SitesBLAST
Comparing WP_055068006.1 NCBI__GCF_001406815.1:WP_055068006.1 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)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
53% identity, 99% coverage: 4:436/439 of query aligns to 5:438/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
52% identity, 98% coverage: 4:434/439 of query aligns to 3:428/429 of 3tviA
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
29% identity, 99% coverage: 4:437/439 of query aligns to 6:461/470 of 2cdqA
- binding lysine: S40 (= S37), A41 (= A38), T46 (≠ N43), E124 (= E115), M327 (= M305), Q330 (≠ E308), F333 (= F311), L334 (≠ C312), S347 (= S325), V348 (≠ I326), D349 (≠ E327)
- binding s-adenosylmethionine: G345 (= G323), I346 (= I324), S347 (= S325), W368 (≠ E346), S369 (≠ G347), R370 (≠ K348), L372 (vs. gap), E376 (≠ Q351)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
31% identity, 62% coverage: 165:436/439 of query aligns to 188:463/464 of 2hmfA
- binding adenosine-5'-diphosphate: T229 (= T206), D230 (= D207), V231 (= V208), Y235 (≠ L212), T237 (≠ A214), D238 (= D215), P239 (= P216), R240 (= R217), K265 (≠ S242), V266 (= V243)
- binding aspartic acid: F192 (= F169), R206 (= R183), G207 (= G184), S209 (= S186)
Sites not aligning to the query:
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
31% identity, 62% coverage: 165:436/439 of query aligns to 187:458/458 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)
34% identity, 62% coverage: 165:436/439 of query aligns to 188:467/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: T229 (= T206), D230 (= D207), Y235 (≠ L212), D238 (= D215), P239 (= P216), R240 (= R217), K265 (≠ S242), V266 (= V243)
- binding aspartic acid: F192 (= F169), R206 (= R183), G207 (= G184), S209 (= S186)
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)
28% identity, 100% coverage: 1:438/439 of query aligns to 88:555/916 of O81852
- I441 (= I326) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (≠ H328) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I405) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q407) 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)
29% identity, 75% coverage: 108:436/439 of query aligns to 139:493/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
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)
25% identity, 99% coverage: 2:436/439 of query aligns to 4:449/449 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 (= E115) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R183) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D187) 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)
25% identity, 99% coverage: 2:436/439 of query aligns to 2:447/447 of 2j0xA
- binding aspartic acid: F182 (= F169), G197 (= G184), G198 (= G185), S199 (= S186), D200 (= D187)
- binding lysine: M316 (= M304), S319 (= S307), F322 (= F311), L323 (≠ C312), S336 (= S325), V337 (≠ I326), D338 (≠ E327), S343 (≠ G332), E344 (≠ I333)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
25% identity, 99% coverage: 2:436/439 of query aligns to 2:447/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T206), D220 (= D207), I224 (≠ C211), Y225 (≠ L212), D228 (= D215), R230 (= R217), K255 (≠ S242), V256 (= V243)
- binding aspartic acid: S37 (= S37), T43 (= T50), E117 (= E115), F182 (= F169), R196 (= R183), G197 (= G184), S199 (= S186)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
27% identity, 62% coverage: 164:434/439 of query aligns to 131:400/405 of P61489
- G135 (= G168) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R183) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D187) 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 (= D207) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D215) 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.
P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 2 papers)
28% identity, 75% coverage: 107:434/439 of query aligns to 66:405/421 of P26512
- G277 (= G310) mutation to A: Change in the inhibitory profile upon addition of threonine.
- A279 (≠ C312) mutation to V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
- Q298 (≠ S331) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- S301 (≠ D334) 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 (≠ T387) mutation to A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
- T361 (≠ A388) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- E363 (≠ R390) mutation to A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
- F364 (≠ I391) 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)
29% identity, 75% coverage: 107:434/439 of query aligns to 66:405/421 of P41398
- D345 (= D366) mutation to G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.
5yeiC Mechanistic insight into the regulation of pseudomonas aeruginosa aspartate kinase (see paper)
28% identity, 62% coverage: 165:434/439 of query aligns to 131:393/397 of 5yeiC
- binding lysine: M342 (= M381), H345 (≠ T384), A346 (≠ R385), G347 (= G386), V348 (≠ T387), A349 (= A388), S350 (≠ G389)
- binding threonine: T265 (≠ N306), P266 (≠ S307), A269 (≠ G310), Q288 (≠ S331), N362 (= N401), I363 (≠ V402)
3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
27% identity, 65% coverage: 148:434/439 of query aligns to 100:388/392 of 3aawC
- binding lysine: G136 (= G185), S137 (= S186), D138 (= D187), M337 (= M381), H340 (≠ T384), T344 (≠ A388), S364 (= S410)
- binding threonine: K258 (≠ E308), G260 (= G310), E261 (≠ F311), A262 (≠ C312), Q281 (≠ S331), N357 (= N401), I358 (≠ V402)
Sites not aligning to the query:
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
28% identity, 64% coverage: 154:434/439 of query aligns to 113:404/585 of 3l76A
- binding lysine: D286 (≠ S325), I287 (vs. gap), D288 (vs. gap), M353 (= M381), R356 (≠ T384), I359 (≠ T387), S380 (= S410), E381 (= E411)
- binding threonine: R269 (vs. gap), V272 (≠ F311), A273 (≠ C312), Q292 (≠ E327), N373 (= N401), I374 (≠ V402)
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)
27% identity, 53% coverage: 203:434/439 of query aligns to 135:367/370 of 3ab4A
- binding lysine: M316 (= M381), H319 (≠ T384), P320 (≠ R385), V322 (≠ T387), T323 (≠ A388), S343 (= S410), E344 (= E411)
- binding threonine: K239 (≠ E308), G241 (= G310), E242 (≠ F311), A243 (≠ C312), Q262 (≠ S331), N336 (= N401), I337 (≠ V402)
2dt9A Crystal structure of the regulatory subunit of aspartate kinase from thermus flavus (see paper)
24% identity, 28% coverage: 310:434/439 of query aligns to 25:152/153 of 2dt9A
Sites not aligning to the query:
Query Sequence
>WP_055068006.1 NCBI__GCF_001406815.1:WP_055068006.1
MVKVVKFGGSSLASAEQFAKVGDIIRADESRKYVVPSAPGKRNSRDTKVTDMLYACYAKA
EAGEEFRVPLMKIKERYDSIINGLGLKVTLDEEFKTISKNFKEKAGVDYAASRGEYLNGI
LMADYLGYEFIDSATVIFFDEEGNLDADKTDKVLAKKLSECEKAVIPGFYGIGADGRVKT
FSRGGSDITGSIVAKACHASLYENWTDVSGCLVADPRIIDNPQPIHVITYRELRELSYMG
ASVLHEDAVFPVRKAGIPINIRNTNDPEAEGTLIVESTCQKPEYTITGIAGKKGFVAVSI
DKDMMNSEVGFCRKALQAFEENGISIEHMPSGIDTMTVFVHQEEFEGKEQQVISSIRRLT
HPDVIDLEADLGLIAVVGRGMKSTRGTAGRIFSALAHANINVKMIDQGSSELNIIIGVSN
DDFEAAIKAIYDIFVETRL
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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