SitesBLAST
Comparing WP_079556774.1 NCBI__GCF_002201795.1:WP_079556774.1 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)
1tuuA Acetate kinase crystallized with atpgs (see paper)
50% identity, 99% coverage: 1:399/405 of query aligns to 1:396/399 of 1tuuA
- active site: N7 (= N7), R91 (= R93), H180 (= H182), R241 (= R243), E384 (= E387)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G212), D283 (= D285), F284 (≠ M286), R285 (= R287), G331 (= G333), I332 (= I334), N335 (= N337)
- binding sulfate ion: R91 (= R93), H180 (= H182), G212 (= G214)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
50% identity, 99% coverage: 1:399/405 of query aligns to 1:396/408 of P38502
- N7 (= N7) 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 (= S10) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S12) 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 (= K14) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R93) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V95) mutation to A: Decreases affinity for acetate.
- L122 (= L124) 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 (= F181) 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.
1tuuB Acetate kinase crystallized with atpgs (see paper)
50% identity, 99% coverage: 1:399/405 of query aligns to 1:396/398 of 1tuuB
- active site: N7 (= N7), R91 (= R93), H180 (= H182), R241 (= R243), E384 (= E387)
- binding adenosine monophosphate: D283 (= D285), R285 (= R287), G331 (= G333), I332 (= I334), N335 (= N337), S336 (≠ G338)
- binding trihydrogen thiodiphosphate: H180 (= H182), G212 (= G214), R241 (= R243)
7fj9A Kpacka (pduw) with amppnp complex structure
45% identity, 98% coverage: 2:399/405 of query aligns to 3:392/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
45% identity, 98% coverage: 2:399/405 of query aligns to 3:392/395 of 7fj8A
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwsA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding cytidine-5'-triphosphate: G202 (= G212), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ M286), R277 (= R287), G323 (= G333), I324 (= I334), N327 (= N337)
- binding 1,2-ethanediol: V21 (≠ G22), C24 (≠ W25), H115 (= H125), N203 (= N213), T232 (= T242), R233 (= R243), K262 (= K272)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwrA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding cytidine-5'-monophosphate: G202 (= G212), N203 (= N213), D275 (= D285), L276 (≠ M286), R277 (= R287), G323 (= G333), I324 (= I334), N327 (= N337)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwqA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding guanosine-5'-triphosphate: H172 (= H182), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ M286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwpA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H125), K262 (= K272)
- binding guanosine-5'-diphosphate: N203 (= N213), D275 (= D285), L276 (≠ M286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337), S328 (≠ G338)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwoA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding guanosine-5'-monophosphate: G202 (= G212), N203 (= N213), D275 (= D285), L276 (≠ M286), R277 (= R287), E280 (= E290), G323 (= G333), I324 (= I334), N327 (= N337)
- binding 1,2-ethanediol: E100 (= E110), N104 (≠ K114)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwnA
- active site: N8 (= N7), R83 (= R93), H172 (= H182), R233 (= R243), E378 (= E387)
- binding adenosine-5'-tetraphosphate: H172 (= H182), H200 (= H210), N203 (= N213), G204 (= G214), D275 (= D285), L276 (≠ M286), R277 (= R287), G323 (= G333), I324 (= I334), N327 (= N337)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
44% identity, 97% coverage: 3:395/405 of query aligns to 4:386/394 of 4fwmA