SitesBLAST
Comparing WP_083491847.1 NCBI__GCF_001431535.1:WP_083491847.1 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)
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)
43% identity, 97% coverage: 25:835/837 of query aligns to 91:914/916 of O81852
- I441 (= I367) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q369) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (= I448) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q450) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
38% identity, 54% coverage: 25:477/837 of query aligns to 3:456/458 of 3c1nA
- binding threonine: G7 (= G29), G8 (= G30), T9 (= T31), S10 (= S32), W227 (= W245), T228 (= T246), D229 (= D247), A406 (≠ Q427), I409 (≠ V430), A410 (= A431), N423 (= N444), I424 (= I445), Q429 (= Q450), E433 (= E454)
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
37% identity, 54% coverage: 25:477/837 of query aligns to 3:461/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G29), T229 (= T246), D230 (= D247), V231 (= V248), Y235 (≠ L252), T237 (≠ A254), D238 (= D255), P239 (= P256), R240 (= R257), K265 (= K282), V266 (= V283)
- binding aspartic acid: S39 (= S59), T45 (= T65), F192 (= F209), R206 (= R223), G207 (≠ N224), S209 (= S226)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
38% identity, 54% coverage: 25:477/837 of query aligns to 3:465/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K27), G7 (= G29), G8 (= G30), S39 (= S59), T229 (= T246), D230 (= D247), Y235 (≠ L252), D238 (= D255), P239 (= P256), R240 (= R257), K265 (= K282), V266 (= V283)
- binding aspartic acid: T45 (= T65), E129 (= E145), F192 (= F209), R206 (= R223), G207 (≠ N224), S209 (= S226)
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
42% identity, 42% coverage: 479:830/837 of query aligns to 1:356/359 of P31116
- 11:18 (vs. 489:496, 63% identical) binding
- T93 (≠ S573) binding
- K117 (= K597) binding
- E208 (= E685) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D696) mutation to L: Reduces kcat 150-fold.
- K223 (= K700) mutation to V: Loss of activity.
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
42% identity, 42% coverage: 480:830/837 of query aligns to 1:355/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
42% identity, 42% coverage: 480:830/837 of query aligns to 1:355/358 of 1q7gA
- active site: D218 (= D696), K222 (= K700)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G492), V14 (≠ N493), V15 (= V494), E39 (≠ R520), N91 (≠ C572), T92 (≠ S573), S93 (≠ G574), I97 (≠ V578), P114 (= P595), K116 (= K597), A143 (= A625), S173 (= S655), K222 (= K700), A338 (= A813), T343 (= T818)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
42% identity, 42% coverage: 480:830/837 of query aligns to 1:355/358 of 1ebuD
- active site: D218 (= D696), K222 (= K700)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G490), A12 (≠ P491), G13 (= G492), V14 (≠ N493), V15 (= V494), E39 (≠ R520), A40 (= A521), N91 (≠ C572), S93 (≠ G574), K116 (= K597), T343 (= T818)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
42% identity, 42% coverage: 480:830/837 of query aligns to 1:355/358 of 1ebfA
- active site: D218 (= D696), K222 (= K700)
- binding nicotinamide-adenine-dinucleotide: I10 (= I489), A12 (≠ P491), G13 (= G492), V14 (≠ N493), V15 (= V494), E39 (≠ R520), A40 (= A521), T92 (≠ S573), S93 (≠ G574), P114 (= P595)
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 38% coverage: 486:806/837 of query aligns to 10:341/376 of O94671
- S201 (≠ P670) modified: Phosphoserine
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
29% identity, 54% coverage: 25:480/837 of query aligns to 6:461/470 of 2cdqA
- binding lysine: S40 (= S59), A41 (= A60), T46 (= T65), E124 (= E145), M327 (≠ L343), Q330 (≠ V346), F333 (≠ T349), L334 (≠ A350), S347 (= S363), V348 (= V364), D349 (≠ V365)
