SitesBLAST
Comparing AO353_14875 FitnessBrowser__pseudo3_N2E3:AO353_14875 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)
3na8A Crystal structure of a putative dihydrodipicolinate synthetase from pseudomonas aeruginosa
29% identity, 87% coverage: 9:274/305 of query aligns to 5:271/291 of 3na8A
2atsA Dihydrodipicolinate synthase co-crystallised with (s)-lysine
30% identity, 94% coverage: 7:293/305 of query aligns to 2:289/292 of 2atsA
- active site: T44 (= T49), Y107 (≠ S114), Y133 (= Y138), R138 (≠ I143), K161 (= K166), I203 (≠ V208)
- binding d-lysine: A49 (≠ T54), L51 (= L56), H53 (≠ T58), H56 (≠ K61), N80 (= N89), E84 (≠ V93), Y106 (= Y113)
P0A6L2 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 from Escherichia coli (strain K12) (see 7 papers)
30% identity, 94% coverage: 7:293/305 of query aligns to 2:289/292 of P0A6L2
- T44 (= T49) mutation to S: 8% of wild-type activity. 4-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA.; mutation to V: Reduced kcat by 99.9%.
- T45 (≠ V50) binding pyruvate
- Y107 (≠ S114) mutation to F: Reduced kcat by 90%.; mutation to W: Reduced activity by 95%. Reduced affinity for both substrates. Exists as a mixture of monomer, dimer and tetramer in solution. Has significantly lower thermal stability than the wild-type enzyme.
- Y133 (= Y138) mutation to F: Reduced kcat by 99.7%. Reduced affinity for both substrates.
- R138 (≠ I143) mutation R->A,H: Strongly increased KM for L-aspartate 4-semialdehyde. No effect on KM for pyruvate. Reduced activity by 99.7%.
- K161 (= K166) mutation to A: 0.1% of wild-type activity. 3-fold decrease in affinity for pyruvate, and 2-fold decrease in that for (S)-ASA.; mutation to R: 0.35% of wild-type activity. 3-fold decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA.
- L197 (≠ V202) mutation L->Y,D: 1.4 to 2.5% of wild-type activity. Decrease in affinity for pyruvate, but nearly no change in that for (S)-ASA. Exists as a dimer in solution.
- I203 (≠ V208) binding pyruvate
5t25A Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia coli.
30% identity, 94% coverage: 7:293/305 of query aligns to 3:290/293 of 5t25A
- active site: T45 (= T49), Y108 (≠ S114), Y134 (= Y138), R139 (≠ I143), K162 (= K166), I204 (≠ V208)
- binding lysine: A50 (≠ T54), L52 (= L56), H54 (≠ T58), N81 (= N89), E85 (≠ V93), Y107 (= Y113)
4ptnA Crystal structure of yage, a kdg aldolase protein in complex with magnesium cation coordinated l-glyceraldehyde (see paper)
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 4ptnA
4onvA Crystal structure of yage, a kdg aldolase protein in complex with 2- keto-3-deoxy gluconate
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 4onvA
- active site: S45 (≠ T49), Y108 (≠ V112), Y134 (= Y138), L139 (≠ I143), K163 (= K166), I208 (≠ V208)
- binding 2-keto-3-deoxygluconate: P9 (≠ A13), F41 (≠ V45), G44 (= G48), S45 (≠ T49), Y134 (= Y138), K163 (= K166), G191 (= G191), Y192 (≠ L192), I208 (≠ V208), S209 (= S209)
4oe7D Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 4oe7D
- active site: S45 (≠ T49), Y108 (≠ V112), Y134 (= Y138), L139 (≠ I143), K163 (= K166), I208 (≠ V208)
- binding (4S)-4-hydroxy-2,5-dioxopentanoic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), K163 (= K166), T165 (vs. gap), G191 (= G191)
- binding (4R)-4-hydroxy-2,5-dioxopentanoic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), F136 (≠ N140), K163 (= K166), T165 (vs. gap), G191 (= G191)
