KEGG   ENZYME: 2.4.99.19
Entry
EC 2.4.99.19                Enzyme                                 
Name
undecaprenyl-diphosphooligosaccharide---protein glycotransferase;
PglB
Class
Transferases;
Glycosyltransferases;
Transferring other glycosyl groups
Sysname
tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase
Reaction(IUBMB)
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
Substrate
tritrans,heptacis-undecaprenyl diphosphooligosaccharide;
[protein]-L-asparagine
Product
tritrans,heptacis-undecaprenyl diphosphate [CPD:C19852];
glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
Comment
A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
History
EC 2.4.99.19 created 2012
Orthology
K17251  undecaprenyl-diphosphooligosaccharide---protein glycotransferase
Genes
TDNSuden_1474
SUASaut_1513
SULNFJR47_06870
SULGFJR48_03690
SULCCVO_02645
SPALFM071_07115
SSEIFJR45_04540
SBALHUE88_02955
SMASHUE87_09400
SMAXFJR03_03615
SAQTGJV85_04745
SKUSulku_2413
SULRB649_10060
CJECj1126c(pglB)
CJBBN148_1126c(pglB)
CJJCJJ81176_1143(pglB)
CJUC8J_1066(wlaF)
CJNICDCCJ07001_1083
CJICJSA_1068(pglB)
CJMCJM1_1104(wlaF)
CJSCJS3_1172(pglB)
CJPA911_05455
CJEJN564_01094
CJEUN565_01137
CJENN755_01130
CJEIN135_01163
CJERH730_06600
CJVMTVDSCj20_1129(pglB)
CJYQZ67_01204(pglB_2)
CJQUC78_1083(pglB)
CJLPJ17_05770
CJWPJ18_05585
CJRCJE1268(pglB)
CJDJJD26997_0595(pglB)
CJZM635_01335
CJXBN867_11170
CFFCFF8240_1383
CFTCFF04554_1398(pglB)
CFVCFVI03293_1421(pglB)
CFXCFV97608_1521(pglB)
CFZCSG_15200
CAMPCFT03427_1346(pglB)
CFPCR44_06810
CCVCCV52592_1213(pglB)
CHACHAB381_0954
CCOCCC13826_0452(pglB)
CCOCCCON33237_1465(pglB)
CLACLA_1253(pglB)
CLRUPTC16701_1236(pglB)
CLMUPTC16712_1254(pglB)
CLQUPTC4110_1238(pglB)
CLNUPTC3659_1473(pglB)
CLLCONCH_1204(pglB)
CCOLBN865_10020
CCCG157_03305
CCQN149_1067
CCFYSQ_03340
CCYYSS_06095
CCOIYSU_03375
CCOFVC76_05525(pglB)
CCOOATE51_01352(pglB)
CAJCIG1485E_1392(pglB)
CISCINS_1218(pglB)
CVOCVOL_1232(pglB)
CPELCPEL_1359(pglB)
CAMRCAQ16704_1264(pglB)
CSMCSUB8521_1440(pglB)
CSFCSUB8523_1536(pglB)
CGRACGRAC_1490(pglB)
CURECUREO_1374(pglB)
CHYOCHH_0377(pglB)
CHVCHELV3228_0554(pglB)
CSPFCSF_0893(pglB)
CPINCPIN18020_0862(pglB)
CCUNCCUN_1171(pglB)
CLXCLAN_0354(pglB)
CAVICAV_0416(pglB)
CHWA2J15_001350
CAMZCVIC12175_1316(pglB)
CAMYCSUIS_0199(pglB)
COJCORN_1323(pglB)
CUXCUP3940_1137(pglB)
CRXCRECT_1676(pglB)
CGEOCGEO_1574(pglB)
CBLACBLAS_0330(pglB)
CCORCCORG_0293(pglB)
CARMCARM_1286(pglB)
CMUCCMCT_0317(pglB)
CSHOCSHOW_1518(pglB)
CINFCINF_0352(pglB)
CNVCNZW441b_1129(pglB)
CVUCVULP_0492(pglB)
SDLSdel_1767
SBASulba_1853
SMULSMUL_2464
SHALSHALO_2210
SULSSdiek1_2290
SULJSJPD1_2224
HTMRZR91_00680
HCJHCR_14870(pglB)
SMABLN246_00615
 » show all
Reference
1  [PMID:20007322]
  Authors
Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D
  Title
Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases.
  Journal
J Biol Chem 285:4941-50 (2010)
DOI:10.1074/jbc.M109.081752
  Sequence
[cjr:CJE1268]
Reference
2  [PMID:21677752]
  Authors
Lizak C, Gerber S, Numao S, Aebi M, Locher KP
  Title
X-ray structure of a bacterial oligosaccharyltransferase.
  Journal
Nature 474:350-5 (2011)
DOI:10.1038/nature10151
  Sequence
[cla:CLA_1253]
Other DBs
ExplorEnz - The Enzyme Database: 2.4.99.19
IUBMB Enzyme Nomenclature: 2.4.99.19
ExPASy - ENZYME nomenclature database: 2.4.99.19
BRENDA, the Enzyme Database: 2.4.99.19

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