- binding s-adenosylmethionine: G345 (≠ Q361), I346 (≠ V362), S347 (= S363), W368 (≠ R387), S369 (≠ G388), R370 (= R389), L372 (≠ A391), E376 (≠ A395)
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 54% coverage: 24:474/837 of query aligns to 16:491/519 of O60163
- S326 (vs. gap) modified: Phosphoserine
- T328 (vs. gap) modified: Phosphothreonine
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
25% identity, 54% coverage: 23:477/837 of query aligns to 3:436/439 of 3tviE
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)
29% identity, 55% coverage: 22:478/837 of query aligns to 3:448/449 of P08660
- K8 (= K27) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E145) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R223) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D227) 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)
29% identity, 55% coverage: 22:478/837 of query aligns to 1:446/447 of 2j0xA
- binding aspartic acid: F182 (= F209), G197 (≠ N224), G198 (= G225), S199 (= S226), D200 (= D227)
- binding lysine: M316 (≠ L343), S319 (≠ V346), F322 (≠ T349), L323 (≠ A350), S336 (= S363), V337 (= V364), D338 (≠ V365), S343 (= S372), E344 (= E373)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
29% identity, 55% coverage: 22:478/837 of query aligns to 1:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T246), D220 (= D247), I224 (≠ V251), Y225 (≠ L252), D228 (= D255), R230 (= R257), K255 (= K282), V256 (= V283)
- binding aspartic acid: S37 (= S59), T43 (= T65), E117 (= E145), F182 (= F209), R196 (= R223), G197 (≠ N224), S199 (= S226)
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
24% identity, 54% coverage: 23:477/837 of query aligns to 1:428/429 of 3tviA
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
33% identity, 41% coverage: 137:481/837 of query aligns to 65:410/585 of 3l76A
- binding lysine: D286 (≠ S363), I287 (≠ V364), D288 (≠ V365), M353 (= M424), R356 (≠ Q427), I359 (≠ V430), S380 (= S453), E381 (= E454)
- binding threonine: R269 (vs. gap), V272 (≠ T349), A273 (= A350), Q292 (= Q369), N373 (= N444), I374 (= I445)
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)
31% identity, 42% coverage: 132:479/837 of query aligns to 61:395/397 of 5yeiC
- binding lysine: M342 (= M424), H345 (≠ Q427), A346 (≠ P428), G347 (= G429), V348 (= V430), A349 (= A431), S350 (≠ A432)
- binding threonine: T265 (≠ V346), P266 (= P347), A269 (= A350), Q288 (= Q369), N362 (= N444), I363 (= I445)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
31% identity, 41% coverage: 133:479/837 of query aligns to 62:402/405 of P61489
- E74 (= E145) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G208) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R223) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D227) 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 (= D247) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D255) 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.
Query Sequence
>WP_083491847.1 NCBI__GCF_001431535.1:WP_083491847.1
MSIAAAAPSADSAPPRSAVQPHVVVHKFGGTSVADADCYRHVARLLQARPEALQVTVVSA
MKGVTDALIALARLAAAGDAQWREDWHDLRARHRGAAASLLGEHAGASVEWLDARFDELA
ELLAALAVIGGLPEEVLDRVQGLGEVCSAHLLGQHFQASGEPCAVLDAREVLVVEHGELG
VNVDWETSAQRLHAWRQANVQQRIVVTGFIARDRRDRITTLGRNGSDYSGAIFAALFNAD
ELQIWTDVDGVLSADPRLVPEAVQLEALSYDEACELAYFGAKVVHPQTMSPAIQRGLPIL
IRNTFQPEHPGTRITAERSVRGPIKGLTLSAELAVLNLEGTGLIGVPGTAERVFSALRQA
QVSVVMISQGSSEHSICCVVRGNESERGRDALLQAFAHELAVGQVQRVQLRGGVSVLAAV
GDGMAGQPGVAARLFESLGRAQVNILAIAQGSSERNISVAVDSGDATRALRAAHAGFWLS
PQTFAVGVIGPGNVGAALLDQLQAAQPQLLGKANIDLRLRAVASRRGMHLAPRALQGPWR
AALADAASASDLDAFTAHLLSAHLPHAVVIDCSGSAEVAGRYEGWLAAGIHVVTPNKQAG
SGPLARYQSIRAAAAASGARFRYEATVGAGLPVITTLRDLVDTGDEVLSIEGIFSGTLAW
LFNRFDGSQPFSALVEQARGMGYTEPDPRDDLSGIDVARKLVILAREAGRDLSLEQVQVE
SLVPEALRAGSVDAFMQRLGDNDDALLQRLQQARARGAVLRYVAALSAQGASVGLVEIPL
DHAFANLKLTDNVVQFRTRRYCDNPLVVQGPGAGPEVTAAGVFADLLRVAAGEGARL
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