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P21163

- PNGF_ELIMR

UniProt

P21163 - PNGF_ELIMR

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
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    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

    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 – 505
    Beta strandi54 – 574
    Beta strandi60 – 623
    Beta strandi65 – 739
    Beta strandi80 – 8910
    Helixi92 – 943
    Beta strandi102 – 1087
    Turni110 – 1123
    Beta strandi115 – 1228
    Beta strandi125 – 1273
    Beta strandi132 – 1343
    Beta strandi136 – 1394
    Helixi141 – 1433
    Turni144 – 1463
    Beta strandi147 – 15711
    Beta strandi165 – 17612
    Beta strandi181 – 19111
    Helixi195 – 1973
    Beta strandi198 – 2036
    Beta strandi210 – 2145
    Beta strandi220 – 23112
    Beta strandi233 – 2386
    Turni239 – 2413
    Beta strandi242 – 2454
    Beta strandi250 – 2567
    Beta strandi259 – 2668
    Helixi271 – 2733
    Beta strandi300 – 3034
    Helixi306 – 3083
    Beta strandi311 – 3188
    Beta strandi326 – 3283
    Beta strandi332 – 34514
    Beta strandi351 – 3533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MRKLLIFSIS AYLMAGIVSC KGVDSATPVT EDRLALNAVN APADNTVNIK    50
    TFDKVKNAFG DGLSQSAEGT FTFPADVTTV KTIKMFIKNE CPNKTCDEWD 100
    RYANVYVKNK TTGEWYEIGR FITPYWVGTE KLPRGLEIDV TDFKSLLSGN 150
    TELKIYTETW LAKGREYSVD FDIVYGTPDY KYSAVVPVIQ YNKSSIDGVP 200
    YGKAHTLGLK KNIQLPTNTE KAYLRTTISG WGHAKPYDAG SRGCAEWCFR 250
    THTIAINNAN TFQHQLGALG CSANPINNQS PGNWAPDRAG WCPGMAVPTR 300
    IDVLNNSLTG STFSYEYKFQ SWTNNGTNGD AFYAISSFVI AKSNTPISAP 350
    VVTN 354
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 90 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