SitesBLAST
Comparing WP_034525942.1 NCBI__GCF_000740055.1:WP_034525942.1 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
45% identity, 98% coverage: 3:394/398 of query aligns to 3:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
45% identity, 98% coverage: 3:394/398 of query aligns to 3:391/395 of 7fj8A
1tuuA Acetate kinase crystallized with atpgs (see paper)
47% identity, 98% coverage: 3:394/398 of query aligns to 2:395/399 of 1tuuA
- active site: N7 (= N8), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E383)
- binding adenosine-5'-diphosphate: K14 (= K15), G210 (= G209), D283 (= D283), F284 (≠ Q284), R285 (= R285), G331 (= G330), I332 (≠ S331), N335 (= N334)
- binding sulfate ion: R91 (= R90), H180 (= H179), G212 (= G211)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
47% identity, 98% coverage: 3:394/398 of query aligns to 2:395/408 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 (≠ T13) 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 (= 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 (≠ A178) mutation to A: Decreases affinity for acetate.
- N211 (≠ S210) 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 (= E383) 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)
47% identity, 98% coverage: 3:394/398 of query aligns to 2:395/398 of 1tuuB
- active site: N7 (= N8), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E383)
- binding adenosine monophosphate: D283 (= D283), R285 (= R285), G331 (= G330), I332 (≠ S331), N335 (= N334), S336 (≠ G335)
- binding trihydrogen thiodiphosphate: H180 (= H179), G212 (= G211), R241 (= R240)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwsA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding cytidine-5'-triphosphate: G202 (= G209), N203 (≠ S210), G204 (= G211), D275 (= D283), L276 (≠ Q284), R277 (= R285), G323 (= G330), I324 (≠ S331), N327 (= N334)
- binding 1,2-ethanediol: V21 (≠ L21), C24 (≠ E24), H115 (= H122), N203 (≠ S210), T232 (= T239), R233 (= R240), K262 (≠ Q270)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwrA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding cytidine-5'-monophosphate: G202 (= G209), N203 (≠ S210), D275 (= D283), L276 (≠ Q284), R277 (= R285), G323 (= G330), I324 (≠ S331), N327 (= N334)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwqA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding guanosine-5'-triphosphate: H172 (= H179), N203 (≠ S210), G204 (= G211), D275 (= D283), L276 (≠ Q284), R277 (= R285), E280 (= E288), G323 (= G330), I324 (≠ S331), N327 (= N334)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwpA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding 1,2-ethanediol: S11 (= S11), H115 (= H122), K262 (≠ Q270)
- binding guanosine-5'-diphosphate: N203 (≠ S210), D275 (= D283), L276 (≠ Q284), R277 (= R285), E280 (= E288), G323 (= G330), I324 (≠ S331), N327 (= N334), S328 (≠ G335)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwoA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding guanosine-5'-monophosphate: G202 (= G209), N203 (≠ S210), D275 (= D283), L276 (≠ Q284), R277 (= R285), E280 (= E288), G323 (= G330), I324 (≠ S331), N327 (= N334)
- binding 1,2-ethanediol: E100 (= E107), N104 (≠ K111)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwnA
- active site: N8 (= N8), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E383)
- binding adenosine-5'-tetraphosphate: H172 (= H179), H200 (= H207), N203 (≠ S210), G204 (= G211), D275 (= D283), L276 (≠ Q284), R277 (= R285), G323 (= G330), I324 (≠ S331), N327 (= N334)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
37% identity, 99% coverage: 4:397/398 of query aligns to 4:392/394 of 4fwmA