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P21163 (PNGF_ELIMR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F

Short name=PNGase F
EC=3.5.1.52
Alternative name(s):
Glycopeptide N-glycosidase
N-glycanase
Gene names
Name:ngl
Synonyms:png
OrganismElizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifier172045 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves an entire glycan from a glycoprotein. Requires that the glycosylated asparagine moiety (reaction 1) be substituted on its amino (R1) and carboxyl (R2) terminus with a polypeptide chain.

Catalytic activity

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.

Subunit structure

Monomer.

Biotechnological use

Widely used for the removal of N-glycans from glycoproteinss and glycopeptides in laboratory.

Miscellaneous

PNGase F binds primarily to the polypeptide chain around the glycosamine junction including the inner di-N-acetylchitobiose core on the carbohydrate moiety.

Caution

Submitted as Flavobacterium meningosepticum ATCC 33958 by the authors and identified as Elizabethkingia miricola by ATCC Catalog.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Ref.2
Chain41 – 354314Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F
PRO_0000022079

Sites

Active site1001
Active site1581
Active site2461

Amino acid modifications

Disulfide bond91 ↔ 96 Ref.4
Disulfide bond244 ↔ 248 Ref.4
Disulfide bond271 ↔ 292 Ref.4

Experimental info

Mutagenesis1001D → N: Complete loss of activity.
Mutagenesis1581E → Q: Loss of activity.
Mutagenesis2461E → Q: Loss of activity.
Sequence conflict331R → G in AAA85323. Ref.1
Sequence conflict1601W → C in AAA24932. Ref.2
Sequence conflict2831N → I in AAA85323. Ref.1

Secondary structure

.............................................................. 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21163 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 22CF510F77C22539

FASTA35439,032
        10         20         30         40         50         60 
MRKLLIFSIS AYLMAGIVSC KGVDSATPVT EDRLALNAVN APADNTVNIK TFDKVKNAFG 

        70         80         90        100        110        120 
DGLSQSAEGT FTFPADVTTV KTIKMFIKNE CPNKTCDEWD RYANVYVKNK TTGEWYEIGR 

       130        140        150        160        170        180 
FITPYWVGTE KLPRGLEIDV TDFKSLLSGN TELKIYTETW LAKGREYSVD FDIVYGTPDY 

       190        200        210        220        230        240 
KYSAVVPVIQ YNKSSIDGVP YGKAHTLGLK KNIQLPTNTE KAYLRTTISG WGHAKPYDAG 

       250        260        270        280        290        300 
SRGCAEWCFR THTIAINNAN TFQHQLGALG CSANPINNQS PGNWAPDRAG WCPGMAVPTR 

       310        320        330        340        350 
IDVLNNSLTG STFSYEYKFQ SWTNNGTNGD AFYAISSFVI AKSNTPISAP VVTN 

« Hide

References

[1]"Molecular cloning and amino acid sequence of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase from flavobacterium meningosepticum."
Tarentino A.L., Quinones G., Trumble A., Changchien L.-M., Duceman B., Maley F., Plummer T.H. Jr.
J. Biol. Chem. 265:6961-6966(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"Cloning and expression of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F in Escherichia coli."
Barsomian G.D., Johnson T.L., Borowski M., Denman J., Ollington J.F., Hirani S., McNeilly D.S., Rasmussen J.R.
J. Biol. Chem. 265:6967-6972(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 41-61.
Strain: ATCC 33958.
[3]"Molecular cloning and heterologous expression of N-glycosidase F from Flavobacterium meningosepticum."
Lemp D., Haselbeck A., Klebl F.
J. Biol. Chem. 265:15606-15610(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution."
Kuhn P., Tarantino A.L., Plummer T.H. Jr., van Roey P.
Biochemistry 33:11699-11706(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum."
Norris G.E., Stillman T.J., Anderson B.F., Baker E.N.
Structure 2:1049-1059(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[6]"Active site and oligosaccharide recognition residues of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F."
Kuhn P., Guan C., Cui T., Tarentino A.L., Plummer T.H. Jr., van Roey P.
J. Biol. Chem. 270:29493-29497(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05449 mRNA. Translation: AAA85323.1.
J05411 Genomic DNA. Translation: AAA24932.1.
M57237 Genomic DNA. Translation: AAA24928.1. Sequence problems.
PIRPNFMGF. A38365.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGSX-ray1.80A41-354[»]
1PNFX-ray2.00A41-354[»]
1PNGX-ray2.20A41-354[»]
ProteinModelPortalP21163.
SMRP21163. Positions 41-354.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.230. 2 hits.
InterProIPR014784. Cu2_ascorb_mOase-like_C.
IPR008977. PHM/PNGase_F_dom.
IPR015197. PngaseF_C.
IPR015196. PngaseF_N.
[Graphical view]
PfamPF09113. N-glycanase_C. 1 hit.
PF09112. N-glycanase_N. 1 hit.
[Graphical view]
SUPFAMSSF49742. SSF49742. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP21163.

Entry information

Entry namePNGF_ELIMR
AccessionPrimary (citable) accession number: P21163
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1991
Last modified: October 16, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references