SitesBLAST
Comparing WP_095512017.1 NCBI__GCF_002283365.1:WP_095512017.1 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)
1tuuB Acetate kinase crystallized with atpgs (see paper)
49% identity, 98% coverage: 1:395/405 of query aligns to 1:395/398 of 1tuuB
- active site: N7 (= N7), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E384)
- binding adenosine monophosphate: D283 (= D282), R285 (= R284), G331 (= G330), I332 (= I331), N335 (≠ F334), S336 (≠ A335)
- binding trihydrogen thiodiphosphate: H180 (= H179), G212 (= G211), R241 (= R240)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
49% identity, 98% coverage: 1:395/405 of query aligns to 1:395/408 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 (= R90) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V92) mutation to A: Decreases affinity for acetate.
- L122 (= L121) mutation to A: Decreases affinity for acetate.
- D148 (= D147) 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 (= N210) mutation to A: Slightly reduced enzyme activity.
- P232 (= P231) mutation to A: Decreases affinity for acetate.
- R241 (= R240) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E384) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
1tuuA Acetate kinase crystallized with atpgs (see paper)
49% identity, 98% coverage: 1:395/405 of query aligns to 1:395/399 of 1tuuA
- active site: N7 (= N7), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E384)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G209), D283 (= D282), F284 (≠ M283), R285 (= R284), G331 (= G330), I332 (= I331), N335 (≠ F334)
- binding sulfate ion: R91 (= R90), H180 (= H179), G212 (= G211)
7fj9A Kpacka (pduw) with amppnp complex structure
46% identity, 98% coverage: 3:397/405 of query aligns to 4:393/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
46% identity, 98% coverage: 3:397/405 of query aligns to 4:393/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
45% identity, 96% coverage: 1:390/405 of query aligns to 2:371/376 of 4ijnA
- active site: N8 (= N7), R72 (= R90), H161 (= H179), R222 (= R240), E365 (= E384)
- binding adenosine monophosphate: G191 (= G209), N192 (= N210), D263 (= D282), F264 (≠ M283), R265 (= R284), G311 (= G330), V312 (≠ I331), N315 (≠ F334), V316 (≠ A335)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwsA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding cytidine-5'-triphosphate: G202 (= G209), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ M283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (≠ F334)
- binding 1,2-ethanediol: V21 (≠ A20), C24 (≠ G23), H115 (= H122), N203 (= N210), T232 (= T239), R233 (= R240), K262 (≠ R269)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwrA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding cytidine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ M283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (≠ F334)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwqA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding guanosine-5'-triphosphate: H172 (= H179), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ M283), R277 (= R284), E280 (≠ L287), G323 (= G330), I324 (= I331), N327 (≠ F334)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwpA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H122), K262 (≠ R269)
- binding guanosine-5'-diphosphate: N203 (= N210), D275 (= D282), L276 (≠ M283), R277 (= R284), E280 (≠ L287), G323 (= G330), I324 (= I331), N327 (≠ F334), S328 (≠ A335)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwoA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding guanosine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ M283), R277 (= R284), E280 (≠ L287), G323 (= G330), I324 (= I331), N327 (≠ F334)
- binding 1,2-ethanediol: E100 (= E107), N104 (≠ A111)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
45% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwnA