SitesBLAST
Comparing WP_013981377.1 NCBI__GCF_000013785.1:WP_013981377.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 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)
25% identity, 97% coverage: 3:465/476 of query aligns to 2:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G8), T229 (≠ K239), D230 (≠ E240), V231 (≠ F241), Y235 (≠ S244), T237 (≠ A246), D238 (= D247), P239 (= P248), R240 (≠ N249), K265 (≠ E276), V266 (≠ A277)
- binding aspartic acid: S39 (= S40), T45 (= T46), F192 (≠ Y203), R206 (= R216), G207 (= G217), S209 (= S219)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
24% identity, 97% coverage: 3:465/476 of query aligns to 2:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K6), G7 (= G8), G8 (= G9), S39 (= S40), T229 (≠ K239), D230 (≠ E240), Y235 (≠ S244), D238 (= D247), P239 (= P248), R240 (≠ N249), K265 (≠ E276), V266 (≠ A277)
- binding aspartic acid: T45 (= T46), E129 (= E146), F192 (≠ Y203), R206 (= R216), G207 (= G217), S209 (= S219)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
24% identity, 97% coverage: 4:465/476 of query aligns to 6:460/470 of 2cdqA
- binding lysine: S40 (= S40), A41 (= A41), T46 (= T46), E124 (= E146), M327 (= M338), Q330 (≠ D341), F333 (≠ Y344), L334 (≠ D345), S347 (≠ Y358), V348 (vs. gap), D349 (vs. gap)
- binding s-adenosylmethionine: G345 (≠ K356), I346 (≠ L357), S347 (≠ Y358), W368 (≠ G375), S369 (= S376), R370 (= R377), L372 (= L379), E376 (≠ A383)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
25% identity, 97% coverage: 3:465/476 of query aligns to 2:458/458 of 3c1nA
- binding threonine: G7 (= G8), G8 (= G9), T9 (= T10), S10 (= S11), W227 (≠ H238), T228 (≠ K239), D229 (≠ E240), A406 (≠ V413), I409 (= I416), A410 (≠ L417), N423 (≠ S430), I424 (= I431), Q429 (= Q436), E433 (≠ Q440)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 56% coverage: 198:465/476 of query aligns to 166:438/439 of 3tviE
Sites not aligning to the query:
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 71% coverage: 130:466/476 of query aligns to 130:497/519 of O60163
- S326 (= S314) modified: Phosphoserine
- T328 (≠ K316) modified: Phosphothreonine
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
26% identity, 56% coverage: 198:463/476 of query aligns to 162:428/429 of 3tviA
Sites not aligning to the query:
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)
23% identity, 97% coverage: 1:460/476 of query aligns to 88:548/916 of O81852
- I441 (≠ V360) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (≠ K362) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I434) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q436) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
26% identity, 71% coverage: 139:474/476 of query aligns to 66:419/585 of 3l76A
- binding lysine: D286 (≠ N361), I287 (≠ K362), D288 (= D363), M353 (≠ L411), R356 (≠ K414), I359 (= I416), S380 (= S437), E381 (≠ Q440)
- binding threonine: R269 (≠ Y344), V272 (≠ E347), A273 (≠ I348), Q292 (vs. gap), N373 (≠ S430), I374 (= I431)
Sites not aligning to the query:
- binding lysine: 457, 458, 459, 522, 525, 528, 548, 549, 553
- binding threonine: 440, 443, 463, 542, 543
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)
23% identity, 97% coverage: 4:465/476 of query aligns to 6:449/449 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 (= E146) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R216) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (≠ E220) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
23% identity, 97% coverage: 4:465/476 of query aligns to 4:447/447 of 2j0xA
- binding aspartic acid: F182 (≠ Y203), G197 (= G217), G198 (≠ Y218), S199 (= S219), D200 (≠ E220)
- binding lysine: M316 (= M338), S319 (≠ D341), F322 (≠ Y344), L323 (≠ D345), S336 (vs. gap), V337 (≠ L355), D338 (≠ K356), S343 (≠ N361), E344 (≠ K362)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
23% identity, 97% coverage: 4:465/476 of query aligns to 4:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (≠ K239), D220 (≠ E240), I224 (≠ L243), Y225 (≠ S244), D228 (= D247), R230 (≠ N249), K255 (≠ E276), V256 (≠ A277)
- binding aspartic acid: S37 (= S40), T43 (= T46), E117 (= E146), F182 (≠ Y203), R196 (= R216), G197 (= G217), S199 (= S219)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
27% identity, 56% coverage: 198:463/476 of query aligns to 132:400/405 of P61489
- G135 (≠ T201) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R216) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (≠ E220) 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 (≠ E240) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D247) 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.
- 74 E→A: Loss of aspartokinase activity.; E→Q: Loss of aspartokinase activity.
Query Sequence
>WP_013981377.1 NCBI__GCF_000013785.1:WP_013981377.1
MHTVEKIGGTSMSRFEEVLDNIFIGRREGAALYQRIFVVSAYSGMTNLLLEHKKTGEPGV
YQRFADAQSEGAWREALEGVRQRMLAKNAELFSSEYELHAANQFINSRIDDASECMHSLQ
KLCAYGHFQLSEHLMKVREMLASLGEAHSAFNSVLALKQRGVNARLADLTGWQQEAPLPF
EEMISSHFAGFDFSRELVVATGYTHCAEGLMNTFDRGYSEITFAQIAAATGAREAIIHKE
FHLSSADPNLVGADKVVTIGRTNYDVADQLSNLGMEAIHPRAAKTLRRAGVELRIKNAFE
PEHGGTLISQDYKSEKPCVEIIAGRKDVFGIEVFDQDMLGDIGYDMEISKLLKQLKLYVV
NKDSDANSITYYASGSRKLINRAARLIEEQYPAAEVTVHNLAIVSAIGSDLKVKGILAKT
VAALAEAGISIQAIHQSIRQVEMQCVVNEEDYDAAIAALHRALIEPENHGDVIAAA
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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