SitesBLAST
Comparing WP_007474201.1 NCBI__GCF_000170735.1:WP_007474201.1 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)
56% identity, 100% coverage: 2:401/402 of query aligns to 2:396/397 of 5yeiC
- binding lysine: M342 (= M347), H345 (= H350), A346 (≠ S351), G347 (= G352), V348 (= V353), A349 (= A354), S350 (≠ A355)
- binding threonine: T265 (≠ R272), P266 (= P273), A269 (≠ S276), Q288 (= Q295), N362 (= N367), I363 (= I368)
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)
49% identity, 99% coverage: 2:400/402 of query aligns to 3:407/421 of P26512
- G277 (= G274) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ S276) 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 (≠ G298) 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 (= V353) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A354) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ K356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ A357) 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)
49% identity, 99% coverage: 2:400/402 of query aligns to 3:407/421 of P41398
- D345 (≠ A338) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
48% identity, 100% coverage: 2:402/402 of query aligns to 3:404/405 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 (= E73) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G134) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R149) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D153) 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 (= D173) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D181) 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)
46% identity, 99% coverage: 2:400/402 of query aligns to 3:390/392 of 3aawC
- binding lysine: K7 (= K6), S41 (= S40), G136 (= G151), S137 (= S152), D138 (= D153), M337 (= M347), H340 (= H350), T344 (≠ A354), S364 (= S374)
- binding threonine: K258 (≠ R272), G260 (= G274), E261 (≠ I275), A262 (≠ S276), Q281 (= Q295), N357 (= N367), I358 (= I368)
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
45% identity, 99% coverage: 2:398/402 of query aligns to 2:404/585 of 3l76A
- binding lysine: D286 (≠ N289), I287 (≠ V290), D288 (= D291), M353 (= M347), R356 (≠ H350), I359 (≠ V353), S380 (= S374), E381 (= E375)
- binding threonine: R269 (= R272), V272 (≠ I275), A273 (≠ S276), Q292 (= Q295), N373 (= N367), I374 (= I368)
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)
43% identity, 99% coverage: 2:400/402 of query aligns to 2:369/370 of 3ab4A
- binding lysine: M316 (= M347), H319 (= H350), P320 (≠ S351), V322 (= V353), T323 (≠ A354), S343 (= S374), E344 (= E375)
- binding threonine: K239 (≠ R272), G241 (= G274), E242 (≠ I275), A243 (≠ S276), Q262 (= Q295), N336 (= N367), I337 (= I368)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
40% identity, 85% coverage: 59:398/402 of query aligns to 117:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T172), D230 (= D173), V231 (= V174), Y235 (= Y178), T237 (= T180), D238 (= D181), P239 (= P182), R240 (= R183), K265 (= K208), V266 (= V209)
- binding aspartic acid: F192 (= F135), R206 (= R149), G207 (= G150), S209 (= S152)
Sites not aligning to the query:
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
41% identity, 85% coverage: 59:398/402 of query aligns to 116:456/458 of 3c1nA
Sites not aligning to the query:
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
40% identity, 85% coverage: 59:398/402 of query aligns to 117:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T172), D230 (= D173), Y235 (= Y178), D238 (= D181), P239 (= P182), R240 (= R183), K265 (= K208), V266 (= V209)
- binding aspartic acid: E129 (= E73), F192 (= F135), R206 (= R149), G207 (= G150), S209 (= S152)
Sites not aligning to the query:
2re1A Crystal structure of aspartokinase alpha and beta subunits
54% identity, 37% coverage: 252:400/402 of query aligns to 2:148/148 of 2re1A
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 99% coverage: 3:398/402 of query aligns to 5:458/470 of 2cdqA
- binding lysine: S40 (= S40), A41 (= A41), T46 (vs. gap), E124 (= E73), M327 (vs. gap), Q330 (≠ R272), F333 (≠ I275), L334 (≠ S276), S347 (≠ N289), V348 (= V290), D349 (= D291)
- binding s-adenosylmethionine: G345 (≠ N287), I346 (= I288), S347 (≠ N289), W368 (≠ E315), S369 (≠ L316), R370 (≠ T317), L372 (≠ E319), E376 (= E323)
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: 2:395/402 of query aligns to 4:444/449 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 (= E73) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R149) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D153) 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)
30% identity, 98% coverage: 2:395/402 of query aligns to 2:442/447 of 2j0xA
- binding aspartic acid: F182 (= F135), G197 (= G150), G198 (= G151), S199 (= S152), D200 (= D153)
- binding lysine: M316 (vs. gap), S319 (≠ R272), F322 (≠ I275), L323 (≠ S276), S336 (≠ N289), V337 (= V290), D338 (= D291), S343 (≠ N296), E344 (≠ D300)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
30% identity, 98% coverage: 2:395/402 of query aligns to 2:442/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T172), D220 (= D173), I224 (= I177), Y225 (= Y178), D228 (= D181), R230 (= R183), K255 (= K208), V256 (= V209)
- binding aspartic acid: S37 (= S40), T43 (= T46), E117 (= E73), F182 (= F135), R196 (= R149), G197 (= G150), S199 (= S152)
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)
26% identity, 100% coverage: 1:402/402 of query aligns to 88:555/916 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 (= I371) 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.
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
27% identity, 99% coverage: 2:398/402 of query aligns to 3:436/439 of 3tviE
4go7X The regulatory subunit of aspartate kinase in complex with threonine from mycobacterium tuberculosis (see paper)
41% identity, 39% coverage: 244:401/402 of query aligns to 1:160/165 of 4go7X
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
44% identity, 37% coverage: 252:399/402 of query aligns to 3:153/153 of 2dt9A
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
26% identity, 99% coverage: 2:398/402 of query aligns to 1:428/429 of 3tviA
Query Sequence
>WP_007474201.1 NCBI__GCF_000170735.1:WP_007474201.1
MLVVQKFGGTSVGDLDRIENVANIVKSYKERGDDVVVVVSAMAGETNKLLDYANHFSKTP
PQREVDLLVSSGERVTSALLSIALQSKGIPAIALTGRQAGIKTTSDHTKARIMDIDPEKM
QKHLKEGKVVIVAGFQGINENGDVTTLGRGGSDLTAVAIAGALKADKCEIYTDVDGIYTT
DPRIEPKAKKIDVISYDEMLELASLGAKVMQSRSVELAKKLNVDIEVKSSFKPEIKGTLI
TKESKDMEKVLVSGIALDKNQARVSIFGVDDRPGISAEIFEKLANKNINVDMIVQNVGKD
GKANLTFTVPQTEVELTKEVLKEYENNTENIEYDTDIAKVSVVGVGMKSHSGVAAKAFKT
LANENINILMISTSEIKISMVIDEKYGELAVRALHKAYELDK
Or try a new SitesBLAST search
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