Latest update: September 24, 2018


ProGT8 (Aah)

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ProGT ID ProGT8 (Aah)
ProGT Pathway
Organism Information
Organism NameEscherichia coli K12
Clinical ImplicationNon-pathogenic
DomainBacteria
PhylumProteobacteria
ClassificationFamily: Enterobacteriaceae
Order: Enterobacteriales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)562
Genome Information
Gene BankGU810159
EMBLGU810159
Gene Information
Gene Nameaah
NCBI Reference SequenceAJ304444.1
Protein information
Protein NameAah 
UniProtKB/ SwissProt IDQ93K96
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 CDSADH10229.1
Sequence length391 AA
Subcellular LocationCytoplasm
Function in Native Organism 1) Aah is a heptosyltransferase which transfers a heptose sugar to acceptor protein AIDA.
Additional Information1) 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 TypeO- (Ser/Thr) linked 
CAZY FamilyGTNC
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Acceptor specificity Sequon_1NGGKTTATTVNSSGSQNVG
Donor TypeNucleotide activated sugars
Donor SpecificityADP-Heptose
Glycan Information
Glycan transferredMonosaccharide (Heptose) 
Method of Glycan IndentificationGC MS, MS-MS (CID) and, MALDI-TOF
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name AIDA-I
ProGPdb ID ProGP201
Acceptor Substrate name Ag 43
ProGPdb ID ProGP249
Litrature
Year Of Validation2001 
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.

Authors Benz, I., & Schmidt, M. A.
Research groupsInstitute of Infectiology, Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany
Corresponding Author Schmidt, M. A.
ContactsInstitute of Infectiology - Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany
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.

Authors Charbonneau, M.È., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lépine, F.& Mourez, M.
Research groupsUniversity of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
Corresponding Author Mourez, M.
ContactsUniversity of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
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.

Authors Knudsen, S. K., Stensballe, A., Franzmann, M., Westergaard, U. B., & Otzen, D. E.
Research groupsDepartment of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
Corresponding Author Otzen, D. E.
ContactsDepartment of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark.
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.

Authors Charbonneau, M.È., Côté, J.P., Haurat, M.F., Reiz, B., Crépin, S., Berthiaume, F., Dozois, C.M., Feldman, M.F. & Mourez, M.
Research groupsCanada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
Corresponding Author Mourez, M.
ContactsCanada Research Chair on Bacterial Animal Diseases, University of Montreal, Faculty of Veterinary Medicine St-Hyacinthe, 3200 Sicotte, St-Hyacinthe, Quebec, Canada.
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.

Authors Lu, Q., Yao, Q., Xu, Y., Li, L., Li, S., Liu, Y., Gao, W., Niu, M., Sharon, M., Ben-Nissan, G. & Zamyatina, A.
Research groups1 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
Corresponding Author Zamyatina, A.
Contacts1 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.
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.

Authors Yao, Q., Lu, Q., Wan, X., Song, F., Xu, Y., Hu, M., ... & Shao, F.
Research groups1 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.
Corresponding Author Shao, F.
ContactsDr Feng Shaos Laboratory, National Institute of Biological Sciences, Beijing, China