Latest update: September 24, 2018


ProGT37.1 (Gtf3)

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ProGT ID ProGT37.1 (Gtf3)
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 BankEU821531
EMBLEU821531
Gene Information
Gene Namenss 
NCBI Reference SequenceACF35267.1
Protein information
Protein NameGtf3 
UniProtKB/ SwissProt IDB5A7L9
UniProtKB Sequence>tr|B5A7L9|B5A7L9_STRPA Nucleotide sugar synthetase-like protein OS=Streptococcus parasanguinis GN=nss PE=1 SV=1 MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVA GLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAY YNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERF SFVKEWKYDIPLKVYTWQNVELPQNVHKINYRPDEQLLMEMSQGGFGLVWMDDKDKEYQS LYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELV KNVRSFNPILRKGFFTRRLLTESVFQAICD
EMBL CDSACF35267.1.
Sequence length330 AA
PDB ID (Structural Information)3QKW, 3RHZ
Glycosylation Information
CAZY FamilyGTNC
EC Number (BRENDA)2.4.1.-
Sugar Donor SpecificityUDP-Glc 
Acceptor Substrate SpecificityGlc-GalNAc modified Fap1
Experimental ValidationIn vitro and In vivo
Donor SpecificityUDP-Glc
Function in Glycosylation pathway1) Transfer Glucose to the Glc-GalNAc modified Fap1.
Additional Information1) Gtf3 transfer Glucose on previously modified Fap1 protein and it also plays an important role in the biofilm formation by S. parasanguinis. 
Litrature
Year Of Validation2010 
Reference Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H. (2010). A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinis. Journal of Biological Chemistry, jbc-M109.

Authors Zhou, M., Zhu, F., Dong, S., Pritchard, D., & Wu, H.
Research groupsDepartment of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA
Corresponding Author Wu, H.
ContactsDepartment of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35244, USA
Reference Zhu, F., Erlandsen, H., Ding, L., Li, J., Huang, Y., Zhou, M., ... & Wu, H. (2011). Structural and functional analysis of a new subfamily of glycosyltransferases required for glycosylation of serine-rich streptococcal adhesins. Journal of Biological Chemistry, jbc-M110.

Authors Zhu, F., Erlandsen, H., Ding, L., Li, J., Huang, Y., Zhou, M., ... & Wu, H.
Research groupsDepartment of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama 35294, USA
Corresponding Author Wu, H.
ContactsDepartment of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama 35294, USA
Reference Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H. (2016). Engineering and dissecting the glycosylation pathway of a streptococcal serine-rich repeat adhesin. Journal of Biological Chemistry, jbc-M116.

Authors Zhu, F., Zhang, H., Yang, T., Haslam, S. M., Dell, A., & Wu, H.
Research groups1 University of Alabama at Birmingham, United States. 2 Imperial College London, United Kingdom. 3 University of Alabama at Birmingham, United States
Corresponding Author Wu, H.
ContactsUniversity of Alabama at Birmingham, United States