SitesBLAST
Comparing WP_011020190.1 NCBI__GCF_000007345.1:WP_011020190.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
52% identity, 97% coverage: 4:460/472 of query aligns to 3:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G8), T229 (≠ K232), D230 (≠ E233), V231 (= V234), Y235 (≠ M238), T237 (= T240), D238 (= D241), P239 (= P242), R240 (= R243), K265 (≠ N268), V266 (= V269)
- binding aspartic acid: S39 (= S40), T45 (= T46), F192 (= F195), R206 (= R209), G207 (≠ S210), S209 (= S212)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
52% identity, 97% coverage: 4:460/472 of query aligns to 3:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K6), G7 (= G8), G8 (= G9), S39 (= S40), T229 (≠ K232), D230 (≠ E233), Y235 (≠ M238), D238 (= D241), P239 (= P242), R240 (= R243), K265 (≠ N268), V266 (= V269)
- binding aspartic acid: T45 (= T46), E129 (= E130), F192 (= F195), R206 (= R209), G207 (≠ S210), S209 (= S212)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
53% identity, 97% coverage: 4:460/472 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G8), G8 (= G9), T9 (= T10), S10 (= S11), W227 (= W231), T228 (≠ K232), D229 (≠ E233), A406 (≠ T410), I409 (≠ V413), A410 (= A414), N423 (= N427), I424 (= I428), Q429 (= Q433), E433 (≠ Q437)
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)
35% identity, 98% coverage: 1:462/472 of query aligns to 88:553/916 of O81852
- I441 (= I354) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q356) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I431) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q433) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
35% identity, 97% coverage: 4:460/472 of query aligns to 6:458/470 of 2cdqA
- binding lysine: S40 (= S40), A41 (= A41), T46 (= T46), E124 (= E130), M327 (= M330), Q330 (≠ T333), F333 (≠ T336), L334 (≠ V337), S347 (≠ N350), V348 (≠ I351), D349 (≠ V352)
- binding s-adenosylmethionine: G345 (= G348), I346 (≠ V349), S347 (≠ N350), W368 (vs. gap), S369 (vs. gap), R370 (vs. gap), L372 (vs. gap), E376 (≠ A375)
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
32% identity, 97% coverage: 3:462/472 of query aligns to 3:395/397 of 5yeiC
- binding lysine: M342 (= M407), H345 (≠ T410), A346 (≠ P411), G347 (= G412), V348 (= V413), A349 (= A414), S350 (≠ K415)
- binding threonine: T265 (= T333), P266 (≠ V334), A269 (≠ V337), Q288 (= Q356), N362 (= N427), I363 (= I428)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 97% coverage: 3:460/472 of query aligns to 16:494/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
31% identity, 97% coverage: 3:462/472 of query aligns to 4:402/405 of P61489
- K7 (= K6) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
- G9 (= G8) mutation to M: Loss of aspartokinase activity.
- G10 (= G9) mutation to A: Significant decrease in the catalytic efficiency.
- S41 (= S40) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- A42 (= A41) mutation to S: Loss of aspartokinase activity.
- T47 (= T46) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
- E74 (= E102) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G194) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R209) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D213) 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 (≠ E233) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D241) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
30% identity, 97% coverage: 3:460/472 of query aligns to 4:436/439 of 3tviE
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)
32% identity, 97% coverage: 3:462/472 of query aligns to 4:407/421 of P26512
- G277 (= G335) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ V337) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (= S359) 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 (= V413) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A414) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R416) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ V417) 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)
32% identity, 97% coverage: 3:462/472 of query aligns to 4:407/421 of P41398
- D345 (≠ C398) 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)
32% identity, 97% coverage: 3:460/472 of query aligns to 3:404/585 of 3l76A
- binding lysine: D286 (≠ N350), I287 (= I351), D288 (≠ V352), M353 (= M407), R356 (≠ T410), I359 (≠ V413), S380 (= S436), E381 (≠ Q437)
- binding threonine: R269 (≠ T333), V272 (≠ T336), A273 (≠ V337), Q292 (= Q356), N373 (= N427), I374 (= I428)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
31% identity, 96% coverage: 3:457/472 of query aligns to 3:442/447 of 2j0xA
- binding aspartic acid: F182 (= F195), G197 (≠ S210), G198 (= G211), S199 (= S212), D200 (= D213)
- binding lysine: M316 (= M330), S319 (≠ T333), F322 (≠ T336), L323 (≠ V337), S336 (≠ N350), V337 (≠ I351), D338 (≠ V352), S343 (= S359), E344 (= E360)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
31% identity, 96% coverage: 3:457/472 of query aligns to 3:442/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (≠ K232), D220 (≠ E233), I224 (= I237), Y225 (≠ M238), D228 (= D241), R230 (= R243), K255 (≠ N268), V256 (= V269)
- binding aspartic acid: S37 (= S40), T43 (= T46), E117 (= E130), F182 (= F195), R196 (= R209), G197 (≠ S210), S199 (= S212)
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)
31% identity, 96% coverage: 3:457/472 of query aligns to 5:444/449 of P08660
- K8 (= K6) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E130) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R209) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D213) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 97% coverage: 3:460/472 of query aligns to 2:428/429 of 3tviA
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
30% identity, 97% coverage: 3:462/472 of query aligns to 4:390/392 of 3aawC
- binding lysine: K7 (= K6), S41 (= S40), G136 (= G211), S137 (= S212), D138 (= D213), M337 (= M407), H340 (≠ T410), T344 (≠ A414), S364 (= S436)
- binding threonine: K258 (≠ M330), G260 (= G335), E261 (≠ T336), A262 (≠ V337), Q281 (= Q356), N357 (= N427), I358 (= I428)
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
31% identity, 73% coverage: 119:462/472 of query aligns to 62:369/370 of 3ab4A
- binding lysine: M316 (= M407), H319 (≠ T410), P320 (= P411), V322 (= V413), T323 (≠ A414), S343 (= S436), E344 (≠ Q437)
- binding threonine: K239 (≠ M330), G241 (= G335), E242 (≠ T336), A243 (≠ V337), Q262 (= Q356), N336 (= N427), I337 (= I428)
2re1A Crystal structure of aspartokinase alpha and beta subunits
32% identity, 32% coverage: 311:462/472 of query aligns to 2:148/148 of 2re1A
Query Sequence
>WP_011020190.1 NCBI__GCF_000007345.1:WP_011020190.1
MKIVMKFGGTSVGDGKKIRHVAQLLKRYHEEGNQIVVVTSALGGVTDRLLENARLASTKG
KVSLVKEFKTELTNKHHEAVKDAIEDPRVAKEVLQVLDLRIEELEKALIGICYLGELTSR
SIDYISSYGERLAAPIVSGAVRSLGAASIEYTGGEAGIVTTSDYGNARPLEKTYELVLKR
LGCRLESHILVVTGFIGENEDGIITTLGRSGSDFSASILGAALKADEIWLWKEVNGIMTT
DPRIVPEAKTIPQISYAEAMELSYFGANVLHPRTIEPAMREHIPVRVKNTFNPEFPGTLV
VAEKFQCRHVVKAVSLIKNVALINISGAEMPGTVGTVARLFTALARAGVNIVMISQGSSE
SNLSFVVSESHVESALKALHAEFNREIVKEITSDRNVCVVAVVGAGMAGTPGVAKRVFGA
LGNSMINIIMISQGSSQYNISFVVREGDAFAAVKTLHDEFELYNGNGIEKKL
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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