SitesBLAST
Comparing CA265_RS09655 CA265_RS09655 aspartate kinase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
35% identity, 100% coverage: 3:437/437 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S35), A41 (= A36), T46 (= T41), E124 (= E119), M327 (= M314), Q330 (≠ A317), F333 (= F320), L334 (= L321), S347 (≠ P334), V348 (≠ I335), D349 (= D336)
- binding s-adenosylmethionine: G345 (≠ K332), I346 (≠ T333), S347 (≠ P334), W368 (vs. gap), S369 (vs. gap), R370 (vs. gap), L372 (vs. gap), E376 (≠ H354)
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
34% identity, 99% coverage: 5:437/437 of query aligns to 6:447/447 of 2j0xA
- binding aspartic acid: F182 (≠ Y181), G197 (= G196), G198 (= G197), S199 (= S198), D200 (= D199)
- binding lysine: M316 (= M314), S319 (≠ A317), F322 (= F320), L323 (= L321), S336 (≠ P334), V337 (≠ I335), D338 (= D336), S343 (= S341), E344 (= E342)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
34% identity, 99% coverage: 5:437/437 of query aligns to 6:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T218), D220 (= D219), I224 (≠ M223), Y225 (≠ H224), D228 (= D227), R230 (= R229), K255 (= K254), V256 (≠ I255)
- binding aspartic acid: S37 (= S35), T43 (= T41), E117 (= E119), F182 (≠ Y181), R196 (= R195), G197 (= G196), S199 (= S198)
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)
34% identity, 99% coverage: 5:437/437 of query aligns to 8:449/449 of P08660
- K8 (= K5) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E119) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R195) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D199) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
30% identity, 100% coverage: 3:437/437 of query aligns to 3:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T218), D230 (= D219), V231 (≠ I220), Y235 (≠ H224), T237 (≠ N226), D238 (= D227), P239 (= P228), R240 (= R229), K265 (= K254), V266 (≠ I255)
- binding aspartic acid: S39 (= S35), T45 (= T41), F192 (≠ Y181), R206 (= R195), G207 (= G196), S209 (= S198)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
30% identity, 100% coverage: 3:437/437 of query aligns to 3:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S35), T229 (= T218), D230 (= D219), Y235 (≠ H224), D238 (= D227), P239 (= P228), R240 (= R229), K265 (= K254), V266 (≠ I255)
- binding aspartic acid: T45 (= T41), E129 (= E119), F192 (≠ Y181), R206 (= R195), G207 (= G196), S209 (= S198)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
30% identity, 100% coverage: 3:437/437 of query aligns to 3:458/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (= T9), S10 (= S10), W227 (= W217), T228 (= T218), D229 (= D219), A406 (≠ K387), I409 (≠ F390), A410 (= A391), N423 (≠ P402), I424 (= I403), Q429 (≠ Y408), E433 (≠ N412)
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: 5:436/437 of query aligns to 93:552/916 of O81852
- I441 (= I338) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (vs. gap) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I406) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (≠ Y408) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 100% coverage: 3:437/437 of query aligns to 5:438/439 of 3tviE
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 61% coverage: 173:437/437 of query aligns to 203:496/519 of O60163
- S326 (≠ K294) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
26% identity, 99% coverage: 3:433/437 of query aligns to 3:426/429 of 3tviA
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
30% identity, 85% coverage: 61:432/437 of query aligns to 16:390/397 of 5yeiC
- binding lysine: M342 (≠ S385), H345 (= H388), A346 (vs. gap), G347 (= G389), V348 (≠ F390), A349 (= A391), S350 (= S392)
- binding threonine: T265 (≠ L315), P266 (≠ L316), A269 (≠ G319), Q288 (≠ T340), N362 (≠ P402), I363 (= I403)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
22% identity, 99% coverage: 3:433/437 of query aligns to 5:398/405 of P61489
- K7 (= K5) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G7) mutation to M: Loss of aspartokinase activity.
- G10 (= G8) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S35) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A36) mutation to S: Loss of aspartokinase activity.
- T47 (= T41) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E111) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G180) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R195) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D199) 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 (= D219) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D227) 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)
26% identity, 77% coverage: 98:434/437 of query aligns to 53:387/392 of 3aawC
- binding lysine: G136 (= G197), S137 (= S198), D138 (= D199), M337 (≠ G384), H340 (≠ K387), T344 (≠ A391), S364 (= S411)
- binding threonine: K258 (vs. gap), G260 (= G319), E261 (≠ F320), A262 (≠ L321), Q281 (vs. gap), N357 (≠ R404), I358 (≠ M405)
Sites not aligning to the query:
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)
26% identity, 77% coverage: 98:435/437 of query aligns to 53:405/421 of P26512
- G277 (= G319) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ L321) 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 (vs. gap) 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 (≠ F390) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A391) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R393) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ V394) 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)
27% identity, 77% coverage: 98:435/437 of query aligns to 53:405/421 of P41398
- D345 (≠ S375) 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)
30% identity, 53% coverage: 110:341/437 of query aligns to 64:293/585 of 3l76A
Sites not aligning to the query:
- binding lysine: 353, 356, 359, 380, 381, 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 373, 374, 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)
27% identity, 55% coverage: 196:434/437 of query aligns to 116:366/370 of 3ab4A
- binding lysine: M316 (≠ G384), H319 (≠ K387), P320 (≠ H388), V322 (≠ F390), T323 (≠ A391), S343 (= S411), E344 (≠ N412)
- binding threonine: K239 (vs. gap), G241 (= G319), E242 (≠ F320), A243 (≠ L321), Q262 (vs. gap), N336 (≠ R404), I337 (≠ M405)
Query Sequence
>CA265_RS09655 CA265_RS09655 aspartate kinase
MKILKFGGTSVGSPERMTKLLDIINPNEEQIVVLSAVSGTTNSLVEIANYFLAGDKKKGS
ECVENLYQKYKTFVVELLPAAEFQEQGNEVIDYHFGFLAGLANDIFTSIEEKVVLAQGEL
LSTTLYHIYLKSIGVPSVLLPALDFMKTDEDNEPDIPFTTKHLTPLLEQHKDNKLFITQG
YICRNSFGEVDNLRRGGSDYTASLLGAAILAEEVQIWTDIDGMHNNDPRIVKGTKPIAQL
SFDEAAELAYFGAKILHPQSVFPAQKYKIPVRLLNTMEPSAAGTLITHDSERGKIKSIAA
KDGITAIRIQSSRMLLAYGFLRRVFEVFERYKTPIDMITTSEVAVSLTIDETAHLPQIIE
ELESFGTVEVDTNHSIVCVVGDFGSEKHGFASRVLEGLKHIPIRMISYGGSNYNVSLLIL
SEYKTEALRSLHNRLFE
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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