SitesBLAST
Comparing 203070 FitnessBrowser__MR1:203070 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
P08660 Lysine-sensitive aspartokinase 3; Aspartate kinase III; AKIII; Lysine-sensitive aspartokinase III; EC 2.7.2.4 from Escherichia coli (strain K12) (see paper)
60% identity, 99% coverage: 3:449/451 of query aligns to 4:449/449 of P08660
- K8 (= K7) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E119) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R198) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D202) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
60% identity, 99% coverage: 3:449/451 of query aligns to 2:447/447 of 2j0xA
- binding aspartic acid: F182 (= F184), G197 (= G199), G198 (= G200), S199 (= S201), D200 (= D202)
- binding lysine: M316 (= M318), S319 (≠ A321), F322 (= F324), L323 (= L325), S336 (= S338), V337 (= V339), D338 (= D340), S343 (= S345), E344 (= E346)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
60% identity, 99% coverage: 3:449/451 of query aligns to 2:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T221), D220 (= D222), I224 (= I226), Y225 (= Y227), D228 (= D230), R230 (= R232), K255 (= K257), V256 (= V258)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E119), F182 (= F184), R196 (= R198), G197 (= G199), S199 (= S201)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
35% identity, 99% coverage: 5:449/451 of query aligns to 3:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G9), T229 (= T221), D230 (= D222), V231 (= V223), Y235 (= Y227), T237 (= T229), D238 (= D230), P239 (= P231), R240 (= R232), K265 (= K257), V266 (= V258)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F184), R206 (= R198), G207 (= G199), S209 (= S201)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
35% identity, 99% coverage: 5:449/451 of query aligns to 3:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K7), G7 (= G9), G8 (= G10), S39 (= S38), T229 (= T221), D230 (= D222), Y235 (= Y227), D238 (= D230), P239 (= P231), R240 (= R232), K265 (= K257), V266 (= V258)
- binding aspartic acid: T45 (= T44), E129 (= E119), F192 (= F184), R206 (= R198), G207 (= G199), S209 (= S201)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
35% identity, 99% coverage: 5:449/451 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G9), G8 (= G10), T9 (= T11), S10 (= S12), W227 (= W220), T228 (= T221), D229 (= D222), A406 (≠ T399), I409 (= I402), A410 (≠ C403), N423 (= N414), I424 (≠ V415), Q429 (= Q420), E433 (≠ P424)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
33% identity, 99% coverage: 5:449/451 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (≠ A39), A41 (≠ S40), T46 (vs. gap), E124 (= E119), M327 (= M318), Q330 (≠ A321), F333 (= F324), L334 (= L325), S347 (= S338), V348 (= V339), D349 (= D340)
- binding s-adenosylmethionine: G345 (≠ K336), I346 (= I337), S347 (= S338), W368 (≠ S361), S369 (≠ G362), R370 (≠ Q363), L372 (= L365), E376 (≠ A369)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 99% coverage: 4:449/451 of query aligns to 16:496/519 of O60163
- S326 (≠ V293) modified: Phosphoserine
- T328 (≠ D295) modified: Phosphothreonine
O81852 Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 98% coverage: 5:448/451 of query aligns to 91:552/916 of O81852
- I441 (= I342) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (vs. gap) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I418) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q420) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
26% identity, 100% coverage: 1:450/451 of query aligns to 1:439/439 of 3tviE