SitesBLAST
Comparing WP_012503132.1 NCBI__GCF_000020505.1:WP_012503132.1 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)
39% identity, 100% coverage: 3:817/818 of query aligns to 91:912/916 of O81852
- I441 (= I349) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (= Q351) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (≠ V430) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q432) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
39% identity, 56% coverage: 3:460/818 of query aligns to 3:462/464 of 2hmfA
- binding adenosine-5'-diphosphate: G7 (= G7), T229 (= T224), D230 (≠ H225), V231 (= V226), Y235 (= Y230), T237 (≠ A232), D238 (= D233), P239 (= P234), R240 (≠ K235), K265 (= K260), V266 (= V261)
- binding aspartic acid: S39 (= S38), T45 (= T44), F192 (= F187), R206 (= R201), G207 (= G202), S209 (= S204)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
39% identity, 56% coverage: 3:460/818 of query aligns to 3:457/458 of 3c1nA
- binding threonine: G7 (= G7), G8 (= G8), T9 (≠ S9), S10 (= S10), W227 (= W223), T228 (= T224), D229 (≠ H225), A406 (≠ H409), I409 (≠ V412), A410 (≠ S413), N423 (= N426), I424 (≠ V427), Q429 (= Q432), E433 (= E436)
3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
39% identity, 56% coverage: 3:460/818 of query aligns to 3:466/468 of 3c1mC
- binding phosphoaminophosphonic acid-adenylate ester: K5 (= K5), G7 (= G7), G8 (= G8), S39 (= S38), T229 (= T224), D230 (≠ H225), Y235 (= Y230), D238 (= D233), P239 (= P234), R240 (≠ K235), K265 (= K260), V266 (= V261)
- binding aspartic acid: T45 (= T44), E129 (= E124), F192 (= F187), R206 (= R201), G207 (= G202), S209 (= S204)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s-adenosylmethionine (see paper)
32% identity, 56% coverage: 3:462/818 of query aligns to 6:461/470 of 2cdqA
- binding lysine: S40 (= S38), A41 (= A39), T46 (= T44), E124 (= E124), M327 (= M325), Q330 (≠ V328), F333 (≠ T331), L334 (≠ A332), S347 (≠ N345), V348 (≠ I346), D349 (≠ I347)
- binding s-adenosylmethionine: G345 (≠ S343), I346 (= I344), S347 (≠ N345), W368 (≠ M369), S369 (≠ A370), R370 (≠ K371), L372 (≠ V373), E376 (= E377)
O94671 Probable homoserine dehydrogenase; HDH; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 43% coverage: 462:815/818 of query aligns to 4:366/376 of O94671
- S201 (vs. gap) modified: Phosphoserine
O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 56% coverage: 3:460/818 of query aligns to 17:495/519 of O60163
- S326 (≠ Q302) modified: Phosphoserine
- T328 (≠ R304) modified: Phosphothreonine
P31116 Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 44% coverage: 461:817/818 of query aligns to 1:359/359 of P31116
- 11:18 (vs. 471:478, 25% identical) binding
- T93 (= T556) binding
- K117 (= K580) binding
- E208 (= E668) binding ; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D679) mutation to L: Reduces kcat 150-fold.
- K223 (= K683) mutation to V: Loss of activity.
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
33% identity, 44% coverage: 462:817/818 of query aligns to 1:358/358 of 1tveA
1q7gA Homoserine dehydrogenase in complex with suicide inhibitor complex NAD-5-hydroxy-4-oxonorvaline (see paper)
33% identity, 44% coverage: 462:817/818 of query aligns to 1:358/358 of 1q7gA
- active site: D218 (= D679), K222 (= K683)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G474), V14 (≠ T475), V15 (≠ I476), E39 (≠ N506), N91 (≠ C555), T92 (= T556), S93 (≠ A557), I97 (≠ V561), P114 (≠ A578), K116 (= K580), A143 (≠ T608), S173 (= S638), K222 (= K683), A338 (= A797), T343 (= T802)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
33% identity, 44% coverage: 462:817/818 of query aligns to 1:358/358 of 1ebuD
- active site: D218 (= D679), K222 (= K683)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G472), A12 (≠ T473), G13 (= G474), V14 (≠ T475), V15 (≠ I476), E39 (≠ N506), A40 (≠ T507), N91 (≠ C555), S93 (≠ A557), K116 (= K580), T343 (= T802)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
33% identity, 44% coverage: 462:817/818 of query aligns to 1:358/358 of 1ebfA
- active site: D218 (= D679), K222 (= K683)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ A471), A12 (≠ T473), G13 (= G474), V14 (≠ T475), V15 (≠ I476), E39 (≠ N506), A40 (≠ T507), T92 (= T556), S93 (≠ A557), P114 (≠ A578)
3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 56% coverage: 3:459/818 of query aligns to 5:436/439 of 3tviE
3tviA Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
28% identity, 56% coverage: 3:459/818 of query aligns to 3:428/429 of 3tviA
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, 56% coverage: 3:460/818 of query aligns to 6:448/449 of P08660
- K8 (= K5) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E124) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R201) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D205) 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, 56% coverage: 3:460/818 of query aligns to 4:446/447 of 2j0xA
- binding aspartic acid: F182 (= F187), G197 (= G202), G198 (= G203), S199 (= S204), D200 (= D205)
- binding lysine: M316 (= M325), S319 (≠ V328), F322 (≠ T331), L323 (≠ A332), S336 (≠ N345), V337 (≠ I346), D338 (≠ I347), S343 (= S354), E344 (= E355)
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
29% identity, 56% coverage: 3:460/818 of query aligns to 4:446/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (= T224), D220 (≠ H225), I224 (≠ F229), Y225 (= Y230), D228 (= D233), R230 (≠ K235), K255 (= K260), V256 (= V261)
- binding aspartic acid: S37 (= S38), T43 (= T44), E117 (= E124), F182 (= F187), R196 (= R201), G197 (= G202), S199 (= S204)
P61489 Aspartokinase; Aspartate kinase; AK; ASK; Threonine-sensitive AK; ThrA; EC 2.7.2.4 from Thermus thermophilus (see paper)
32% identity, 43% coverage: 114:461/818 of query aligns to 64:402/405 of P61489
- E74 (= E124) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
- G135 (= G186) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
- R150 (= R201) mutation to A: Significant decrease in the catalytic efficiency.
- D154 (= D205) 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 (≠ H225) mutation to A: Significant decrease in the catalytic efficiency.
- D182 (= D233) 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.
3l76A Crystal structure of aspartate kinase from synechocystis (see paper)
28% identity, 56% coverage: 3:463/818 of query aligns to 4:408/585 of 3l76A
- binding lysine: D286 (≠ N345), I287 (= I346), D288 (≠ I347), M353 (= M406), R356 (≠ H409), I359 (≠ V412), S380 (≠ N435), E381 (= E436)
- binding threonine: R269 (≠ S323), V272 (≠ T331), A273 (= A332), Q292 (= Q351), N373 (= N426), I374 (≠ V427)
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)
30% identity, 43% coverage: 114:461/818 of query aligns to 63:395/397 of 5yeiC
- binding lysine: M342 (= M406), H345 (= H409), A346 (≠ P410), G347 (= G411), V348 (= V412), A349 (≠ S413), S350 (≠ A414)
- binding threonine: T265 (≠ V328), P266 (= P329), A269 (= A332), Q288 (= Q351), N362 (= N426), I363 (≠ V427)
Query Sequence
>WP_012503132.1 NCBI__GCF_000020505.1:WP_012503132.1
MKVFKFGGSSIASAANISNAAAIIRKELERSELIVVVSAIARVTDLLAEAGAQAGKGDEA
WRETLDVIGSLHADVIRELFGEEAAPEEAWLREVVAELNDVLHGVALLRELSDKSLVLIL
SYGERLSCRIMSRCLDVSGTPAECVDARELIVTDENYCYAKVDRLATGKRIKERFQTYDP
VPVVTGFIASAEDGSVTNLGRGGSDFTATILGAALHAEEVWIWTHVDGFYSADPKRVPDA
KVLPEISYAEAMELSHAGAKVLHPLAVQPVMKASIPLLIRNASDPENPGTRIGQLPASTD
GQPRPVTGLTSINRVVLLNLSGSGMAGVPGTASRLFTCLARHSINIIFISQASSEQSISL
AVAPDQASMAKKVLEEEYSREIKERRIDPVSVRRNLAMVAIVGNKMSGHPGVSAQLFETL
GKNGVNVIAVAQGANEMNISVVIDSSDEDKALNCIHESFFLSMRKVHVFIAGTGTIAKSL
ISQIRDHRATLQQEMALDIVVAGLANTRAICIEPEGIDLEHWEESMKTREAHQGIGHYIK
LIRAENLHNTIVVDCTASKQVAESYPELLQANISVATANKLGMAGSGELYGKIMKAERSS
NARFLYETNVGAGLPIISTLNDLKNSGDRIICIEGVLSGTLSYIFNELRKGGRFSEIVRK
AKESGYTEPDPRDDLSGADFARKMLILGRALGYQLEYDDVECQSLVPESCQGDMSTAEFL
DRLATIDDWYVEEMESAAKEGKTIAYTGELKDGKAKVGLKRVPLESPVAGLNGTENLVVF
TTDRYLDTPLVVKGPGAGGEVTAGGVFADILRIASYLV
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