SitesBLAST
Comparing PfGW456L13_1981 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1981 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)
89% identity, 98% coverage: 2:407/413 of query aligns to 1:397/397 of 5yeiC
- binding lysine: M342 (= M352), H345 (= H355), A346 (= A356), G347 (= G357), V348 (= V358), A349 (= A359), S350 (= S360)
- binding threonine: T265 (≠ I275), P266 (= P276), A269 (= A279), Q288 (= Q298), N362 (= N372), I363 (= I373)
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)
48% identity, 98% coverage: 1:405/413 of query aligns to 1:407/421 of P26512
- G277 (= G277) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A279) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q298) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ A301) 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 (= V358) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A359) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R361) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ M362) 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)
48% identity, 98% coverage: 1:405/413 of query aligns to 1:407/421 of P41398
- D345 (≠ A343) 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)
48% identity, 98% coverage: 1:406/413 of query aligns to 1:403/405 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 (= E76) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G137) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R152) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D156) 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 (= D176) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D184) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
46% identity, 98% coverage: 1:405/413 of query aligns to 1:390/392 of 3aawC
- binding lysine: K7 (= K7), S41 (= S41), G136 (= G154), S137 (= S155), D138 (= D156), M337 (= M352), H340 (= H355), T344 (≠ A359), S364 (= S379)
- binding threonine: K258 (≠ I275), G260 (= G277), E261 (≠ V278), A262 (= A279), Q281 (= Q298), N357 (= N372), I358 (= I373)
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
47% identity, 99% coverage: 2:411/413 of query aligns to 1:414/585 of 3l76A
- binding lysine: D286 (≠ E292), I287 (≠ V293), D288 (= D294), M353 (= M352), R356 (≠ H355), I359 (≠ V358), S380 (= S379), E381 (= E380)
- binding threonine: R269 (≠ I275), V272 (= V278), A273 (= A279), Q292 (= Q298), N373 (= N372), I374 (= I373)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
43% identity, 98% coverage: 2:405/413 of query aligns to 1:369/370 of 3ab4A
- binding lysine: M316 (= M352), H319 (= H355), P320 (≠ A356), V322 (= V358), T323 (≠ A359), S343 (= S379), E344 (= E380)
- binding threonine: K239 (≠ I275), G241 (= G277), E242 (≠ V278), A243 (= A279), Q262 (= Q298), N336 (= N372), I337 (= I373)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
34% identity, 97% coverage: 5:403/413 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G9), G8 (= G10), T9 (= T11), S10 (= S12), W227 (≠ Y174), T228 (= T175), D229 (= D176), A406 (≠ H355), I409 (≠ V358), A410 (= A359), N423 (= N372), I424 (= I373), Q429 (vs. gap), E433 (= E380)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
35% identity, 83% coverage: 61:403/413 of query aligns to 114:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T175), D230 (= D176), V231 (= V177), Y235 (= Y181), T237 (= T183), D238 (= D184), P239 (= P185), R240 (= R186), K265 (= K211), V266 (= V212)
- binding aspartic acid: F192 (= F138), R206 (= R152), G207 (= G153), S209 (= S155)
Sites not aligning to the query:
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
34% identity, 83% coverage: 61:403/413 of query aligns to 114:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T175), D230 (= D176), Y235 (= Y181), D238 (= D184), P239 (= P185), R240 (= R186), K265 (= K211), V266 (= V212)
- binding aspartic acid: E129 (= E76), F192 (= F138), R206 (= R152), G207 (= G153), S209 (= S155)
Sites not aligning to the query:
2re1A Crystal structure of aspartokinase alpha and beta subunits
58% identity, 37% coverage: 255:405/413 of query aligns to 2:148/148 of 2re1A
4go7X The regulatory subunit of aspartate kinase in complex with threonine from mycobacterium tuberculosis (see paper)
47% identity, 38% coverage: 250:407/413 of query aligns to 4:161/165 of 4go7X
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)
27% identity, 97% coverage: 5:405/413 of query aligns to 91:553/916 of O81852