SitesBLAST
Comparing WP_061533398.1 NCBI__GCF_001584165.1:WP_061533398.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
7fj9A Kpacka (pduw) with amppnp complex structure
40% identity, 95% coverage: 14:400/406 of query aligns to 4:389/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
40% identity, 95% coverage: 14:400/406 of query aligns to 4:389/395 of 7fj8A
1tuuA Acetate kinase crystallized with atpgs (see paper)
39% identity, 97% coverage: 14:405/406 of query aligns to 3:398/399 of 1tuuA
- active site: N7 (= N18), R91 (= R99), H180 (= H187), R241 (= R247), E384 (= E391)
- binding adenosine-5'-diphosphate: K14 (= K25), G210 (= G216), D283 (= D289), F284 (= F294), R285 (≠ A295), G331 (= G340), I332 (= I341), N335 (≠ H344)
- binding sulfate ion: R91 (= R99), H180 (= H187), G212 (= G218)
1tuuB Acetate kinase crystallized with atpgs (see paper)
39% identity, 97% coverage: 14:405/406 of query aligns to 3:398/398 of 1tuuB
- active site: N7 (= N18), R91 (= R99), H180 (= H187), R241 (= R247), E384 (= E391)
- binding adenosine monophosphate: D283 (= D289), R285 (≠ A295), G331 (= G340), I332 (= I341), N335 (≠ H344), S336 (= S345)
- binding trihydrogen thiodiphosphate: H180 (= H187), G212 (= G218), R241 (= R247)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
39% identity, 97% coverage: 14:405/406 of query aligns to 3:398/408 of P38502
- N7 (= N18) 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 (= S21) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S23) 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 (= K25) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R99) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V101) mutation to A: Decreases affinity for acetate.
- L122 (= L130) mutation to A: Decreases affinity for acetate.
- D148 (= D156) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F186) mutation to A: Decreases affinity for acetate.
- N211 (≠ S217) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A238) mutation to A: Decreases affinity for acetate.
- R241 (= R247) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E391) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding cytidine-5'-triphosphate: G202 (= G216), N203 (≠ S217), G204 (= G218), D275 (= D289), L276 (≠ P290), R277 (≠ P291), G323 (= G340), I324 (= I341), N327 (≠ H344)
- binding 1,2-ethanediol: V21 (vs. gap), C24 (≠ S32), H115 (= H131), N203 (≠ S217), T232 (= T246), R233 (= R247), K262 (≠ H276)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding cytidine-5'-monophosphate: G202 (= G216), N203 (≠ S217), D275 (= D289), L276 (≠ P290), R277 (≠ P291), G323 (= G340), I324 (= I341), N327 (≠ H344)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding guanosine-5'-triphosphate: H172 (= H187), N203 (≠ S217), G204 (= G218), D275 (= D289), L276 (≠ P290), R277 (≠ P291), E280 (= E297), G323 (= G340), I324 (= I341), N327 (≠ H344)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding 1,2-ethanediol: S11 (= S21), H115 (= H131), K262 (≠ H276)
- binding guanosine-5'-diphosphate: N203 (≠ S217), D275 (= D289), L276 (≠ P290), R277 (≠ P291), E280 (= E297), G323 (= G340), I324 (= I341), N327 (≠ H344), S328 (= S345)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwoA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding guanosine-5'-monophosphate: G202 (= G216), N203 (≠ S217), D275 (= D289), L276 (≠ P290), R277 (≠ P291), E280 (= E297), G323 (= G340), I324 (= I341), N327 (≠ H344)
- binding 1,2-ethanediol: E100 (= E116), N104 (≠ D120)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwnA
- active site: N8 (= N18), R83 (= R99), H172 (= H187), R233 (= R247), E378 (= E391)
- binding adenosine-5'-tetraphosphate: H172 (= H187), H200 (= H214), N203 (≠ S217), G204 (= G218), D275 (= D289), L276 (≠ P290), R277 (≠ P291), G323 (= G340), I324 (= I341), N327 (≠ H344)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 94% coverage: 14:396/406 of query aligns to 4:383/394 of 4fwmA