SitesBLAST
Comparing AO356_07855 FitnessBrowser__pseudo5_N2C3_1:AO356_07855 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 hits to proteins with known functional sites (download)
1jg8D Crystal structure of threonine aldolase (low-specificity)
45% identity, 98% coverage: 1:346/353 of query aligns to 1:344/344 of 1jg8D
1lw5B X-ray structure of l-threonine aldolase (low-specificity) in complex with glycine (see paper)
45% identity, 98% coverage: 2:346/353 of query aligns to 1:343/343 of 1lw5B
- binding calcium ion: T8 (= T9), T10 (= T11), S198 (= S202), A203 (= A207), N326 (≠ D329), E329 (≠ H332)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S6 (= S7), G58 (= G59), T59 (= T60), H83 (= H84), E135 (= E139), D168 (= D172), A170 (= A174), R171 (= R175), K199 (= K203), R316 (= R319)
- binding pyridoxal-5'-phosphate: G58 (= G59), T59 (= T60), H83 (= H84), E135 (= E139), D168 (= D172), A170 (= A174), R171 (= R175), K199 (= K203)
1lw4B X-ray structure of l-threonine aldolase (low-specificity) in complex with l-allo-threonine (see paper)
45% identity, 98% coverage: 2:346/353 of query aligns to 1:343/343 of 1lw4B
- binding calcium ion: T8 (= T9), T10 (= T11), S198 (= S202), A203 (= A207), N326 (≠ D329), E329 (≠ H332)
- binding pyridoxal-5'-phosphate: G58 (= G59), T59 (= T60), H83 (= H84), E135 (= E139), D168 (= D172), A170 (= A174), R171 (= R175), K199 (= K203)
- binding 3-hydroxy-2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-butyric acid: S6 (= S7), G58 (= G59), T59 (= T60), H83 (= H84), E135 (= E139), D168 (= D172), A170 (= A174), R171 (= R175), K199 (= K203), R316 (= R319)
O07051 L-allo-threonine aldolase; L-allo-TA; L-allo-threonine acetaldehyde-lyase; EC 4.1.2.49 from Aeromonas jandaei (see paper)
40% identity, 94% coverage: 2:333/353 of query aligns to 3:327/338 of O07051
- K51 (= K50) mutation to A: No loss of activity.
- K199 (= K203) mutation K->A,C: Loss of activity.
- K224 (= K228) mutation to A: No loss of activity.
3wgcB Aeromonas jandaei l-allo-threonine aldolase h128y/s292r double mutant (see paper)
39% identity, 94% coverage: 2:333/353 of query aligns to 2:324/333 of 3wgcB
3wgbD Crystal structure of aeromonas jandaei l-allo-threonine aldolase (see paper)
40% identity, 93% coverage: 2:331/353 of query aligns to 1:314/324 of 3wgbD
- binding glycine: A166 (= A174), R167 (= R175), C192 (= C200), L193 (= L201), K195 (= K203), G196 (= G204), L197 (= L205)
- binding n-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: S6 (= S7), S57 (≠ G58), G58 (= G59), T59 (= T60), H83 (= H84), E134 (= E139), D164 (= D172), A166 (= A174), R167 (= R175), K195 (= K203), R302 (= R319)
Q8RXU4 Low-specificity L-threonine aldolase 1; Threonine aldolase 1; EC 4.1.2.48 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
37% identity, 93% coverage: 3:332/353 of query aligns to 6:339/358 of Q8RXU4
- G114 (= G109) mutation to R: In tha1-1; loss of function; 50-fold increase in seed Thr content and 2-fold decrease in seedling Gly content.
3wlxA Crystal structure of low-specificity l-threonine aldolase from escherichia coli
32% identity, 96% coverage: 2:340/353 of query aligns to 1:329/331 of 3wlxA
4rjyA Crystal structure of e. Coli l-threonine aldolase in complex with a non-covalently uncleaved bound l-serine substrate (see paper)
32% identity, 96% coverage: 2:340/353 of query aligns to 1:329/332 of 4rjyA
4lnlA Structure of escherichia coli threonine aldolase in complex with allo- thr (see paper)
32% identity, 96% coverage: 2:340/353 of query aligns to 1:329/332 of 4lnlA
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-allothreonine: S6 (= S7), G58 (= G59), T59 (= T60), H83 (= H84), E136 (= E139), D166 (= D172), A168 (= A174), R169 (= R175), K197 (= K203), R308 (= R319)
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-threonine: S6 (= S7), G58 (= G59), T59 (= T60), H83 (= H84), E136 (= E139), D166 (= D172), A168 (= A174), R169 (= R175), K197 (= K203), R308 (= R319)
- binding magnesium ion: T8 (= T9), T10 (= T11), V94 (≠ A95), S97 (≠ G98), S196 (= S202), T201 (≠ A207)
4lnjA Structure of escherichia coli threonine aldolase in unliganded form (see paper)
32% identity, 96% coverage: 2:340/353 of query aligns to 1:329/332 of 4lnjA
- binding magnesium ion: T8 (= T9), T10 (= T11), S196 (= S202), T201 (≠ A207)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G58 (= G59), T59 (= T60), H83 (= H84), E136 (= E139), D166 (= D172), A168 (= A174), K197 (= K203)
4lnmA Structure of escherichia coli threonine aldolase in complex with serine (see paper)
32% identity, 96% coverage: 2:340/353 of query aligns to 1:329/331 of 4lnmA
- binding calcium ion: T8 (= T9), T10 (= T11), V94 (≠ A95), S97 (≠ G98), S196 (= S202), T201 (≠ A207)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: T57 (≠ G58), G58 (= G59), T59 (= T60), H83 (= H84), E136 (= E139), D166 (= D172), A168 (= A174), K197 (= K203)
5vyeB Crystal structure of l-threonine aldolase from pseudomonas putida
23% identity, 61% coverage: 28:242/353 of query aligns to 30:237/344 of 5vyeB
