SitesBLAST
Comparing WP_008807866.1 NCBI__GCF_000025465.1:WP_008807866.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
32% identity, 98% coverage: 14:810/810 of query aligns to 91:912/916 of O81852
- I441 (≠ V351) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q443 (≠ V353) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
- I522 (≠ T423) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
- Q524 (= Q425) mutation to A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
O94671 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 40% coverage: 458:783/810 of query aligns to 7:341/376 of O94671
- S201 (≠ P646) modified: Phosphoserine
P31116 Homoserine dehydrogenase; HDH; HSD; EC 1.1.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
33% identity, 44% coverage: 455:810/810 of query aligns to 2:359/359 of P31116
- A13 (≠ K466) binding NAD(+)
- V15 (≠ N468) binding NAD(+)
- V16 (≠ I469) binding NAD(+)
- A41 (≠ S500) binding NAD(+)
- H79 (≠ W534) mutation to A: Reduces kcat 2-fold.
- T93 (= T549) binding NAD(+)
- E143 (vs. gap) binding Na(+)
- V146 (= V603) binding Na(+)
- A148 (= A605) binding Na(+)
- L150 (= L607) binding Na(+)
- E208 (= E661) binding L-homoserine; mutation to D: Increases KM for aspartate-semialdehyde 48-fold and reduces kcat by 50%.; mutation E->L,Q: Loss of activity.
- D219 (= D672) binding L-homoserine; mutation to L: Reduces kcat 150-fold.
- K223 (= K676) mutation to V: Loss of activity.
- H309 (= H759) mutation to A: Reduces kcat 40-fold. Affects dimer formation.
- G340 (= G791) binding NAD(+)
1tveA Homoserine dehydrogenase in complex with 4-(4-hydroxy-3- isopropylphenylthio)-2-isopropylphenol (see paper)
33% identity, 44% coverage: 455:810/810 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: 455:810/810 of query aligns to 1:358/358 of 1q7gA
- active site: D218 (= D672), K222 (= K676)
- binding nicotinamide-adenine-dinucleotide-5-hydroxy-4-oxonorvaline: G13 (= G467), V14 (≠ N468), V15 (≠ I469), E39 (≠ D499), N91 (≠ V548), T92 (= T549), S93 (≠ A550), I97 (≠ L554), P114 (≠ A571), K116 (= K573), A143 (= A601), S173 (= S631), K222 (= K676), A338 (= A790), T343 (= T795)
1ebuD Homoserine dehydrogenase complex with NAD analogue and l-homoserine (see paper)
33% identity, 44% coverage: 455:810/810 of query aligns to 1:358/358 of 1ebuD
- active site: D218 (= D672), K222 (= K676)
- binding 3-aminomethyl-pyridinium-adenine-dinucleotide: G11 (= G465), A12 (≠ K466), G13 (= G467), V14 (≠ N468), V15 (≠ I469), E39 (≠ D499), A40 (≠ S500), N91 (≠ V548), S93 (≠ A550), K116 (= K573), T343 (= T795)
1ebfA Homoserine dehydrogenase from s. Cerevisiae complex with NAD+ (see paper)
33% identity, 44% coverage: 455:810/810 of query aligns to 1:358/358 of 1ebfA
- active site: D218 (= D672), K222 (= K676)
- binding nicotinamide-adenine-dinucleotide: I10 (≠ F464), A12 (≠ K466), G13 (= G467), V14 (≠ N468), V15 (≠ I469), E39 (≠ D499), A40 (≠ S500), T92 (= T549), S93 (≠ A550), P114 (≠ A571)
2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
27% identity, 54% coverage: 16:455/810 of query aligns to 8:461/470 of 2cdqA
- binding lysine: S40 (= S48), A41 (= A49), T46 (= T54), E124 (= E130), M327 (≠ E321), Q330 (= Q323), F333 (≠ A326), L334 (≠ S327), S347 (≠ L340), V348 (≠ L341), D349 (≠ K342)
- binding s-adenosylmethionine: G345 (≠ D338), I346 (≠ A339), S347 (≠ L340), W368 (vs. gap), S369 (vs. gap), R370 (= R357), L372 (= L359), E376 (≠ V368)
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)
32% identity, 35% coverage: 14:298/810 of query aligns to 6:289/449 of P08660
- K8 (= K16) mutation to R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
- E119 (= E130) mutation to D: Increases KM for aspartate about 3000-fold.
- R198 (= R207) mutation to K: Increases KM for aspartate about 200-fold.
- D202 (= D211) 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)
32% identity, 35% coverage: 14:298/810 of query aligns to 4:287/447 of 2j0xA
Sites not aligning to the query:
2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
32% identity, 35% coverage: 14:298/810 of query aligns to 4:287/447 of 2j0wA
- binding adenosine-5'-diphosphate: T219 (≠ S230), D220 (= D231), I224 (≠ V235), Y225 (= Y236), D228 (= D239), R230 (= R241), K255 (≠ P266), V256 (= V267)
- binding aspartic acid: S37 (= S48), T43 (= T54), E117 (= E130), F182 (= F193), R196 (= R207), G197 (≠ N208), S199 (= S210)
3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
28% identity, 48% coverage: 14:401/810 of query aligns to 3:403/458 of 3c1nA