- binding magnesium ion: P9 (≠ A13), G46 (≠ V50)
4oe7B Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 4oe7B
- active site: S45 (≠ T49), Y108 (≠ V112), Y134 (= Y138), L139 (≠ I143), K163 (= K166), I208 (≠ V208)
- binding (4S)-4-hydroxy-2,5-dioxopentanoic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), F136 (≠ N140), K163 (= K166), T165 (vs. gap), G191 (= G191)
- binding (4R)-4-hydroxy-2,5-dioxopentanoic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), F136 (≠ N140), K163 (= K166), G191 (= G191)
4oe7A Crystal structure of yage, a kdg aldolase protein, in complex with aldol condensed product of pyruvate and glyoxal
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 4oe7A
- active site: S45 (≠ T49), Y108 (≠ V112), Y134 (= Y138), L139 (≠ I143), K163 (= K166), I208 (≠ V208)
- binding pyruvic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), K163 (= K166), I208 (≠ V208)
3nevA Crystal structure of yage, a prophage protein from e. Coli k12 in complex with kdgal (see paper)
29% identity, 91% coverage: 7:283/305 of query aligns to 3:284/298 of 3nevA
- active site: S45 (≠ T49), Y108 (≠ V112), Y134 (= Y138), L139 (≠ I143), K163 (= K166), I208 (≠ V208)
- binding 3-deoxy-d-lyxo-hexonic acid: P9 (≠ A13), G44 (= G48), S45 (≠ T49), G46 (≠ V50), Y134 (= Y138), F136 (≠ N140), K163 (= K166), T165 (vs. gap), G191 (= G191), A210 (≠ G210)
3i7sA Dihydrodipicolinate synthase mutant - k161a - with the substrate pyruvate bound in the active site. (see paper)
30% identity, 94% coverage: 7:293/305 of query aligns to 2:289/292 of 3i7sA
5ktlA Dihydrodipicolinate synthase from the industrial and evolutionarily important cyanobacteria anabaena variabilis. (see paper)
29% identity, 94% coverage: 6:291/305 of query aligns to 4:290/295 of 5ktlA
Q8UGL3 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 from Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) (see paper)
31% identity, 78% coverage: 7:244/305 of query aligns to 2:240/294 of Q8UGL3
- T45 (≠ V50) binding pyruvate
- P49 (≠ T54) L-lysine inhibitor binding; via carbonyl oxygen
- H56 (≠ K61) L-lysine inhibitor binding
- N80 (≠ F85) L-lysine inhibitor binding
- E84 (≠ N89) L-lysine inhibitor binding
- Y106 (= Y113) L-lysine inhibitor binding
- K162 (= K166) active site, Schiff-base intermediate with substrate
4i7wA Agrobacterium tumefaciens dhdps with lysine and pyruvate
31% identity, 78% coverage: 7:244/305 of query aligns to 2:240/294 of 4i7wA
- active site: T44 (= T49), Y107 (≠ S114), Y133 (= Y138), R138 (≠ I143), K162 (= K166), I204 (≠ V208)
- binding lysine: S48 (≠ N53), P49 (≠ T54), L51 (= L56), H56 (≠ K61), N80 (≠ F85), E84 (≠ N89), Y106 (= Y113)
7mjfA Crystal structure of candidatus liberibacter solanacearum dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site
29% identity, 89% coverage: 11:282/305 of query aligns to 6:279/296 of 7mjfA
- binding (4R)-4-oxidanyl-2-oxidanylidene-heptanedioic acid: A8 (= A13), T44 (= T49), T45 (≠ V50), Y133 (= Y138), R138 (≠ I143), K162 (= K166), G187 (= G191)
- binding (4S)-4-hydroxy-2-oxoheptanedioic acid: A8 (= A13), T44 (= T49), T45 (≠ V50), Y133 (= Y138), R138 (≠ I143), K162 (= K166), G187 (= G191)
7lvlA Dihydrodipicolinate synthase bound with allosteric inhibitor (s)- lysine from candidatus liberibacter solanacearum
29% identity, 89% coverage: 11:282/305 of query aligns to 6:279/296 of 7lvlA