SitesBLAST
Comparing WP_041267424.1 NCBI__GCF_000022265.1:WP_041267424.1 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)
52% identity, 95% coverage: 1:400/421 of query aligns to 1:397/399 of 1tuuA
- active site: N7 (= N7), R91 (= R91), H180 (= H180), R241 (= R241), E384 (= E387)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G210), D283 (= D283), F284 (≠ R284), R285 (= R285), G331 (= G331), I332 (≠ V332), N335 (≠ M335)
- binding sulfate ion: R91 (= R91), H180 (= H180), G212 (= G212)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
52% identity, 95% coverage: 1:400/421 of query aligns to 1:397/408 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 (= 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 (= D148) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F179) mutation to A: Decreases affinity for acetate.
- N211 (= N211) mutation to A: Slightly reduced enzyme activity.
- P232 (= P232) mutation to A: Decreases affinity for acetate.
- R241 (= R241) 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)
52% identity, 95% coverage: 1:400/421 of query aligns to 1:397/398 of 1tuuB
- active site: N7 (= N7), R91 (= R91), H180 (= H180), R241 (= R241), E384 (= E387)
- binding adenosine monophosphate: D283 (= D283), R285 (= R285), G331 (= G331), I332 (≠ V332), N335 (≠ M335), S336 (≠ G336)
- binding trihydrogen thiodiphosphate: H180 (= H180), G212 (= G212), R241 (= R241)
7fj9A Kpacka (pduw) with amppnp complex structure
42% identity, 93% coverage: 3:395/421 of query aligns to 4:388/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
42% identity, 93% coverage: 3:395/421 of query aligns to 4:388/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
43% identity, 93% coverage: 3:392/421 of query aligns to 4:370/376 of 4ijnA
- active site: N8 (= N7), R72 (= R91), H161 (= H180), R222 (= R241), E365 (= E387)
- binding adenosine monophosphate: G191 (= G210), N192 (= N211), D263 (vs. gap), F264 (= F281), R265 (≠ T282), G311 (= G331), V312 (= V332), N315 (≠ M335), V316 (≠ G336)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
41% identity, 95% coverage: 3:401/421 of query aligns to 6:381/381 of 4iz9A
- active site: N10 (= N7), R74 (= R91), H163 (= H180), R224 (= R241), E367 (= E387)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K14), G193 (= G210), N194 (= N211), D265 (≠ R280), F266 (= F281), R267 (≠ T282), G313 (= G331), I314 (≠ V332), N317 (≠ M335), D318 (≠ G336)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
41% identity, 93% coverage: 3:394/421 of query aligns to 4:385/394 of 4fwsA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding cytidine-5'-triphosphate: G202 (= G210), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
- binding 1,2-ethanediol: V21 (≠ W20), C24 (≠ K23), H115 (= H123), N203 (= N211), T232 (= T240), R233 (= R241), K262 (= K270)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
41% identity, 93% coverage: 3:394/421 of query aligns to 4:385/394 of 4fwrA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding cytidine-5'-monophosphate: G202 (= G210), N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
41% identity, 93% coverage: 3:394/421 of query aligns to 4:385/394 of 4fwqA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding guanosine-5'-triphosphate: H172 (= H180), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), E280 (≠ I288), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
41% identity, 93% coverage: 3:394/421 of query aligns to 4:385/394 of 4fwpA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H123), K262 (= K270)
- binding guanosine-5'-diphosphate: N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), E280 (≠ I288), G323 (= G331), I324 (≠ V332), N327 (≠ M335), S328 (≠ G336)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
41% identity, 93% coverage: 3:394/421 of query aligns to 4:385/394 of 4fwoA