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. 2012 Feb 10;287(14):10780–10790. doi: 10.1074/jbc.M111.322974

TABLE 2.

Conserved active site residues in AfUGM compared to prokaryotic UGMs

The OH group of Tyr-317 makes the same hydrogen bonding interaction with the α-phosphate of the nucleotide as OH group of Tyr-209 in DrUGM and Tyr-185 in KpUGM (single letter amino acid abbreviations are indicated).

AfUGM DrUGM KpUGM EcUGM MtUGM
H63 H85 H60 H56 H65
F66 H88 H63 H59 H68
R91 H109 N84 N80 H89
F158 F175 F151 L147 F157
M159 F176 F152 I148 V158
Y162 Y179 Y155 Y151 Y161
N163 T180 T156 T152 T162
W167 W184 W160 W156 W166
R182 R198 R174 R170 R180
P206 Y209 Y185 Y181 Y191
N207 F210 F186 F182 F192
W315 T294 V268 V266 T162
Y317 N296 N270 N268 N282
R327 R305 R280 R278 R292
E373 E325 E301 E298 E315
Y419 Y335 Y314 Y311 Y328
R447 R364 R343 R340 R360
Y453 Y370 Y349 Y346 Y366
N457 N372 D351 D348 D368
Q458 M373 M352 M349 M369