SitesBLAST
Comparing WP_053768520.1 NCBI__GCF_001280255.1:WP_053768520.1 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)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
96% identity, 100% coverage: 1:405/405 of query aligns to 1:405/405 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 (= T47) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E74) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G135) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R150) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D154) 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 (= D174) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D182) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
48% identity, 99% coverage: 2:403/405 of query aligns to 1:396/397 of 5yeiC
- binding lysine: M342 (≠ L349), H345 (≠ A352), A346 (≠ P353), G347 (≠ E354), V348 (≠ I355), A349 (≠ P356), S350 (≠ A357)
- binding threonine: T265 (≠ Q271), P266 (= P272), A269 (= A275), Q288 (= Q294), N362 (= N369), I363 (= I370)
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)
47% identity, 99% coverage: 1:402/405 of query aligns to 1:407/421 of P26512
- G277 (= G273) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A275) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q294) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ P297) 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 (≠ I355) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ P356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K358) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ M359) 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)
47% identity, 99% coverage: 1:402/405 of query aligns to 1:407/421 of P41398
- D345 (≠ A340) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
48% identity, 99% coverage: 2:400/405 of query aligns to 1:404/585 of 3l76A
- binding lysine: D286 (≠ A288), I287 (≠ V289), D288 (= D290), M353 (≠ L349), R356 (≠ A352), I359 (= I355), S380 (= S376), E381 (= E377)
- binding threonine: R269 (≠ Q271), V272 (≠ I274), A273 (= A275), Q292 (= Q294), N373 (= N369), I374 (= I370)
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)
45% identity, 99% coverage: 1:402/405 of query aligns to 1:390/392 of 3aawC
- binding lysine: K7 (= K7), S41 (= S41), G136 (= G152), S137 (= S153), D138 (= D154), M337 (≠ L349), H340 (≠ A352), T344 (≠ P356), S364 (= S376)
- binding threonine: K258 (≠ Q271), G260 (= G273), E261 (≠ I274), A262 (= A275), Q281 (= Q294), N357 (= N369), I358 (= I370)
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
95% identity, 38% coverage: 249:401/405 of query aligns to 1:153/153 of 2dt9A
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
42% identity, 99% coverage: 2:402/405 of query aligns to 1:369/370 of 3ab4A
- binding lysine: M316 (≠ L349), H319 (≠ A352), P320 (= P353), V322 (≠ I355), T323 (≠ P356), S343 (= S376), E344 (= E377)
- binding threonine: K239 (≠ Q271), G241 (= G273), E242 (≠ I274), A243 (= A275), Q262 (= Q294), N336 (= N369), I337 (= I370)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
34% identity, 95% coverage: 15:400/405 of query aligns to 57:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T173), D230 (= D174), V231 (≠ T175), Y235 (= Y179), T237 (= T181), D238 (= D182), P239 (= P183), R240 (≠ H184), K265 (≠ R209), V266 (= V210)
- binding aspartic acid: F192 (= F136), R206 (= R150), G207 (= G151), S209 (= S153)
Sites not aligning to the query:
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
33% identity, 95% coverage: 15:400/405 of query aligns to 57:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T173), D230 (= D174), Y235 (= Y179), D238 (= D182), P239 (= P183), R240 (≠ H184), K265 (≠ R209), V266 (= V210)
- binding aspartic acid: E129 (= E74), F192 (= F136), R206 (= R150), G207 (= G151), S209 (= S153)
Sites not aligning to the query:
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
34% identity, 95% coverage: 15:400/405 of query aligns to 57:456/458 of 3c1nA
Sites not aligning to the query:
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 98% coverage: 4:400/405 of query aligns to 5:458/470 of 2cdqA