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P21163

- PNGF_ELIMR

UniProt

P21163 - PNGF_ELIMR

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Protein

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

Gene

ngl

Organism
Elizabethkingia miricola (Chryseobacterium miricola)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei100 – 1001
Active sitei158 – 1581
Active sitei246 – 2461

GO - Molecular functioni

  1. 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 Source: InterPro
  2. peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F (EC:3.5.1.52)
Short name:
PNGase F
Alternative name(s):
Glycopeptide N-glycosidase
N-glycanase
Gene namesi
Name:ngl
Synonyms:png
OrganismiElizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifieri172045 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Pathology & Biotechi

Biotechnological usei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001D → N: Complete loss of activity. 1 Publication
Mutagenesisi158 – 1581E → Q: Loss of activity. 1 Publication
Mutagenesisi246 – 2461E → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 40401 PublicationAdd
BLAST
Chaini41 – 354314Peptide-N(4)-(N-acetyl-beta-D-glucosaminyl)asparagine amidase FPRO_0000022079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 961 Publication
Disulfide bondi244 ↔ 2481 Publication
Disulfide bondi271 ↔ 2921 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 505Combined sources
Beta strandi54 – 574Combined sources
Beta strandi60 – 623Combined sources
Beta strandi65 – 739Combined sources
Beta strandi80 – 8910Combined sources
Helixi92 – 943Combined sources
Beta strandi102 – 1087Combined sources
Turni110 – 1123Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi136 – 1394Combined sources
Helixi141 – 1433Combined sources
Turni144 – 1463Combined sources
Beta strandi147 – 15711Combined sources
Beta strandi165 – 17612Combined sources
Beta strandi181 – 19111Combined sources
Helixi195 – 1973Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi210 – 2145Combined sources
Beta strandi220 – 23112Combined sources
Beta strandi233 – 2386Combined sources
Turni239 – 2413Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi250 – 2567Combined sources
Beta strandi259 – 2668Combined sources
Helixi271 – 2733Combined sources
Beta strandi300 – 3034Combined sources
Helixi306 – 3083Combined sources
Beta strandi311 – 3188Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi332 – 34514Combined sources
Beta strandi351 – 3533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PGSX-ray1.80A41-354[»]
1PNFX-ray2.00A41-354[»]
1PNGX-ray2.20A41-354[»]
ProteinModelPortaliP21163.
SMRiP21163. Positions 41-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21163.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.230. 2 hits.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR008977. PHM/PNGase_F_dom.
IPR015197. PngaseF_C.
IPR015196. PngaseF_N.
[Graphical view]
PfamiPF09113. N-glycanase_C. 1 hit.
PF09112. N-glycanase_N. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21163-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKLLIFSIS AYLMAGIVSC KGVDSATPVT EDRLALNAVN APADNTVNIK
60 70 80 90 100
TFDKVKNAFG DGLSQSAEGT FTFPADVTTV KTIKMFIKNE CPNKTCDEWD
110 120 130 140 150
RYANVYVKNK TTGEWYEIGR FITPYWVGTE KLPRGLEIDV TDFKSLLSGN
160 170 180 190 200
TELKIYTETW LAKGREYSVD FDIVYGTPDY KYSAVVPVIQ YNKSSIDGVP
210 220 230 240 250
YGKAHTLGLK KNIQLPTNTE KAYLRTTISG WGHAKPYDAG SRGCAEWCFR
260 270 280 290 300
THTIAINNAN TFQHQLGALG CSANPINNQS PGNWAPDRAG WCPGMAVPTR
310 320 330 340 350
IDVLNNSLTG STFSYEYKFQ SWTNNGTNGD AFYAISSFVI AKSNTPISAP

VVTN
Length:354
Mass (Da):39,032
Last modified:November 1, 1991 - v2
Checksum:i22CF510F77C22539
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331R → G in AAA85323. (PubMed:2182634)Curated
Sequence conflicti160 – 1601W → C in AAA24932. (PubMed:2182635)Curated
Sequence conflicti283 – 2831N → I in AAA85323. (PubMed:2182634)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05449 mRNA. Translation: AAA85323.1.
J05411 Genomic DNA. Translation: AAA24932.1.
M57237 Genomic DNA. Translation: AAA24928.1. Sequence problems.
PIRiA38365. PNFMGF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05449 mRNA. Translation: AAA85323.1 .
J05411 Genomic DNA. Translation: AAA24932.1 .
M57237 Genomic DNA. Translation: AAA24928.1 . Sequence problems.
PIRi A38365. PNFMGF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PGS X-ray 1.80 A 41-354 [» ]
1PNF X-ray 2.00 A 41-354 [» ]
1PNG X-ray 2.20 A 41-354 [» ]
ProteinModelPortali P21163.
SMRi P21163. Positions 41-354.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P21163.

Family and domain databases

Gene3Di 2.60.120.230. 2 hits.
InterProi IPR014784. Cu2_ascorb_mOase-like_C.
IPR008977. PHM/PNGase_F_dom.
IPR015197. PngaseF_C.
IPR015196. PngaseF_N.
[Graphical view ]
Pfami PF09113. N-glycanase_C. 1 hit.
PF09112. N-glycanase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49742. SSF49742. 2 hits.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPNGF_ELIMR
AccessioniPrimary (citable) accession number: P21163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3