SitesBLAST
Comparing WP_020563310.1 NCBI__GCF_000372865.1:WP_020563310.1 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)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
75% identity, 99% coverage: 2:403/406 of query aligns to 1:396/397 of 5yeiC
- binding lysine: M342 (= M349), H345 (= H352), A346 (= A353), G347 (= G354), V348 (≠ I355), A349 (= A356), S350 (= S357)
- binding threonine: T265 (≠ K272), P266 (= P273), A269 (= A276), Q288 (= Q295), N362 (= N369), I363 (= I370)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
49% identity, 100% coverage: 1:405/406 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.
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)
50% identity, 99% coverage: 1:402/406 of query aligns to 1:407/421 of P26512
- G277 (= G274) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A276) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q295) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ A298) 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 (≠ A356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ T358) 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)
50% identity, 99% coverage: 1:402/406 of query aligns to 1:407/421 of P41398
- D345 (≠ V340) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
48% identity, 99% coverage: 1:402/406 of query aligns to 1:390/392 of 3aawC
- binding lysine: K7 (= K7), S41 (= S41), G136 (= G152), S137 (= S153), D138 (= D154), M337 (= M349), H340 (= H352), T344 (≠ A356), S364 (= S376)
- binding threonine: K258 (= K272), G260 (= G274), E261 (≠ V275), A262 (= A276), Q281 (= Q295), N357 (= N369), I358 (= I370)
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
47% identity, 98% coverage: 2:400/406 of query aligns to 1:404/585 of 3l76A
- binding lysine: D286 (≠ E289), I287 (≠ V290), D288 (= D291), M353 (= M349), R356 (≠ H352), I359 (= I355), S380 (= S376), E381 (= E377)
- binding threonine: R269 (≠ K272), V272 (= V275), A273 (= A276), Q292 (= Q295), 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
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
45% identity, 99% coverage: 2:402/406 of query aligns to 1:369/370 of 3ab4A
- binding lysine: M316 (= M349), H319 (= H352), P320 (≠ A353), V322 (≠ I355), T323 (≠ A356), S343 (= S376), E344 (= E377)
- binding threonine: K239 (= K272), G241 (= G274), E242 (≠ V275), A243 (= A276), Q262 (= Q295), N336 (= N369), I337 (= I370)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
35% identity, 98% coverage: 5:400/406 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G9), G8 (= G10), T9 (= T11), S10 (= S12), W227 (≠ F172), T228 (= T173), D229 (= D174), A406 (≠ H352), I409 (= I355), A410 (= A356), N423 (= N369), I424 (= I370), Q429 (vs. gap), E433 (= E377)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
35% identity, 94% coverage: 20:400/406 of query aligns to 77:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T173), D230 (= D174), V231 (= V175), Y235 (= Y179), T237 (= T181), D238 (= D182), P239 (= P183), R240 (= R184), K265 (= K209), 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)
35% identity, 94% coverage: 20:400/406 of query aligns to 77:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T173), D230 (= D174), Y235 (= Y179), D238 (= D182), P239 (= P183), R240 (= R184), K265 (= K209), V266 (= V210)
- binding aspartic acid: E129 (= E74), F192 (= F136), R206 (= R150), G207 (= G151), S209 (= S153)
Sites not aligning to the query:
2re1A Crystal structure of aspartokinase alpha and beta subunits
58% identity, 37% coverage: 252:402/406 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)
45% identity, 39% coverage: 246:403/406 of query aligns to 3:160/165 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)
28% identity, 99% coverage: 5:404/406 of query aligns to 91:555/916 of O81852
- I441 (= I293) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q295) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I373) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (vs. gap) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
41% identity, 37% coverage: 252:401/406 of query aligns to 3:153/153 of 2dt9A
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
27% identity, 98% coverage: 5:400/406 of query aligns to 6:458/470 of 2cdqA
- binding lysine: S40 (= S41), A41 (= A42), T46 (= T47), E124 (= E74), M327 (≠ V269), Q330 (≠ K272), F333 (≠ V275), L334 (≠ A276), S347 (≠ E289), V348 (= V290), D349 (= D291)
- binding s-adenosylmethionine: G345 (≠ N287), I346 (= I288), S347 (≠ E289), W368 (≠ F305), S369 (≠ T306), R370 (≠ F307), L372 (≠ V309), E376 (≠ D313)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
30% identity, 98% coverage: 3:398/406 of query aligns to 2:443/447 of 2j0xA
- binding aspartic acid: F182 (= F136), G197 (= G151), G198 (= G152), S199 (= S153), D200 (= D154)
- binding lysine: M316 (vs. gap), S319 (≠ K272), F322 (≠ V275), L323 (≠ A276), S336 (≠ E289), V337 (= V290), D338 (= D291), S343 (≠ N296), E344 (≠ I297)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
30% identity, 98% coverage: 3:398/406 of query aligns to 2:443/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T173), D220 (= D174), I224 (≠ V178), Y225 (= Y179), D228 (= D182), R230 (= R184), K255 (= K209), V256 (= V210)
- binding aspartic acid: S37 (= S41), T43 (= T47), E117 (= E74), F182 (= F136), R196 (= R150), G197 (= G151), S199 (= S153)
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)
30% identity, 98% coverage: 3:398/406 of query aligns to 4:445/449 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 (= E74) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R150) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D154) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 83% coverage: 62:397/406 of query aligns to 134:491/519 of O60163
- S326 (= S249) modified: Phosphoserine
- T328 (≠ L251) modified: Phosphothreonine
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
26% identity, 69% coverage: 120:400/406 of query aligns to 154:436/439 of 3tviE
Sites not aligning to the query:
Query Sequence
>WP_020563310.1 NCBI__GCF_000372865.1:WP_020563310.1
MALYVYKFGGTSVGSVERIKAVAEKVKQAHDLGDRIVVVVSAMSGETNRLIALAKDIQKQ
PNARELDVLVSTGEQVTVALLAMALEEIGCPAYSFTGGQVKILTDSSHTKARIRDIDDSR
MRARLDQGNVVVVAGFQGVDEHGNITTLGRGGSDTTAVALAAALKADECLIFTDVDGVYT
TDPRIEPKARRLDKITFEEMLEMASLGSKVLQIRSVEFAGKYNVALRVLSSFTEGKGTLI
TYEDSQMESALISGIAFNRDEAKLTITGVPDKPGVASRILGPIAEANIEVDMIVQNIAED
DTTDFTFTVHRNDYLRAKESLELTRAELGAKKVTGDDAIVKISIVGVGMRSHAGIASTMF
QALASEGINIKMISTSEIKISVVVDEKYLELAVRTLHSAFKLDQAA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory