SitesBLAST
Comparing BWI76_RS20235 BWI76_RS20235 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)
44% identity, 98% coverage: 6:398/400 of query aligns to 3:395/399 of 1tuuA
- active site: N7 (= N10), R91 (= R91), H180 (= H182), R241 (= R243), E384 (= E387)
- binding adenosine-5'-diphosphate: K14 (= K17), G210 (= G212), N211 (= N213), D283 (= D285), F284 (≠ C286), R285 (= R287), A330 (≠ G332), G331 (= G333), I332 (= I334), N335 (= N337), S336 (≠ A338)
- binding sulfate ion: R91 (= R91), H123 (= H123), H180 (= H182), N211 (= N213), G212 (= G214), R241 (= R243)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
44% identity, 98% coverage: 6:398/400 of query aligns to 3:395/408 of P38502
- N7 (= N10) 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 (= S13) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S15) 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 (= K17) 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 (= D150) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (≠ A181) mutation to A: Decreases affinity for acetate.
- N211 (= N213) mutation to A: Slightly reduced enzyme activity.
- P232 (= P234) mutation to A: Decreases affinity for acetate.
- R241 (= R243) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E387) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
1tuyB Acetate kinase complexed with adp, alf3 and acetate (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 3:395/398 of 1tuyB
- active site: N7 (= N10), R91 (= R91), H180 (= H182), R241 (= R243), E384 (= E387)
- binding adenosine-5'-diphosphate: L209 (= L211), G210 (= G212), N211 (= N213), D283 (= D285), F284 (≠ C286), R285 (= R287), A330 (≠ G332), G331 (= G333), I332 (= I334), N335 (= N337), S336 (≠ A338), R362 (= R365)
- binding aluminum fluoride: H180 (= H182), G212 (= G214)
1tuuB Acetate kinase crystallized with atpgs (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 3:395/398 of 1tuuB
- active site: N7 (= N10), R91 (= R91), H180 (= H182), R241 (= R243), E384 (= E387)
- binding adenosine monophosphate: G210 (= G212), N211 (= N213), D283 (= D285), F284 (≠ C286), R285 (= R287), G331 (= G333), I332 (= I334), N335 (= N337), S336 (≠ A338), R362 (= R365)
- binding trihydrogen thiodiphosphate: H180 (= H182), N211 (= N213), G212 (= G214), R241 (= R243)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwsA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding cytidine-5'-triphosphate: H172 (= H182), H200 (= H210), G202 (= G212), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ C286), R277 (= R287), G322 (= G332), G323 (= G333), I324 (= I334), N327 (= N337)
- binding 1,2-ethanediol: S11 (= S13), H115 (= H123), E159 (≠ S169), L164 (≠ H174), N203 (= N213), T232 (= T242), R233 (= R243), R233 (= R243), K262 (= K272)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwrA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding cytidine-5'-monophosphate: G202 (= G212), N203 (= N213), D275 (= D285), L276 (≠ C286), R277 (= R287), G323 (= G333), I324 (= I334), N327 (= N337)
- binding 1,2-ethanediol: L90 (≠ K98), E100 (≠ S108), N104 (≠ G112)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwqA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding 1,2-ethanediol: H172 (= H182), M220 (= M230), P224 (= P234), R233 (= R243)
- binding guanosine-5'-triphosphate: H172 (= H182), H200 (= H210), G202 (= G212), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ C286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337), S328 (≠ A338)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwpA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding 1,2-ethanediol: S11 (= S13), H115 (= H123), Y160 (≠ L170), S163 (≠ E173), R233 (= R243), K262 (= K272)
- binding guanosine-5'-diphosphate: G202 (= G212), N203 (= N213), D275 (= D285), L276 (≠ C286), R277 (= R287), E280 (= E290), G322 (= G332), G323 (= G333), I324 (= I334), N327 (= N337), S328 (≠ A338)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwoA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding guanosine-5'-monophosphate: G202 (= G212), N203 (= N213), D275 (= D285), L276 (≠ C286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337), S328 (≠ A338)
- binding 1,2-ethanediol: L90 (≠ K98), F91 (≠ Y99), E100 (≠ S108), N104 (≠ G112), G340 (= G350), G343 (= G353), Q368 (≠ R378)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwnA
- active site: N8 (= N10), R83 (= R91), H172 (= H182), R233 (= R243), E378 (= E387)
- binding adenosine-5'-tetraphosphate: H172 (= H182), H200 (= H210), G202 (= G212), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ C286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337), S328 (≠ A338)
- binding 1,2-ethanediol: D140 (= D150), H172 (= H182), M220 (= M230), P224 (= P234), R233 (= R243)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
42% identity, 99% coverage: 5:398/400 of query aligns to 3:389/394 of 4fwmA