7yj1B Cryo-em structure of spt-ormdl3 (ormdl3-deltan2) complex (see paper)
27% identity, 51% coverage: 40:220/353 of query aligns to 175:351/502 of 7yj1B
7k0lB Human serine palmitoyltransferase complex sptlc1/spltc2/ssspta, myriocin-bound (see paper)
27% identity, 51% coverage: 40:220/353 of query aligns to 167:343/492 of 7k0lB
- binding pyridoxal-5'-phosphate: G186 (= G59), H211 (= H84), E263 (= E139), A294 (= A174), H295 (≠ R175), T324 (≠ C200), T326 (≠ S202), K327 (= K203)
- binding Myriocin: H211 (= H84), S267 (≠ G143), H295 (≠ R175), K327 (= K203)
Sites not aligning to the query:
7k0kB Human serine palmitoyltransferase complex sptlc1/spltc2/ssspta, 3ks- bound (see paper)
27% identity, 51% coverage: 40:220/353 of query aligns to 167:343/492 of 7k0kB
Sites not aligning to the query:
7cqiT Cryo-em structure of the substrate-bound spt-ormdl3 complex (see paper)
27% identity, 51% coverage: 40:220/353 of query aligns to 175:351/498 of 7cqiT
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3R)-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-[2-(2-oxidanylideneheptadecylsulfanyl)ethylamino]propyl]amino]butyl] hydrogen phosphate: S214 (≠ L79), N218 (≠ Y83), H219 (= H84), V223 (≠ Y88), I235 (≠ L103)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: G194 (= G59), H219 (= H84), D300 (= D172), T332 (≠ C200), K335 (= K203)
Sites not aligning to the query:
O50584 Low specificity L-threonine aldolase; Low specificity L-TA; EC 4.1.2.48 from Pseudomonas sp. (strain NCIMB 10558) (see paper)
24% identity, 69% coverage: 31:272/353 of query aligns to 35:278/346 of O50584
- K207 (≠ I209) mutation to A: Loss of activity.; mutation to R: 1000-fold decrease in activity.
O15270 Serine palmitoyltransferase 2; Long chain base biosynthesis protein 2; LCB 2; Long chain base biosynthesis protein 2a; LCB2a; Serine-palmitoyl-CoA transferase 2; SPT 2; EC 2.3.1.50 from Homo sapiens (Human) (see 6 papers)
27% identity, 51% coverage: 40:220/353 of query aligns to 219:395/562 of O15270
- S258 (≠ L79) mutation to R: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- R302 (= R134) mutation to A: Reduces the dimerization propensity with SPTLC1; reduces the dimerization propensity with SPTLC1; when associated with A-305. Does not impair enzymatic activity; when associated with A-304 and A-305.
- R304 (vs. gap) mutation to A: Reduces the dimerization propensity with SPTLC1; when associated with A-302 and A-304. Does not impair enzymatic activity; when associated with A-302 and A-304.
- R305 (vs. gap) mutation to A: Reduces the dimerization propensity with SPTLC1; when associated with A-302 and A-304. Does not impair enzymatic activity; when associated with A-302 and A-304.
- M320 (≠ C144) mutation to Q: Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.
- V359 (= V187) to M: in HSAN1C; partial loss of normal activity as measured by reduced formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine; dbSNP:rs267607090
- T378 (≠ S202) mutation to A: Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.
- K379 (= K203) mutation to A: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- G382 (= G206) to V: in HSAN1C; complete loss of normal activity as measured by lack of formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine; dbSNP:rs267607089
Sites not aligning to the query:
- 122 Y→A: Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates. Does not affect the negative regulation by OMRDL3 and ceramides.
- 126 L→W: Some decrease in catalytic activity with L-serine and palmitoyl-CoA as substrates.
- 130 I→W: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- 134 W→A: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- 176 Y→A: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- 182 A → P: in HSAN1C; reduced activity with L-serine as substrate; increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine; dbSNP:rs864621998
- 183 R → W: in HSAN1C; late onset; slightly increased activity with L-serine as substrate; highly increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine; dbSNP:rs775437084
- 479 I→W: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
- 503 I→R: Loss of negative regulation by OMRDL3 and ceramides.
- 504 I → F: in HSAN1C; partial loss of normal activity as measured by reduced formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine; dbSNP:rs267607091
- 509 R→A: Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.
Query Sequence
>AO356_07855 FitnessBrowser__pseudo5_N2C3_1:AO356_07855
MFIDLRSDTVTKPTEGMRKAIYQAEVGDDCFGEDPTVRALEEYCANYFQKEAALFTSGGT
LSNQLAIKALTNPGDEIFLDASYHINFYESASTSAFSGVNFSLSNHDNGLFDVADLEKLH
ASKCRWSQNYALPRVVVIENTLGCKGGDIFPLQQMNDVFAYAKDIGAYRYLDGARILHAS
IASGIDVTSYTDNADLLSMCLSKGLGAPIGSIMVGSQELILRAKKYRKWFGGDLHQAGMM
AAAGLYAMQNHVERLADDHEHAALLHQLLNDIDEAPARYKGTNMVTLDISALGVAPVQFA
ALLRQKGVGGLPYNAREMRFMPHLNISRDDIHKAAGIIKATVRELSRAPETIK
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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