| ProGT ID | ProGT8 (Aah) |
| ProGT Pathway |  | Organism Information | | Organism Name | Escherichia coli K12 | | Clinical Implication | Non-pathogenic | | Domain | Bacteria | | Phylum | Proteobacteria | | Classification | Family: Enterobacteriaceae
Order: Enterobacteriales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria" | | Taxonomic ID (NCBI) | 562 | | Genome Information | | Gene Bank | GU810159 | | EMBL | GU810159 | | Gene Information | | Gene Name | aah | | NCBI Reference Sequence | AJ304444.1 | | Protein information | | Protein Name | Aah | | UniProtKB/ SwissProt ID | Q93K96 | | UniProtKB Sequence | >tr|Q93K96|Q93K96_ECOLX AIDA-associated heptosyltransferase OS=Escherichia coli GN=aah PE=4 SV=1
MTFLSPPEIPTIKADNGTYYDFNNGARILFPKGEWHVNIIDEESGNILFSCDTKAGWVTS
TKKYYVKFRIQAFKKGDEKPFLDTVMELKDKPVLISFPTGTLGDIIAWFHYAEKFRIKHQ
CKLECSVSEEFITLLSDNYPDIKFTSAQDKYEGKPYATYRIGLFFNGDTDNQPVDFRLVG
FHRNAGYILGVSPQEDPPRLNLSAERKIQEPYVCIAVQSTAQAKHWNNGLGWAEVVRYLK
ELGYRVLCIDRNAHAGNGFVWNHIPWGAEDFTGALPLQERVDLLRHASFFVGLSSGLSWL
AWASRIPVVLISGFSRPDSEFYTPWRVFNSHGCNGCWDNTNYNFDHTDFLWCPVHKGTDR
QFECTRLITGKQVCGVIRTLHSYLTNHDRII
| | EMBL CDS | ADH10229.1 | | Sequence length | 391 AA | | Subcellular Location | Cytoplasm | | Function in Native Organism | 1) Aah is a heptosyltransferase which transfers a heptose sugar to acceptor protein AIDA. | | Additional Information | 1) AAH is the prototype of a new large family of bacterial protein O-glycosyltransferases that modify different substrates containing a structural motif of 19 amino acid consensus sequence.
2) Iron binding is required for AAH glycosyltransferase activity.
3) AAH and its paralogue AAH2 are heptosylating autotransporter AIDA-1 which is essential for pathogenesis and colonization in mice.
| | Glycosyltransferase Information | | Glycosylation Type | O- (Ser/Thr) linked | | CAZY Family | GTNC | | EC Number (BRENDA) | 2.4.1.- | | Mechanism of Glycan Transfer | Sequential | | Acceptor specificity Sequon_1 | NGGKTTATTVNSSGSQNVG | | Donor Type | Nucleotide activated sugars | | Donor Specificity | ADP-Heptose | |
|---|
| Glycan Information |
| Glycan transferred | Monosaccharide (Heptose) |
| Method of Glycan Indentification | GC MS, MS-MS (CID) and, MALDI-TOF |
| Experimental_strategies | In vivo |
| Acceptor Subtrate Information |
| Acceptor Substrate name | AIDA-I |
| ProGPdb ID | ProGP201 |
| Acceptor Substrate name | Ag 43 |
| ProGPdb ID | ProGP249 |
| Litrature |
| Year Of Validation | 2001 |
| Reference | Benz, I., & Schmidt, M. A. (2001). Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA?I adhesin. Molecular microbiology, 40(6), 1403-1413.
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| Authors | Benz, I., & Schmidt, M. A.
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| Research groups | Institute of Infectiology, Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany
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| Corresponding Author | Schmidt, M. A.
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| Contacts | Institute of Infectiology - Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany
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| Reference | Charbonneau, M.È., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lépine, F.& Mourez, M. (2007). O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence. Journal of bacteriology, 189(24), 8880-8889.
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| Authors | Charbonneau, M.È., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lépine, F.& Mourez, M.
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| Research groups | University of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
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| Corresponding Author | Mourez, M.
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| Contacts | University of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
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| Reference | Knudsen, S. K., Stensballe, A., Franzmann, M., Westergaard, U. B., & Otzen, D. E. (2008). Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation. Biochemical Journal, 412(3), 563-577.
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| Authors | Knudsen, S. K., Stensballe, A., Franzmann, M., Westergaard, U. B., & Otzen, D. E.
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| Research groups | Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
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| Corresponding Author | Otzen, D. E.
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| Contacts | Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
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| Reference | Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. & Mourez, M. (2012). A structural motif is the recognition site for a new family of bacterial protein O?glycosyltransferases. Molecular microbiology, 83(5), 894-907.
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| Authors | Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. & Mourez, M.
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| Research groups | Canada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
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| Corresponding Author | Mourez, M.
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| Contacts | Canada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
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| Reference | Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. & Zamyatina, A. (2014). An iron-containing dodecameric heptosyltransferase family modifies bacterial autotransporters in pathogenesis. Cell host & microbe, 16(3), 351-363.
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| Authors | Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. & Zamyatina, A.
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| Research groups | 1 National Institute of Biological Sciences, Beijing 102206, China.
2 College of Biological Sciences, China Agricultural University, Beijing 100094, China.
3 Institute of Analytical Chemistry & Synthetic and Functional Biomolecules Center, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
4 Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
5 Department of Chemistry, University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.
6 National Institute of Biological Sciences, Beijing 102206, China
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| Corresponding Author | Zamyatina, A.
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| Contacts | 1 National Institute of Biological Sciences, Beijing 102206, China. 2 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. 3 National Institute of Biological Sciences, Beijing, Collaborative Innovation Center for Cancer Medicine, Beijing 102206, China.
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| Reference | Yao, Q., Lu, Q., Wan, X., Song, F., Xu, Y., Hu, M., ... & Shao, F. (2014). A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. Elife, 3, e03714.
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| Authors | Yao, Q., Lu, Q., Wan, X., Song, F., Xu, Y., Hu, M., ... & Shao, F.
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| Research groups | 1 Dr Feng Shaos Laboratory, National Institute of Biological Sciences, Beijing, China.
2 Dr Niu Huangs Laboratory, National Institute of Biological Sciences, Beijing, China.
3 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
4 Institute of Analytic Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
5 Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
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| Corresponding Author | Shao, F.
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| Contacts | Dr Feng Shaos Laboratory, National Institute of Biological Sciences, Beijing, China
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