ProGT31 (XcOGT)

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ProGT ID ProGT31 (XcOGT)
Organism Information
Organism NameXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Clinical ImplicationPlant Pathogen
DomainBacteria
Classification Phylum : Proteobacteria
Class : GammaProteobacteria
Orders : Xanthomonadales
Family : Xanthomonadaceae
Genus : Xanthomonas
Species : campestris
Strain : ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
Taxonomic ID (NCBI)190485 
Genome Information
Gene BankAE008922
EMBLAE008922
Gene Information
Gene NameXCC0866
NCBI Gene ID999532
Protein information
Protein NameXcOGT 
UniProtKB/ SwissProt IDQ8PC69
NCBI Ref SeqNP_636257
UniProtKB Sequence>tr|Q8PC69|Q8PC69_XANCP Uncharacterized protein OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) GN=XCC0866 PE=1 SV=1 MTADGPRELLQLRAAVRHRPQDFVAWLMLADAELGMGDTTAGEMAVQRGLALHPGHPEAV ARLGRVRWTQQRHAEAAVLLQQASDAAPEHPGIALWLGHALEDAGQAEAAAAAYTRAHQL LPEEPYITAQLLNWRRRLCDWRALDVLSAQVRAAVAQGVGAVEPFAFLSEDASAAEQLAC ARTRAQAIAASVRPLAPTRVRSKGPLRVGFVSNGFGAHPTGLLTVALFEALQRRQPDLQM HLFATSGDDGSTLRTRLAQASTLHDVTALGHLATAKHIRHHGIDLLFDLRGWGGGGRPEV FALRPAPVQVNWLAYPGTSGAPWMDYVLGDAFALPPALEPFYSEHVLRLQGAFQPSDTSR VVAEPPSRTQCGLPEQGVVLCCFNNSYKLNPQSMARMLAVLREVPDSVLWLLSGPGEADA RLRAFAHAQGVDAQRLVFMPKLPHPQYLARYRHADLFLDTHPYNAHTTASDALWTGCPVL TTPGETFAARVAGSLNHHLGLDEMNVADDAAFVAKAVALASDPAALTALHARVDVLRRAS GVFHMDGFADDFGALLQALARRHGWLGI
EMBL CDSAAM40181.1
Sequence length568 AA
String190485.XCC0866. 
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
CAZY FamilyGT41
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Donor TypeUDP-GlcNAc
Donor SpecificityNucleotide activated sugars
Glycan Information
Glycan transferredMonosaccharide (GlcNAc) 
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Litrature
Year Of Validation2008 
Reference Clarke, A.J., Hurtado?Guerrero, R., Pathak, S., Schüttelkopf, A.W., Borodkin, V., Shepherd, S.M., Ibrahim, A.F. and Van Aalten, D.M., 2008. Structural insights into mechanism and specificity of O?GlcNAc transferase. The EMBO journal, 27(20), pp.2780-2788.

Corresponding AuthorDivision of Biological Chemistry & Drug Discovery, College of Life Sciences, University of Dundee, Dundee, UK.
Reference Martinez-Fleites, C., Macauley, M.S., He, Y., Shen, D.L., Vocadlo, D.J. and Davies, G.J., 2008. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nature structural & molecular biology, 15(7), pp.764-765.

Corresponding AuthorStructural Biology Laboratory, Department of Chemistry, The University of York, Heslington, York YO10 5YW, UK.