SitesBLAST
Comparing WP_043744492.1 NCBI__GCF_000009985.1:WP_043744492.1 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)
Q07607 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; Protein MosA; EC 4.3.3.7 from Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
56% identity, 100% coverage: 1:290/290 of query aligns to 1:291/292 of Q07607
- K161 (= K160) active site, Schiff-base intermediate with substrate
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)
59% identity, 100% coverage: 1:290/290 of query aligns to 1:293/294 of Q8UGL3
- T45 (= T44) binding
- P49 (= P48) L-lysine inhibitor binding; via carbonyl oxygen
- H56 (= H55) L-lysine inhibitor binding
- N80 (= N79) L-lysine inhibitor binding
- E84 (= E83) L-lysine inhibitor binding
- Y106 (= Y105) L-lysine inhibitor binding
- K162 (= K160) active site, Schiff-base intermediate with substrate
4i7wA Agrobacterium tumefaciens dhdps with lysine and pyruvate
58% identity, 100% coverage: 1:290/290 of query aligns to 1:293/294 of 4i7wA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K162 (= K160), I204 (= I202)
- binding lysine: S48 (= S47), P49 (= P48), L51 (= L50), S52 (= S51), H53 (= H52), H56 (= H55), N80 (= N79), E84 (= E83), Y106 (= Y105)
7mjfA Crystal structure of candidatus liberibacter solanacearum dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site
49% identity, 100% coverage: 1:289/290 of query aligns to 1:293/296 of 7mjfA
- binding (4R)-4-oxidanyl-2-oxidanylidene-heptanedioic acid: A8 (= A8), G43 (= G42), T44 (= T43), T45 (= T44), Y133 (= Y132), N135 (≠ I134), R138 (= R137), K162 (= K160), G187 (= G185), I204 (= I202), V206 (= V204)
- binding (4S)-4-hydroxy-2-oxoheptanedioic acid: A8 (= A8), G43 (= G42), T44 (= T43), T45 (= T44), Y133 (= Y132), N135 (≠ I134), R138 (= R137), K162 (= K160), G187 (= G185), I204 (= I202)
7lvlA Dihydrodipicolinate synthase bound with allosteric inhibitor (s)- lysine from candidatus liberibacter solanacearum
49% identity, 100% coverage: 1:289/290 of query aligns to 1:293/296 of 7lvlA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K162 (= K160), I204 (= I202)
- binding lysine: S48 (= S47), S49 (≠ P48), L51 (= L50), S52 (= S51), H56 (= H55), N80 (= N79), E84 (= E83), Y106 (= Y105)
4dxvA Crystal structure of dihydrodipicolinate synthase from acinetobacter baumannii complexed with mg and cl ions at 1.80 a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 4dxvA
3u8gA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with oxalic acid at 1.80 a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 3u8gA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K161 (= K160), I203 (= I202)
- binding oxalate ion: A8 (= A8), V40 (= V39), G43 (= G42), T44 (= T43), T45 (= T44), L101 (= L100), Y133 (= Y132), K161 (= K160)
3tdfA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 2-ketobutanoic acid at 1.99 a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 3tdfA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K161 (= K160), I203 (= I202)
- binding 2-ketobutyric acid: A8 (= A8), G43 (= G42), T44 (= T43), T45 (= T44), Y133 (= Y132), K161 (= K160), I203 (= I202)
3tceA Crystal structure of the complex of dihydrodipicolinate synthase from acinetobacter baumannii with 5-hydroxylysine at 2.6 a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 3tceA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K161 (= K160), I203 (= I202)
- binding 5-hydroxylysine: A48 (≠ S47), S49 (≠ P48), L51 (= L50), S52 (= S51), M53 (≠ H52), H56 (= H55), Y106 (= Y105)
3rk8A Crystal structure of the chloride inhibited dihydrodipicolinate synthase from acinetobacter baumannii complexed with pyruvate at 1.8 a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 3rk8A
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K161 (= K160), I203 (= I202)
- binding pyruvic acid: Y133 (= Y132), R138 (= R137), K161 (= K160), G186 (= G185), F244 (= F243), N248 (≠ S247)
3pueB Crystal structure of the complex of dhydrodipicolinate synthase from acinetobacter baumannii with lysine at 2.6a resolution
47% identity, 100% coverage: 2:290/290 of query aligns to 2:291/291 of 3pueB
2atsA Dihydrodipicolinate synthase co-crystallised with (s)-lysine
47% identity, 100% coverage: 1:290/290 of query aligns to 1:292/292 of 2atsA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), K161 (= K160), I203 (= I202)
- binding d-lysine: S48 (= S47), A49 (≠ P48), L51 (= L50), H53 (= H52), H56 (= H55), N80 (= N79), E84 (= E83), Y106 (= Y105)
P0A6L2 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 from Escherichia coli (strain K12) (see 7 papers)
47% identity, 100% coverage: 1:290/290 of query aligns to 1:292/292 of P0A6L2
- T44 (= T43) 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 (= T44) binding
- Y107 (= Y106) 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 (= Y132) mutation to F: Reduced kcat by 99.7%. Reduced affinity for both substrates.
- R138 (= R137) mutation R->A,H: Strongly increased KM for L-aspartate 4-semialdehyde. No effect on KM for pyruvate. Reduced activity by 99.7%.
- K161 (= K160) 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 (≠ Q196) 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 (= I202) binding
5t25A Kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia coli.
47% identity, 100% coverage: 1:290/290 of query aligns to 2:293/293 of 5t25A
- active site: T45 (= T43), Y108 (= Y106), Y134 (= Y132), R139 (= R137), K162 (= K160), I204 (= I202)
- binding lysine: S49 (= S47), A50 (≠ P48), L52 (= L50), H54 (= H52), H57 (= H55), N81 (= N79), E85 (= E83), Y107 (= Y105)
3i7sA Dihydrodipicolinate synthase mutant - k161a - with the substrate pyruvate bound in the active site. (see paper)
47% identity, 100% coverage: 1:290/290 of query aligns to 1:292/292 of 3i7sA
- active site: T44 (= T43), Y107 (= Y106), Y133 (= Y132), R138 (= R137), R161 (≠ K160), I203 (= I202)
- binding pyruvic acid: A8 (= A8), G43 (= G42), T44 (= T43), T45 (= T44), L101 (= L100), Y133 (= Y132)
Q9X1K9 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
42% identity, 100% coverage: 1:290/290 of query aligns to 1:294/294 of Q9X1K9