SitesBLAST
Comparing WP_005350179.1 NCBI__GCF_000173975.1:WP_005350179.1 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)
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, 100% coverage: 2:401/402 of query aligns to 3:408/421 of P26512
- G277 (= G272) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (= A274) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (= Q293) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ G296) 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 (≠ S356) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ M357) 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, 100% coverage: 2:401/402 of query aligns to 3:408/421 of P41398
- D345 (≠ A338) 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)
49% identity, 99% coverage: 2:400/402 of query aligns to 2:406/585 of 3l76A
- binding lysine: D286 (≠ N287), I287 (≠ V288), D288 (= D289), M353 (= M347), R356 (≠ H350), I359 (≠ V353), S380 (= S374), E381 (= E375)
- binding threonine: R269 (≠ E270), V272 (≠ I273), A273 (= A274), Q292 (= Q293), 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
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
46% identity, 99% coverage: 2:400/402 of query aligns to 2:395/397 of 5yeiC
- binding lysine: M342 (= M347), H345 (= H350), A346 (≠ P351), G347 (= G352), V348 (= V353), A349 (= A354), S350 (≠ A355)
- binding threonine: T265 (≠ E270), P266 (= P271), A269 (= A274), Q288 (= Q293), N362 (= N367), I363 (= I368)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
49% identity, 99% coverage: 2:400/402 of query aligns to 3:402/405 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 (= 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)
48% identity, 100% coverage: 2:401/402 of query aligns to 3:391/392 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 (≠ E270), G260 (= G272), E261 (≠ I273), A262 (= A274), Q281 (= Q293), N357 (= N367), I358 (= I368)
3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
45% identity, 100% coverage: 2:401/402 of query aligns to 2:370/370 of 3ab4A
- binding lysine: M316 (= M347), H319 (= H350), P320 (= P351), V322 (= V353), T323 (≠ A354), S343 (= S374), E344 (= E375)
- binding threonine: K239 (≠ E270), G241 (= G272), E242 (≠ I273), A243 (= A274), Q262 (= Q293), N336 (= N367), I337 (= I368)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
36% 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 (≠ G208), V266 (= V209)
- binding aspartic acid: E129 (= E73), F192 (= F135), R206 (= R149), G207 (= G150), S209 (= S152)
Sites not aligning to the query:
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
36% 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 (≠ A180), D238 (= D181), P239 (= P182), R240 (= R183), K265 (≠ G208), 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)
36% identity, 85% coverage: 59:398/402 of query aligns to 116:456/458 of 3c1nA
Sites not aligning to the query:
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
28% identity, 98% coverage: 4:398/402 of query aligns to 6:458/470 of 2cdqA
- binding lysine: S40 (= S40), A41 (= A41), T46 (= T46), E124 (= E73), M327 (≠ L267), Q330 (≠ E270), F333 (≠ I273), L334 (≠ A274), S347 (≠ N287), V348 (= V288), D349 (= D289)
- binding s-adenosylmethionine: G345 (≠ N285), I346 (= I286), S347 (≠ N287), W368 (≠ I319), S369 (≠ Q320), R370 (≠ K321), L372 (≠ F323), E376 (= E327)
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)
32% identity, 73% coverage: 107:400/402 of query aligns to 253:553/916 of O81852
- I441 (= I291) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q293) 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.
2re1A Crystal structure of aspartokinase alpha and beta subunits
46% identity, 38% coverage: 250:400/402 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)
39% identity, 39% coverage: 243:400/402 of query aligns to 2:159/165 of 4go7X
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
43% identity, 37% coverage: 250:398/402 of query aligns to 3:152/153 of 2dt9A
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 71% coverage: 118:401/402 of query aligns to 153:439/439 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)
28% identity, 84% coverage: 61:398/402 of query aligns to 134:494/519 of O60163
- S326 (vs. gap) 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)
27% identity, 70% coverage: 118:398/402 of query aligns to 149:428/429 of 3tviA
Sites not aligning to the query:
2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
25% identity, 99% coverage: 2:398/402 of query aligns to 2:445/447 of 2j0xA
- binding aspartic acid: F182 (= F135), G197 (= G150), G198 (= G151), S199 (= S152), D200 (= D153)
- binding lysine: M316 (≠ L267), S319 (≠ E270), F322 (≠ I273), L323 (≠ A274), S336 (≠ N287), V337 (= V288), D338 (= D289), S343 (= S294), E344 (≠ N298)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
25% identity, 99% coverage: 2:398/402 of query aligns to 2:445/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T172), D220 (= D173), I224 (≠ V177), Y225 (= Y178), D228 (= D181), R230 (= R183), K255 (≠ G208), V256 (= V209)
- binding aspartic acid: S37 (= S40), T43 (= T46), E117 (= E73), F182 (= F135), R196 (= R149), G197 (= G150), S199 (= S152)
Query Sequence
>WP_005350179.1 NCBI__GCF_000173975.1:WP_005350179.1
MLIVKKFGGTSVGNKERILNVAKRCIEDYQKGNDVVVVLSAMGKSTDELIDMAKDINPTP
SKREMDMLMTTGEQVSVSLMAMAMGSLGVPAISLNAFQVAMHTTHRYGNAQLKRIDTDRI
RNELEQRKIVLVTGFQGIDKFDNVTTLGRGGSDTTAVALAAALHADACEIYTDVDGVYTA
DPRYVKKARKLAEITYDEMLDLASLGAGVLHNRSVEMAKKYGVQLVVRSSLNNHEGTIVR
EEVNMEKMLVSGVAADKNATRIAVIGLKDEPGIAFHLFNALAKYNINVDIILQSVGRNGT
KDISFTVAEDEADEAVAIIQKSFPKSEYNKIDEEKDVAKISIVGAGMMTHPGVAASMFEA
LYDAGVNIKMISTSEIRVTVLIDEKYTEKALNAVHDKFALGD
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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