KEGG   ENZYME: 2.4.1.384
Entry
EC 2.4.1.384                Enzyme                                 
Name
NDP-glycosyltransferase;
yjiC (gene name)
Class
Transferases;
Glycosyltransferases;
Hexosyltransferases
Sysname
NDP-glycose:acceptor glycosyltransferase
Reaction(IUBMB)
an NDP-glycose + an acceptor = a glycosylated acceptor + NDP
Substrate
NDP-glycose;
acceptor [CPD:C00028]
Product
glycosylated acceptor;
NDP [CPD:C00454]
Comment
The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase. It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalysing O-, N-, or S-glycosylation. While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine.
History
EC 2.4.1.384 created 2021
Orthology
K25230  NDP-glycosyltransferase
Genes
BSUBSU12220(yjiC)
BSRI33_1374
BSLA7A1_0231
BSHBSU6051_12220(yjiC)
BSYI653_06230
BSUTBSUB_01330(yjiC)
BSULBSUA_01330(yjiC)
BSUSQ433_06955
BSOBSNT_07692(yjiC)
BSNBSn5_18070
BSQB657_12220(yjiC)
BSXC663_1253(yjiC)
BSPU712_06330
BSSBSUW23_06215(yjiC)
BSTGYO_1529
BLIBL00446(yjiC)
BLDBLi01948(yjiC)
BLHBaLi_c19830(yjiC)
BAYRBAM_012300
BAQBACAU_1181(yjiC)
BYABANAU_1162(yjiC)
BAMPB938_06275
BQYMUS_1310(yjiC)
BAMLBAM5036_1136(yjiC)
BAMARBAU_1185(yjiC)
BAMNBASU_1164(yjiC)
BAMBBAPNAU_2561(yjiC)
BAMTAJ82_06895
BAMYV529_11730
BMPNG74_01252(oleD_2)
BAOBAMF_1309(yjiC)
BAZBAMTA208_11035(yjiC)
BQLLL3_01317(yjiC)
BXHBAXH7_02259(yjiC)
BAMIKSO_013425
BAMCU471_12310
BAMFU722_06380
BSIACWD84_15195
BAEBATR1942_03760
BVMB9C48_06160
BSONS101395_02951
BHTDIC78_03385
BMOJHC660_12840(ppuG)
BTEQG4P54_06460
BIQAN935_06335
BJSMY9_1334
BACPSB24_03660
BACBOY17_09250
BACYQF06_05090
BACLBS34A_13530(yjiC)
BALMBsLM_1284
BGYBGLY_2157
BACSAUL54_04470
BITBIS30_16840
BGIBGM20_00385
PSABPSAB_16875
PDUPDUR_18615
PSOPKP014_23270
CPASClopa_1820
AACXDEACI_0885
SCHFIPT68_29230
 » show all
Reference
1  [PMID:23974133]
  Authors
Pandey RP, Parajuli P, Koirala N, Park JW, Sohng JK.
  Title
Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC.
  Journal
Appl Environ Microbiol 79:6833-8 (2013)
DOI:10.1128/AEM.02057-13
Reference
2  [PMID:24893262]
  Authors
Pandey RP, Gurung RB, Parajuli P, Koirala N, Tuoi le T, Sohng JK.
  Title
Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids.
  Journal
Carbohydr Res 393:26-31 (2014)
DOI:10.1016/j.carres.2014.03.011
  Sequence
[bld:BLi01948]
Reference
3  [PMID:25239890]
  Authors
Pandey RP, Parajuli P, Shin JY, Lee J, Lee S, Hong YS, Park YI, Kim JS, Sohng JK.
  Title
Enzymatic Biosynthesis of Novel Resveratrol Glucoside and Glycoside Derivatives.
  Journal
Appl Environ Microbiol 80:7235-43 (2014)
DOI:10.1128/AEM.02076-14
  Sequence
[bld:BLi01948]
Reference
4  [PMID:24949266]
  Authors
Parajuli P, Pandey RP, Koirala N, Yoon YJ, Kim BG, Sohng JK.
  Title
Enzymatic synthesis of epothilone A glycosides.
  Journal
AMB Express 4:31 (2014)
DOI:10.1186/s13568-014-0031-1
  Sequence
[bld:BLi01948]
Reference
5  [PMID:27444326]
  Authors
Pandey RP, Parajuli P, Gurung RB, Sohng JK.
  Title
Donor specificity of YjiC glycosyltransferase determines the conjugation of cytosolic NDP-sugar in in vivo glycosylation reactions.
  Journal
Enzyme Microb Technol 91:26-33 (2016)
DOI:10.1016/j.enzmictec.2016.05.006
Reference
6  [PMID:32238768]
  Authors
Bashyal P, Thapa SB, Kim TS, Pandey RP, Sohng JK.
  Title
Exploring the Nucleophilic N- and S-Glycosylation Capacity of Bacillus licheniformis YjiC Enzyme.
  Journal
J Microbiol Biotechnol 30:1092-1096 (2020)
DOI:10.4014/jmb.2001.01024
Other DBs
ExplorEnz - The Enzyme Database: 2.4.1.384
IUBMB Enzyme Nomenclature: 2.4.1.384
ExPASy - ENZYME nomenclature database: 2.4.1.384
BRENDA, the Enzyme Database: 2.4.1.384

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