SitesBLAST
Comparing WP_078430740.1 NCBI__GCF_002019605.1:WP_078430740.1 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)
P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 2 papers)
37% identity, 97% coverage: 1:403/414 of query aligns to 1:410/421 of P26512
- G277 (= G279) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ Q284) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (vs. gap) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ N304) 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 (= V353) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (= T354) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ I357) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
37% identity, 97% coverage: 1:403/414 of query aligns to 1:410/421 of P41398
- D345 (≠ T334) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
37% identity, 97% coverage: 1:402/414 of query aligns to 1:404/405 of P61489
- K7 (= K7) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G9) mutation to M: Loss of aspartokinase activity.
- G10 (= G10) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S41) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A42) mutation to S: Loss of aspartokinase activity.
- T47 (= T52) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E77) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G138) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R153) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D157) 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 (= D177) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D185) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
36% identity, 96% coverage: 3:398/414 of query aligns to 2:404/585 of 3l76A
- binding lysine: D286 (≠ S297), I287 (≠ V298), D288 (= D299), M353 (= M347), R356 (≠ V350), I359 (≠ V353), S380 (= S374), E381 (≠ H375)
- binding threonine: R269 (≠ K277), V272 (≠ L283), A273 (≠ Q284), Q292 (vs. gap), N373 (≠ Q367), I374 (= I368)
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)
36% identity, 97% coverage: 1:400/414 of query aligns to 1:390/392 of 3aawC
- binding lysine: K7 (= K7), S41 (= S41), G136 (= G155), S137 (= S156), D138 (= D157), M337 (= M347), H340 (≠ V350), T344 (= T354), S364 (= S374)
- binding threonine: K258 (= K277), G260 (= G279), E261 (≠ Q280), A262 (≠ Q284), Q281 (vs. gap), N357 (≠ Q367), I358 (= I368)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
35% identity, 96% coverage: 3:401/414 of query aligns to 2:396/397 of 5yeiC
- binding lysine: M342 (= M347), H345 (≠ V350), A346 (≠ P351), G347 (= G352), V348 (= V353), A349 (≠ T354), S350 (≠ A355)
- binding threonine: T265 (≠ Q280), P266 (≠ Y281), A269 (≠ Q284), Q288 (vs. gap), N362 (≠ Q367), I363 (= I368)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
31% identity, 93% coverage: 12:398/414 of query aligns to 82:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T176), D230 (= D177), V231 (= V178), Y235 (≠ M182), T237 (≠ A184), D238 (= D185), P239 (= P186), R240 (= R187), K265 (= K212), V266 (= V213)
- binding aspartic acid: F192 (= F139), R206 (= R153), G207 (= G154), S209 (= S156)
Sites not aligning to the query:
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
31% identity, 93% coverage: 12:398/414 of query aligns to 82:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T176), D230 (= D177), Y235 (≠ M182), D238 (= D185), P239 (= P186), R240 (= R187), K265 (= K212), V266 (= V213)
- binding aspartic acid: E129 (= E77), F192 (= F139), R206 (= R153), G207 (= G154), S209 (= S156)
Sites not aligning to the query:
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
33% identity, 80% coverage: 67:398/414 of query aligns to 118:456/458 of 3c1nA
Sites not aligning to the query:
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
33% identity, 96% coverage: 3:400/414 of query aligns to 2:369/370 of 3ab4A
- binding lysine: M316 (= M347), H319 (≠ V350), P320 (= P351), V322 (= V353), T323 (= T354), S343 (= S374), E344 (≠ H375)
- binding threonine: K239 (= K277), G241 (= G279), E242 (≠ Q280), A243 (≠ Q284), Q262 (≠ I303), N336 (≠ Q367), I337 (= I368)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
30% identity, 81% coverage: 62:398/414 of query aligns to 109:458/470 of 2cdqA
- binding lysine: E124 (= E77), M327 (vs. gap), Q330 (= Q280), F333 (≠ L283), L334 (≠ Q284), S347 (= S297), V348 (= V298), D349 (= D299)
- binding s-adenosylmethionine: G345 (≠ R295), I346 (= I296), S347 (= S297), W368 (vs. gap), S369 (vs. gap), R370 (vs. gap), L372 (≠ V312), E376 (≠ V316)
Sites not aligning to the query:
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 96% coverage: 1:399/414 of query aligns to 1:437/439 of 3tviE