SitesBLAST
Comparing WP_013684026.1 NCBI__GCF_000194625.1:WP_013684026.1 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)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
50% identity, 98% coverage: 4:457/462 of query aligns to 3:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G8), T229 (≠ K232), D230 (≠ E233), V231 (= V234), Y235 (≠ L238), T237 (= T240), D238 (= D241), P239 (= P242), R240 (≠ K243), K265 (= K268), V266 (≠ I269)
- binding aspartic acid: S39 (= S39), T45 (= T45), F192 (= F195), R206 (= R209), G207 (= G210), S209 (= S212)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
50% identity, 98% coverage: 4:457/462 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G8), G8 (= G9), T9 (≠ A10), S10 (= S11), W227 (= W231), T228 (≠ K232), D229 (≠ E233), A406 (≠ T407), I409 (≠ V410), A410 (= A411), N423 (= N424), I424 (≠ V425), Q429 (= Q430), E433 (= E434)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
49% identity, 98% coverage: 4:457/462 of query aligns to 3:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K6), G7 (= G8), G8 (= G9), S39 (= S39), T229 (≠ K232), D230 (≠ E233), Y235 (≠ L238), D238 (= D241), P239 (= P242), R240 (≠ K243), K265 (= K268), V266 (≠ I269)
- binding aspartic acid: T45 (= T45), E129 (= E128), F192 (= F195), R206 (= R209), G207 (= G210), S209 (= S212)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
35% identity, 98% coverage: 4:457/462 of query aligns to 6:458/470 of 2cdqA
- binding lysine: S40 (= S39), A41 (= A40), T46 (= T45), E124 (= E128), M327 (vs. gap), Q330 (vs. gap), F333 (= F330), L334 (≠ M336), S347 (≠ N349), V348 (= V350), D349 (≠ I351)
- binding s-adenosylmethionine: G345 (≠ R347), I346 (≠ V348), S347 (≠ N349), W368 (≠ G372), S369 (≠ R373), R370 (vs. gap), L372 (vs. gap), E376 (≠ V377)
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)
33% identity, 99% coverage: 1:459/462 of query aligns to 88:553/916 of O81852
- I441 (≠ V353) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q355) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I428) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q430) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 98% coverage: 3:457/462 of query aligns to 16:494/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
34% identity, 74% coverage: 118:459/462 of query aligns to 63:395/397 of 5yeiC
- binding lysine: M342 (= M404), H345 (≠ T407), A346 (≠ P408), G347 (= G409), V348 (= V410), A349 (= A411), S350 (≠ G412)
- binding threonine: T265 (≠ F332), P266 (≠ A333), A269 (≠ M336), Q288 (= Q355), N362 (= N424), I363 (≠ V425)
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)
35% identity, 74% coverage: 118:461/462 of query aligns to 64:409/421 of P26512
- G277 (≠ A333) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ V335) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q355) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (= S358) 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 (= V410) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A411) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R413) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ I414) 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)
34% identity, 74% coverage: 118:461/462 of query aligns to 64:409/421 of P41398
- D345 (≠ A395) 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)
35% identity, 74% coverage: 117:457/462 of query aligns to 62:404/585 of 3l76A
- binding lysine: D286 (≠ N349), I287 (≠ V350), D288 (≠ I351), M353 (= M404), R356 (≠ T407), I359 (≠ V410), S380 (= S433), E381 (= E434)
- binding threonine: R269 (≠ F332), V272 (= V335), A273 (≠ M336), Q292 (= Q355), N373 (= N424), I374 (≠ V425)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
30% identity, 99% coverage: 3:460/462 of query aligns to 4:439/439 of 3tviE
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
30% identity, 98% coverage: 3:454/462 of query aligns to 3:442/447 of 2j0xA
- binding aspartic acid: F182 (= F195), G197 (= G210), G198 (= G211), S199 (= S212), D200 (= D213)
- binding lysine: M316 (≠ F330), S319 (≠ A333), F322 (≠ V335), L323 (≠ M336), S336 (≠ N349), V337 (= V350), D338 (≠ I351), S343 (= S356), E344 (≠ S357)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
30% identity, 98% coverage: 3:454/462 of query aligns to 3:442/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (≠ K232), D220 (≠ E233), I224 (≠ V237), Y225 (≠ L238), D228 (= D241), R230 (≠ K243), K255 (= K268), V256 (≠ I269)
- binding aspartic acid: S37 (= S39), T43 (= T45), E117 (= E128), F182 (= F195), R196 (= R209), G197 (= G210), 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)
30% identity, 98% coverage: 3:454/462 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 (= E128) 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.
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
31% identity, 74% coverage: 118:459/462 of query aligns to 64:402/405 of P61489
- E74 (= E128) 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.
Sites not aligning to the query:
- 7 K→A: Loss of aspartokinase activity.; K→M: Loss of aspartokinase activity.
- 9 G→M: Loss of aspartokinase activity.
- 10 G→A: Significant decrease in the catalytic efficiency.
- 41 S→A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
- 42 A→S: Loss of aspartokinase activity.
- 47 T→A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
30% identity, 99% coverage: 3:458/462 of query aligns to 2:429/429 of 3tviA
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
33% identity, 74% coverage: 118:461/462 of query aligns to 64:392/392 of 3aawC
- binding lysine: G136 (= G211), S137 (= S212), D138 (= D213), M337 (= M404), H340 (≠ T407), T344 (≠ A411), S364 (= S433)
- binding threonine: K258 (≠ D331), G260 (≠ A333), E261 (= E334), A262 (≠ V335), Q281 (= Q355), N357 (= N424), I358 (≠ V425)
Sites not aligning to the query:
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
31% identity, 74% coverage: 118:460/462 of query aligns to 63:370/370 of 3ab4A
- binding lysine: M316 (= M404), H319 (≠ T407), P320 (= P408), V322 (= V410), T323 (≠ A411), S343 (= S433), E344 (= E434)
- binding threonine: K239 (≠ D331), G241 (≠ A333), E242 (= E334), A243 (≠ V335), Q262 (= Q355), N336 (= N424), I337 (≠ V425)
2re1A Crystal structure of aspartokinase alpha and beta subunits
31% identity, 32% coverage: 311:459/462 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)
33% identity, 31% coverage: 319:459/462 of query aligns to 20:159/165 of 4go7X
Query Sequence
>WP_013684026.1 NCBI__GCF_000194625.1:WP_013684026.1
MRIVMKFGGASVKDGNSILHCAKLVKRFSTDNEIVVVVSAMAGVTDSLVHAARKCYTEQS
PGFIKMFIAELAKRHYDAVNTAVAEPHRQRVIAHIDRLIDELEKVLLGISYLGELTRRSE
DYILSFGERLSAPIVSAALLSIGVDSLALTGGDAGIVTNRNFGRAKPIPGVYSIIKSRLE
PLLTIKHTVPVVTGFIGATEDGNITTLGRGGSDLTATLIAAALDADEVWLWKEVDGVLTT
DPKIVPEARVIPEISYQEAMELSHFGAKILHPRALEPVMLKKIPVRIKNTFNPEAPGTVI
SDGCESTKDIVKALSLIEKVAIVNVSGAGFDFAEVMADVFRRLANERVNVIMVSQSSSEL
NLSIVVDESDVGRAMRVLKHMVNGTISISKLEDVAVVSAVGAGMAGTPGVAGRIFSALGK
NGINVIMISQSCSEYNVSFAVSKADGRKAVKILHDEFRLGGS
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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