Latest update: September 24, 2018


ProGT42 (ApNGT)

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ProGT ID ProGT42 (ApNGT)
ProGT Pathway
Organism Information
Organism NameActinobacillus pleuropneumoniae serotype 7 (strain AP76)
Clinical ImplicationPathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Pasteurellaceae
Order: Pasteurellales
Class: Gammaproteobacteria
Phylum: Proteobacteria
Taxonomic ID (NCBI)537457
Genome Information
Gene BankCP001091.1
EMBLCP001091.1
Gene Information
Gene NameAPP7_1697
Protein information
Protein NameApNGT 
UniProtKB/ SwissProt IDB3H2N2
NCBI Ref SeqWP_012478567.1
UniProtKB Sequence>sp|B3H2N2|NGT_ACTP7 UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 7 (strain AP76) GN=APP7_1697 PE=1 SV=1 MENENKPNVANFEAAVAVKDYEKACSELLLILSQLDSNFGGIQEIEFEYPVQLQDLEQEK IVYFCTRMATAITTLFSDPVLEISDLGVQRFLVYQRWLALIFASSPFVNADHILQTYNRE PNRKNSLEIHLDSSKSSLIKFCILYLPESNVNLNLDVMWNISPELCASLCFALQSPRFIG TSTAFNKRATILQWFPRHLDQLKNLNNIPSAISHDVYMHCSYDTSVNKHDVKRALNHVIR RHIESEYGWKDRYVAHIGYRNNKPVMVVLLEHFHSAHSIYRTHSTSMIAAREHFYLIGLG SPSVDQAGQEVFDEFHLVAGDNMKQKLEFIRSVCESNGAAIFYMPSIGMDMTTIFASNTR LAPIQAIALGHPATTHSDFIEYVIVEDDYVGSEACFSETLLRLPKDALPYVPSALAPEKV DYLLRENPEVVNIGIASTTMKLNPYFLEALKAIRDRAKVKVHFHFALGQSNGITHPYVER FIKSYLGDSATAHPHSPYHQYLRILHNCDMMVNPFPFGNTNGIIDMVTLGLVGVCKTGAE VHEHIDEGLFKRLGLPEWLIANTVDEYVERAVRLAENHQERLELRRYIIENNGLNTLFTG DPRPMGQVFLEKLNAFLKEN
EMBL CDSACE62349.1
Sequence length620 AA
Subcellular LocationCytoplasm
Potential Application1) ApNGT novel abilities could use a promising tool for the production of glycoconjugates and for site-specific modification of proteins.
Additional Information1) ApNGT is metal independent glycosyl transfer as it glycosylated the peptide in the presence of EDTA.
2) The N-linked glucose can be elongated by a polymerizing alpha6GlcT, which is sensitive to the UDP-glucose concentration.
3) ApNGT shows a relaxed peptide substrate specificity in vivo. In addition to the canonical NX(S/T) glycosylation consensus sites, it also glycosylates asparagine residues in NXA, NXG, NXD, and NXV sequons.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT41
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Acceptor specificity Sequon_1NX(S/T)
Donor TypeNucleotide activated sugars
Donor SpecificityUDP-Glc and UDP-Gal ( UDP-Glc is preferred over UDP-Gal)
Accessory GT IDProGT42.1
Glycan Information
Glycan transferredMonosaccharides (Glc and Gal) 
Method of Glycan IndentificationNanoLC-ESI-MS/MS (HCD and ETD), MS and MS/MS, NMR and MALDI-TOF MS
Experimental_strategiesIn vitro and In vivo  
Acceptor Subtrate Information
Acceptor Substrate name Hexapeptide DANYTK (labeled with TAMRA at the N terminus)
Acceptor Substrate name Synthetic Acceptor Peptide of Yeast glycoprotein lysophospholipase 2 (Plb2): SIVNPGGSNLTYIER
Acceptor Substrate name AcrA
ProGPdb ID ProGP217
Acceptor Substrate name Autotransporter adhesin
ProGPdb ID ProGP450
Acceptor Substrate name AtaC1866–2428
ProGPdb ID ProGP450
Acceptor Substrate name COK_1394-62–640
ProGPdb ID ProGP451
Acceptor Substrate name HMW1ct
ProGPdb ID ProGP227
Acceptor Substrate name human erythropoietin (hEPO)
Acceptor Substrate name Cholera toxin subunit B (CtxB)
Acceptor Substrate name GAPDH
Acceptor Substrate name PCKA
Acceptor Substrate name PurH
Acceptor Substrate name ArgG
Acceptor Substrate name DnaK (Chaperone protein)
Acceptor Substrate name YuaO (Uncharacterized protein)
Acceptor Substrate name MdtE( Multidrug resistance protein)
Acceptor Substrate name ArgG(Argininosuccinate synthase)
Litrature
Year Of Validation2011 
Reference Schwarz, F., Fan, Y. Y., Schubert, M., & Aebi, M. (2011). Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NXS/T consensus sequence. Journal of Biological Chemistry, jbc-M111.

Authors Schwarz, F., Fan, Y. Y., Schubert, M., & Aebi, M.
Research groupsMolecular Biology and Biophysics, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland
Corresponding Author Aebi, M.
ContactsMolecular Biology and Biophysics, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland Inst. of Microbiology, Dept. of Biology, ETH Zürich, Wolfgang-Pauli-Str. 10, 8093 Zürich, Switzerland
Reference Naegeli, A., Michaud, G., Schubert, M., Lin, C.W., Lizak, C., Darbre, T., Reymond, J.L. & Aebi, M. (2014). Substrate specificity of cytoplasmic N-glycosyltransferase. Journal of biological chemistry, jbc-M114.

Authors Naegeli, A., Michaud, G., Schubert, M., Lin, C.W., Lizak, C., Darbre, T., Reymond, J.L. & Aebi, M.
Research groups1 Department of Biology, Institute of Microbiology, ETH Zurich, CH-8093 Zurich. 2 Department of Chemistry and Biochemistry, University of Berne, 3012 Berne, and. 3 Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, CH-8093 Zurich, Switzerland. 4 Department of Biology, Institute of Microbiology, ETH Zurich, CH-8093 Zurich,
Corresponding Author Aebi, M.
Contacts1 Department of Biology, Institute of Microbiology, ETH Zurich, CH-8093 Zurich.
Reference Naegeli A, Neupert C, Fan YY, Lin CW, Poljak K, Papini AM, Schwarz F, Aebi M. Molecular analysis of an alternative N-glycosylation machinery by functional transfer from Actinobacillus pleuropneumoniae to Escherichia coli. Journal of Biological Chemistry. 2013 Nov 25:jbc-M113.

Authors Naegeli A, Neupert C, Fan YY, Lin CW, Poljak K, Papini AM, Schwarz F, Aebi M.
Research groups 1 Institute of Microbiology, Swiss Federal Institute of Technology, ETH Zurich, CH-8093 Zurich, Switzerland
Corresponding AuthorAebi M.
Contacts 1 Institute of Microbiology, Swiss Federal Institute of Technology, ETH Zurich, CH-8093 Zurich, Switzerland