SitesBLAST
Comparing Dsui_3033 FitnessBrowser__PS:Dsui_3033 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 18 hits to proteins with known functional sites (download)
1tuuA Acetate kinase crystallized with atpgs (see paper)
40% identity, 98% coverage: 5:395/397 of query aligns to 3:396/399 of 1tuuA
- active site: N7 (= N9), R91 (= R98), H180 (= H186), R241 (= R245), E384 (= E383)
- binding adenosine-5'-diphosphate: K14 (= K16), G210 (= G214), D283 (= D287), F284 (≠ M288), R285 (= R289), G331 (= G332), I332 (= I333), N335 (≠ H336)
- binding sulfate ion: R91 (= R98), H180 (= H186), G212 (= G216)
1tuuB Acetate kinase crystallized with atpgs (see paper)
40% identity, 98% coverage: 5:395/397 of query aligns to 3:396/398 of 1tuuB
- active site: N7 (= N9), R91 (= R98), H180 (= H186), R241 (= R245), E384 (= E383)
- binding adenosine monophosphate: D283 (= D287), R285 (= R289), G331 (= G332), I332 (= I333), N335 (≠ H336), S336 (≠ A337)
- binding trihydrogen thiodiphosphate: H180 (= H186), G212 (= G216), R241 (= R245)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
40% identity, 98% coverage: 5:395/397 of query aligns to 3:396/408 of P38502
- N7 (= N9) 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 (= S12) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S14) 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 (= K16) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R98) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V100) mutation to A: Decreases affinity for acetate.
- L122 (= L129) mutation to A: Decreases affinity for acetate.
- D148 (= D155) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F185) mutation to A: Decreases affinity for acetate.
- N211 (= N215) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A236) mutation to A: Decreases affinity for acetate.
- R241 (= R245) 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.
7fj9A Kpacka (pduw) with amppnp complex structure
40% identity, 99% coverage: 2:394/397 of query aligns to 1:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
40% identity, 99% coverage: 2:394/397 of query aligns to 1:391/395 of 7fj8A
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding cytidine-5'-triphosphate: G202 (= G214), N203 (= N215), G204 (= G216), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
- binding 1,2-ethanediol: V21 (≠ L22), C24 (≠ A30), H115 (= H130), N203 (= N215), T232 (= T244), R233 (= R245), K262 (= K274)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding cytidine-5'-monophosphate: G202 (= G214), N203 (= N215), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding guanosine-5'-triphosphate: H172 (= H186), N203 (= N215), G204 (= G216), D275 (= D287), L276 (≠ M288), R277 (= R289), E280 (≠ L292), G323 (= G332), I324 (= I333), N327 (≠ H336)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding 1,2-ethanediol: S11 (= S12), H115 (= H130), K262 (= K274)
- binding guanosine-5'-diphosphate: N203 (= N215), D275 (= D287), L276 (≠ M288), R277 (= R289), E280 (≠ L292), G323 (= G332), I324 (= I333), N327 (≠ H336), S328 (≠ A337)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwoA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding guanosine-5'-monophosphate: G202 (= G214), N203 (= N215), D275 (= D287), L276 (≠ M288), R277 (= R289), E280 (≠ L292), G323 (= G332), I324 (= I333), N327 (≠ H336)
- binding 1,2-ethanediol: E100 (≠ N115), N104 (≠ H119)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwnA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding adenosine-5'-tetraphosphate: H172 (= H186), H200 (= H212), N203 (= N215), G204 (= G216), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwmA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding adenosine-5'-triphosphate: H172 (= H186), H200 (= H212), N203 (= N215), G204 (= G216), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
- binding 1,2-ethanediol: H172 (= H186), R233 (= R245)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 4fwkA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding adenosine monophosphate: G202 (= G214), N203 (= N215), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
- binding 1,2-ethanediol: D103 (≠ E118), N104 (≠ H119), R107 (= R122)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 2e1zA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N9), R83 (= R98), H115 (= H130), G202 (= G214), N203 (= N215), G204 (= G216), P224 (≠ A236), R233 (= R245), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 1x3nA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G214), N203 (= N215), G204 (= G216), D275 (= D287), L276 (≠ M288), R277 (= R289), G323 (= G332), I324 (= I333), N327 (≠ H336)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 5:388/397 of query aligns to 4:383/394 of 1x3mA
- active site: N8 (= N9), R83 (= R98), H172 (= H186), R233 (= R245), E378 (= E383)
- binding adenosine-5'-diphosphate: G202 (= G214), N203 (= N215), D275 (= D287), L276 (≠ M288), R277 (= R289), G322 (= G331), G323 (= G332), I324 (= I333), N327 (≠ H336)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
38% identity, 97% coverage: 5:389/397 of query aligns to 4:371/376 of 4ijnA
- active site: N8 (= N9), R72 (= R98), H161 (= H186), R222 (= R245), E365 (= E383)
- binding adenosine monophosphate: G191 (= G214), N192 (= N215), D263 (≠ P286), F264 (vs. gap), R265 (vs. gap), G311 (= G332), V312 (≠ I333), N315 (≠ H336), V316 (≠ A337)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
37% identity, 99% coverage: 3:395/397 of query aligns to 4:379/381 of 4iz9A
- active site: N10 (= N9), R74 (= R98), H163 (= H186), R224 (= R245), E367 (= E383)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K16), G193 (= G214), N194 (= N215), D265 (≠ P286), F266 (vs. gap), R267 (vs. gap), G313 (= G332), I314 (= I333), N317 (≠ H336), D318 (≠ A337)
Query Sequence
>Dsui_3033 FitnessBrowser__PS:Dsui_3033
MTRAVLTLNAGSSSIKFSLYELENGGGIAAEPVLSGQIDGIGVKAHIKAKDDKGKKLDDV
DIPLQGDAESQHHEALEFLISWLHDHEKGWKIVAVGHRVVHGGERYSRPMKLDDNIIEHL
TRLIPLAPLHQPHNLDGVDALRTMMPEVPQVACFDTAFHRTQAPVAQAFALPRWITGEGV
KRYGFHGLSYEYIARVLPDYSPRANGRVVVAHLGNGASMCGMVDRKSQVSTMGFTAVEGL
MMGTRTGALDPGVMLYLMENKGMDVKALTKLLYKESGLLGVSGISPDMRTLLASDKPEAK
EAVDLFCYRVVRELGSLAAAIGGIDALVFTGGIGEHAAEVRRRVCLQASWLGISIDESAN
ALHANRISEPRSTVDVLVIPTNEEWMIARHTATLLNL
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory