SitesBLAST
Comparing 7023909 FitnessBrowser__ANA3:7023909 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
48% identity, 97% coverage: 12:416/418 of query aligns to 2:396/397 of 5yeiC
- binding lysine: M342 (≠ L362), H345 (≠ K365), A346 (≠ V366), G347 (= G367), V348 (≠ L368), A349 (≠ L369), S350 (≠ T370)
- binding threonine: T265 (≠ S283), P266 (≠ S284), A269 (≠ Y287), Q288 (≠ N310), N362 (≠ H382), I363 (≠ A383)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
41% identity, 97% coverage: 12:417/418 of query aligns to 3:404/405 of P61489
- K7 (= K16) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G18) mutation to M: Loss of aspartokinase activity.
- G10 (= G19) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S50) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A51) mutation to S: Loss of aspartokinase activity.
- T47 (= T56) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E83) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G144) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R159) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D163) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.; mutation to N: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- D174 (= D183) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D191) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
41% identity, 97% coverage: 12:415/418 of query aligns to 3:407/421 of P41398
- D345 (≠ A353) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 2 papers)
41% identity, 97% coverage: 12:415/418 of query aligns to 3:407/421 of P26512
- G277 (≠ E285) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ Y287) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (≠ N310) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (= S313) mutation to F: Absence of inhibition upon addition of threonine and lysine or lysine alone.; mutation to Y: Feedback-resistant and enhanced expression of the asd gene.
- V360 (≠ L368) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ L369) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K371) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ M372) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
40% identity, 96% coverage: 12:413/418 of query aligns to 2:404/585 of 3l76A
- binding lysine: D286 (= D300), I287 (≠ V301), D288 (≠ E302), M353 (≠ L362), R356 (≠ K365), I359 (≠ L368), S380 (= S389), E381 (= E390)
- binding threonine: R269 (≠ S283), V272 (≠ H286), A273 (≠ Y287), Q292 (≠ K308), N373 (≠ H382), I374 (≠ A383)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
40% identity, 97% coverage: 12:415/418 of query aligns to 3:390/392 of 3aawC
- binding lysine: K7 (= K16), S41 (= S50), G136 (= G161), S137 (= S162), D138 (= D163), M337 (≠ L362), H340 (≠ K365), T344 (≠ L369), S364 (= S389)
- binding threonine: K258 (≠ S283), G260 (≠ E285), E261 (≠ H286), A262 (≠ Y287), Q281 (≠ N310), N357 (≠ H382), I358 (≠ A383)
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
36% identity, 97% coverage: 12:415/418 of query aligns to 2:369/370 of 3ab4A
- binding lysine: M316 (≠ L362), H319 (≠ K365), P320 (≠ V366), V322 (≠ L368), T323 (≠ L369), S343 (= S389), E344 (= E390)
- binding threonine: K239 (≠ S283), G241 (≠ E285), E242 (≠ H286), A243 (≠ Y287), Q262 (≠ K308), N336 (≠ H382), I337 (≠ A383)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
30% identity, 96% coverage: 14:413/418 of query aligns to 3:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G18), T229 (= T182), D230 (= D183), V231 (= V184), Y235 (≠ F188), T237 (= T190), D238 (= D191), P239 (= P192), R240 (≠ N193), K265 (= K218), V266 (= V219)
- binding aspartic acid: S39 (= S50), T45 (= T56), F192 (= F145), R206 (= R159), G207 (= G160), S209 (= S162)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
30% identity, 96% coverage: 14:413/418 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G18), G8 (= G19), T9 (= T20), S10 (= S21), W227 (≠ F181), T228 (= T182), D229 (= D183), A406 (≠ K365), I409 (≠ L368), A410 (≠ L369), N423 (≠ H382), I424 (≠ A383), Q429 (vs. gap), E433 (= E390)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
30% identity, 96% coverage: 14:413/418 of query aligns to 3:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K16), G7 (= G18), G8 (= G19), S39 (= S50), T229 (= T182), D230 (= D183), Y235 (≠ F188), D238 (= D191), P239 (= P192), R240 (≠ N193), K265 (= K218), V266 (= V219)
- binding aspartic acid: T45 (= T56), E129 (= E83), F192 (= F145), R206 (= R159), G207 (= G160), S209 (= S162)
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)
32% identity, 96% coverage: 10:410/418 of query aligns to 2:444/449 of P08660