Latest update: September 24, 2018


ProGT37.2 (dGT1)

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ProGT ID ProGT37.2 (dGT1)
ProGT Pathway
Organism Information
Organism NameStreptococcus parasanguinis FW213
Domain Bacteria
PhylumFirmicutes
ClassificationFamily: Streptococcaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)1318
Genome Information
Gene BankNZ_LAUA01000017.1
Gene Information
Gene NamegalT1 
NCBI Reference SequenceAFJ26875.1
Protein information
Protein NamedGT1 
UniProtKB/ SwissProt IDB5A7M0
UniProtKB Sequence>tr|B5A7M0|B5A7M0_STRPA Putative glycosyltransferase OS=Streptococcus parasanguinis GN=galT1 PE=4 SV=1 MKRLSEIKVLPILESLKYIKHNHASVVRFGDGEIDLMTGHSIPYQDYNEKLAKRLQQILQ TKSDEKLLVCLPDVFSNMDRYNQNARHFWERHFLKYSEFYLNCCDAPFYGSTFISRPYID LIDKSPSEAYFESLKELWRGKDLLIVEGATSRSGVGNDLFVAASSIKRLVCPSKNAFQYY DEILRLTEKNAKNRLILVMLGPTAKVLVADLTTKGYQAIDLGHIDSEYEWYEMGATYKVK LTNKHTAEFNYDEGIELEFSQEYQEQIVARIGVDNSKQVQIKEMEKMDNGELISIIVPVY NVEKYLKRCLDSLLRQTYKNFEIILINDGSTDNSSIICEEYAKIDNRIQILHQTNAGPSA ARNAGITYASGKYITFVDSDDFVEEFYLEHLYRALVDNGSDISVCNFNSFNEDRQSFLFS ITKEKYFCKNYTIAEWMDLESSANNNLFLTFTFSPTKLFKAELFEGIRFPLGRLREDDAT IYRLYLKASQITFINEGSYYYSQRSEGLSRTRMLDDISSMISNAEERIALLASMGYDLTE QIKSYKGRLKKCCEDALRNGQIELYQQCCNKLDLIENYPKEK
EMBL CDSACF35268
Sequence length582 AA
PDB ID (Structural Information)4PFX, 4PHR, 4PHS
Glycosylation Information
CAZY FamilyGT101
EC Number (BRENDA)2.4.1.-
Sugar Donor SpecificityUDP-GalNAc 
Acceptor Substrate SpecificityGlc-Glc-GlcNAc modified Fap1
Experimental ValidationIn vivo and In vitro
Donor SpecificityUDP-GalNAc
Function in Glycosylation pathway1) Transfer GalNAc to the Glc-Glc-GlcNAc modified Fap1.
Additional Information1) dGT1 is involved in the biosynthesis of an SRRP adhesin Fap1 of S. parasanguinis.
2) dGT1 is unique bifunctional protein contains an N-terminal unknown function domain (DUF1792) a new type of glycosyltransferases, transferring glucose residues to Glc-GlcNAc-Fap1, and that the C terminus domain (CgT) is an independent glycosyltransferase and important for Fap1 glycosylation it transfers GlcNAc to the Glc-Glc-GlcNAc-modified Fap1.  
Litrature
Year Of Validation2014 
Reference Zhang, H., Zhu, F., Yang, T., Ding, L., Zhou, M., Li, J., Haslam, S.M., Dell, A., Erlandsen, H. & Wu, H. (2014). The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold. Nature communications, 5, 4339.

Authors Zhang, H., Zhu, F., Yang, T., Ding, L., Zhou, M., Li, J., Haslam, S.M., Dell, A., Erlandsen, H. & Wu, H.
Research groupsUniversity of Alabama at Birmingham, United States
Corresponding Author Wu, H.
ContactsUniversity of Alabama at Birmingham, United States
Reference Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). A new helical binding domain mediates a unique glycosyltransferase activity of a bifunctional protein. Journal of Biological Chemistry, jbc-M116.

Authors Zhang, H., Zhou, M., Yang, T., Haslam, S. M., Dell, A., & Wu, H.
Research groupsDepartments of Pediatric Dentistry and Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294 
Corresponding Author Wu, H.
ContactsDepartments of Pediatric Dentistry and Microbiology, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294