ProGP116 (Endo-β-N-acetylglucosaminidase F3)
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| ProGP ID | ProGP116 (Endo-β-N-acetylglucosaminidase F3) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Flavobacterium meningosepticum (Elizabethkingia meningoseptica) |
| Domain | Bacteria |
| Taxonomic ID (NCBI) | 238 |
| Genome Information | |
| GenBank | L06332 |
| EMBL | L06332 |
| Gene Information | |
| Gene Name | endOF3 |
| Protein Information | |
| Protein Name | Endo-β-N-acetylglucosaminidase F3 |
| UniProtKB/SwissProt ID | P36913 |
| EMBL-CDS | AAA24924.1 |
| UniProtKB Sequence | >sp|P36913|EBA3_FLAME Endo-beta-N-acetylglucosaminidase F3 OS=Flavobacterium meningosepticum GN=endOF3 PE=1 SV=1 MKKIFFAQCSILLLMLGSCSKMTEDMTPESVNKEASVKSATALAGSNGVCIAYYITDGRN PTFKLKDIPDKVDMVILFGLKYWSLQDTTKLPGGTGMMGSFKSYKDLDTQIRSLQSRGIK VLQNIDDDVSWQSSKPGGFASAAAYGDAIKSIVIDKWKLDGISLDIEHSGAKPNPIPTFP GYAATGYNGWYSGSMAATPAFLNVISELTKYFGTTAPNNKQLQIASGIDVYAWNKIMENF RNNFNYIQLQSYGANVSRTQLMMNYATGTNKIPASKMVFGAYAEGGTNQANDVEVAKWTP TQGAKGGMMIYTYNSNVSYANAVRDAVKN |
| Sequence length | 329 AA |
| Subcellular Location | Periplasm (secreted) |
| Function | Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins. Hydrolyzes bi- and triantennary glycans. The presence of a core-bound fucose greatly augments endo F3 activity on biantennary and, presumably, triantennary oligosaccharides. EC= 3.2.1.96. |
| Protein Structure | |
| PDB ID | 1EOK, 1EOM |
| Glycosylation Status | |
| Glycosylation Type | O- (Thr) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | (Signal peptide: 1-39) T88 |
| Experimentally Validated Glycosite(s ) in Mature Protein | T49 |
| Glycosite(s) Annotated Protein Sequence | >sp|P36913|EBA3_FLAME Endo-beta-N-acetylglucosaminidase F3 OS=Flavobacterium meningosepticum GN=endOF3 PE=1 SV=1 MKKIFFAQCSILLLMLGSCSKMTEDMTPESVNKEASVKSATALAGSNGVCIAYYITDGRN PTFKLKDIPDKVDMVILFGLKYWSLQDT*(88)TKLPGGTGMMGSFKSYKDLDTQIRSLQSRGIK VLQNIDDDVSWQSSKPGGFASAAAYGDAIKSIVIDKWKLDGISLDIEHSGAKPNPIPTFP GYAATGYNGWYSGSMAATPAFLNVISELTKYFGTTAPNNKQLQIASGIDVYAWNKIMENF RNNFNYIQLQSYGANVSRTQLMMNYATGTNKIPASKMVFGAYAEGGTNQANDVEVAKWTP TQGAKGGMMIYTYNSNVSYANAVRDAVKN |
| Sequence Around Glycosites (21 AA) | FGLKYWSLQDTTKLPGGTGMM |
| Technique(s) used for Glycosylation Detection | Mass shift detected on SDS-polyacrylamide gel and TFA (trifluoroacetic acid) hydrolysis of intact glycopeptide followed by HPAEC chromatography on a PA-1 column |
| Technique(s) used for Glycosylated Residue(s) Detection | Edman degradation and collision activated dissociation (CAD) mass spectrometry |
| Protein Glycosylation- Implication | Glycosylation may contribute towards protein stability |
| Glycan Information | |
| Glycan Annotation | Linkage: Man- Thr. Branched, acidic, heptasaccharide (1244 Da) containing 3 different uronyl analogs, a methylated Rham and Man, a Glc, and a reducing terminal Man. Only pyranose ring forms were detected [(2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU-4[(2-OMe)Rham1-2]Man]. |
| BCSDB ID | 137520 |
| Technique(s) used for Glycan Identification | ESI-MS (electrospray ionization mass spectrometry), CID (collision-induced dissociation), and a combination of isotopic labeling, composition and methylation analysis. |
| Protein Glycosylation linked (PGL) gene(s) | |
| Additional Comment | Identified glycosylation Sequon features: Consensus sequon observed Asp-Ser (DS) or Asp-Thr-Thr (DTT), at turns. DT alone may not serve as a sequon. Interestingly, the experimentally examined other five nonglycosylated DT sequons were followed by N, D and Q. Post translational modification of 1.2-kDa was detected by MS in 1993 (Ref. no. 4). The protein migrated slowly on SDS-PAGE (compared to its theoretical weight) and was found to be heterogeneous by MS. |
| Literature | |
| Year of Identification | 1995 |
| Year of Identification Month Wise | 1995.06.02 |
| Year of Validation | 1995 |
| Reference | Waddling, C.A., Plummer, T.H., Tarentino, A.L. and Van Roey, P., 2000. Structural basis for the substrate specificity of endo-β-N-acetylglucosaminidase F3. Biochemistry, 39(27), pp.7878-7885. |
| Corresponding Author | P Van Roey |
| Contact | Division of Molecular Medicine, Wadsworth Center, New York State Department of Health, Albany, New York 12201, USA. |
| Reference | Plummer, T.H., Tarentino, A.L. and Hauer, C.R., 1995. Novel, Specific O-Glycosylation of Secreted Flavobacterium meningosepticum Proteins.: Asp-Ser∗ AND Asp-Thr∗-Thr CONSENSUS SITES∗. Journal of Biological Chemistry, 270(22), pp.13192-13196. |
| Corresponding Author | Thomas H Plummer Jr |
| Contact | Division of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA. |
| Reference | Reinhold, B.B., Hauer, C.R., Plummer, T.H. and Reinhold, V.N., 1995. Detailed Structural Analysis of a Novel, Specific O-Linked Glycan from the Prokaryote Flavobacterium meningosepticum∗. Journal of Biological Chemistry, 270(22), pp.13197-13203. |
| Corresponding Author | Vernon N Reinhold |
| Contact | Department of Immunology Boston University Medical Center 80 East Concord ST Boston |
| Reference | Tarentino, A.L., Quinones, G., Changchien, L.M. and Plummer, T.H., 1993. Multiple endoglycosidase F activities expressed by Flavobacterium meningosepticum endoglycosidases F2 and F3. Molecular cloning, primary sequence, and enzyme expression. Journal of Biological Chemistry, 268(13), pp.9702-9708. |
| Corresponding Author | Thomas H Plummer Jr A L Tarentino |
| Contact | Division of Clinical Sciences, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509. |