSC KGVDSATPVT EDRLALNAVN APADNTVNIK TFDKVKNAFG
DGLSQSAEGT FTFPADVTTV KTIKMFIKNE CPNKTCDEWD RYANVYVKNK TTGEWYEIGR
FITPYWVGTE KLPRGLEIDV TDFKSLLSGN TELKIYTETW LAKGREYSVD FDIVYGTPDY
KYSAVVPVIQ YNKSSIDGVP YGKAHTLGLK KNIQLPTNTE KAYLRTTISG WGHAKPYDAG
SRGCAEWCFR THTIAINNAN TFQHQLGALG CSANPINNQS PGNWAPDRAG WCPGMAVPTR
IDVLNNSLTG STFSYEYKFQ SWTNNGTNGD AFYAISSFVI AKSNTPISAP VVTN
