SitesBLAST
Comparing SM_b21184 SM_b21184 acetate kinase 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)
1tuuA Acetate kinase crystallized with atpgs (see paper)
39% identity, 99% coverage: 4:392/392 of query aligns to 3:399/399 of 1tuuA
- active site: N7 (= N8), R91 (= R91), H180 (= H179), R241 (= R239), E384 (= E377)
- binding adenosine-5'-diphosphate: K14 (= K15), G210 (= G208), N211 (≠ S209), D283 (= D281), F284 (≠ M282), R285 (= R283), A330 (= A325), G331 (= G326), I332 (= I327), N335 (= N330), S336 (= S331)
- binding sulfate ion: R91 (= R91), H123 (= H123), H180 (= H179), N211 (≠ S209), G212 (= G210), R241 (= R239)
1tuyB Acetate kinase complexed with adp, alf3 and acetate (see paper)
39% identity, 99% coverage: 4:390/392 of query aligns to 3:397/398 of 1tuyB
- active site: N7 (= N8), R91 (= R91), H180 (= H179), R241 (= R239), E384 (= E377)
- binding adenosine-5'-diphosphate: L209 (= L207), G210 (= G208), N211 (≠ S209), D283 (= D281), F284 (≠ M282), R285 (= R283), A330 (= A325), G331 (= G326), I332 (= I327), N335 (= N330), S336 (= S331), R362 (vs. gap)
- binding aluminum fluoride: H180 (= H179), G212 (= G210)
1tuuB Acetate kinase crystallized with atpgs (see paper)
39% identity, 99% coverage: 4:390/392 of query aligns to 3:397/398 of 1tuuB
- active site: N7 (= N8), R91 (= R91), H180 (= H179), R241 (= R239), E384 (= E377)
- binding adenosine monophosphate: G210 (= G208), N211 (≠ S209), D283 (= D281), F284 (≠ M282), R285 (= R283), G331 (= G326), I332 (= I327), N335 (= N330), S336 (= S331), R362 (vs. gap)
- binding trihydrogen thiodiphosphate: H180 (= H179), N211 (≠ S209), G212 (= G210), R241 (= R239)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
39% identity, 99% coverage: 4:392/392 of query aligns to 3:399/408 of P38502
- N7 (= N8) mutation to A: Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate.; mutation to D: Almost abolishes catalytic activity. Strongly decreases affinity for acetate.
- S10 (= S11) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S13) mutation to A: Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity.; mutation to T: Decreases catalytic activity. Strongly decreases affinity for acetate.
- K14 (= K15) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R91) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V93) mutation to A: Decreases affinity for acetate.
- L122 (= L122) mutation to A: Decreases affinity for acetate.
- D148 (= D148) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F178) mutation to A: Decreases affinity for acetate.
- N211 (≠ S209) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A230) mutation to A: Decreases affinity for acetate.
- R241 (= R239) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E377) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
7fj9A Kpacka (pduw) with amppnp complex structure
41% identity, 98% coverage: 4:386/392 of query aligns to 4:389/395 of 7fj9A
- binding phosphoaminophosphonic acid-adenylate ester: H178 (= H179), H206 (= H206), G208 (= G208), N209 (≠ S209), G210 (= G210), D281 (= D281), Y282 (≠ M282), R283 (= R283), G328 (≠ A325), G329 (= G326), I330 (= I327), N333 (= N330), S334 (= S331)
7fj8A Kpacka (pduw) with amp complex structure
41% identity, 98% coverage: 4:386/392 of query aligns to 4:389/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
38% identity, 99% coverage: 1:388/392 of query aligns to 1:376/376 of 4ijnA
- active site: N8 (= N8), R72 (= R91), H161 (= H179), R222 (= R239), E365 (= E377)
- binding adenosine monophosphate: G191 (= G208), N192 (≠ S209), D263 (≠ N280), F264 (vs. gap), R265 (vs. gap), A310 (= A325), G311 (= G326), V312 (≠ I327), N315 (= N330), V316 (≠ S331)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding cytidine-5'-triphosphate: H172 (= H179), H200 (= H206), G202 (= G208), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), G322 (≠ A325), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: S11 (= S11), H115 (= H123), E159 (≠ T167), L164 (vs. gap), N203 (≠ S209), T232 (= T238), R233 (= R239), R233 (= R239), K262 (≠ H268)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding cytidine-5'-monophosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: L90 (≠ D98), E100 (≠ T108), N104 (≠ R112)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding 1,2-ethanediol: H172 (= H179), M220 (= M226), P224 (≠ A230), R233 (= R239)
- binding guanosine-5'-triphosphate: H172 (= H179), H200 (= H206), G202 (= G208), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), E280 (vs. gap), G323 (= G326), I324 (= I327), N327 (= N330), S328 (= S331)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding 1,2-ethanediol: S11 (= S11), H115 (= H123), Y160 (≠ F168), S163 (≠ Q171), R233 (= R239), K262 (≠ H268)
- binding guanosine-5'-diphosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), E280 (vs. gap), G322 (≠ A325), G323 (= G326), I324 (= I327), N327 (= N330), S328 (= S331)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwoA