SitesBLAST
Comparing Synpcc7942_2079 Synpcc7942_2079 acetate kinase 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)
37% identity, 97% coverage: 1:380/393 of query aligns to 1:390/399 of 1tuuA
- active site: N7 (= N7), R91 (= R83), H180 (= H171), R241 (= R232), E384 (= E374)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G201), D283 (= D274), F284 (≠ V275), R285 (= R276), G331 (= G322), I332 (= I323), N335 (= N326)
- binding sulfate ion: R91 (= R83), H180 (= H171), G212 (= G203)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
37% identity, 97% coverage: 1:380/393 of query aligns to 1:390/408 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 (= R83) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V85) mutation to A: Decreases affinity for acetate.
- L122 (= L113) mutation to A: Decreases affinity for acetate.
- D148 (= D140) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F170) mutation to A: Decreases affinity for acetate.
- N211 (= N202) mutation to A: Slightly reduced enzyme activity.
- P232 (= P223) mutation to A: Decreases affinity for acetate.
- R241 (= R232) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E374) 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)
37% identity, 97% coverage: 1:380/393 of query aligns to 1:390/398 of 1tuuB
- active site: N7 (= N7), R91 (= R83), H180 (= H171), R241 (= R232), E384 (= E374)
- binding adenosine monophosphate: D283 (= D274), R285 (= R276), G331 (= G322), I332 (= I323), N335 (= N326), S336 (≠ Y327)
- binding trihydrogen thiodiphosphate: H180 (= H171), G212 (= G203), R241 (= R232)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwsA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding cytidine-5'-triphosphate: G202 (= G201), N203 (= N202), G204 (= G203), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
- binding 1,2-ethanediol: V21 (≠ I20), C24 (≠ A23), H115 (= H114), N203 (= N202), T232 (≠ S231), R233 (= R232), K262 (≠ Q261)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwrA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding cytidine-5'-monophosphate: G202 (= G201), N203 (= N202), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwqA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding guanosine-5'-triphosphate: H172 (= H171), N203 (= N202), G204 (= G203), D275 (= D274), L276 (≠ V275), R277 (= R276), E280 (≠ A279), G323 (= G322), I324 (= I323), N327 (= N326)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwpA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H114), K262 (≠ Q261)
- binding guanosine-5'-diphosphate: N203 (= N202), D275 (= D274), L276 (≠ V275), R277 (= R276), E280 (≠ A279), G323 (= G322), I324 (= I323), N327 (= N326), S328 (≠ Y327)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwoA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding guanosine-5'-monophosphate: G202 (= G201), N203 (= N202), D275 (= D274), L276 (≠ V275), R277 (= R276), E280 (≠ A279), G323 (= G322), I324 (= I323), N327 (= N326)
- binding 1,2-ethanediol: E100 (= E99), N104 (≠ T103)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwnA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding adenosine-5'-tetraphosphate: H172 (= H171), H200 (= H199), N203 (= N202), G204 (= G203), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwmA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding adenosine-5'-triphosphate: H172 (= H171), H200 (= H199), N203 (= N202), G204 (= G203), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
- binding 1,2-ethanediol: H172 (= H171), R233 (= R232)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 4fwkA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding adenosine monophosphate: G202 (= G201), N203 (= N202), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
- binding 1,2-ethanediol: D103 (≠ A102), N104 (≠ T103), R107 (≠ A106)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 2e1zA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N7), R83 (= R83), H115 (= H114), G202 (= G201), N203 (= N202), G204 (= G203), P224 (= P223), R233 (= R232), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 1x3nA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G201), N203 (= N202), G204 (= G203), D275 (= D274), L276 (≠ V275), R277 (= R276), G323 (= G322), I324 (= I323), N327 (= N326)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
40% identity, 96% coverage: 3:381/393 of query aligns to 4:384/394 of 1x3mA
- active site: N8 (= N7), R83 (= R83), H172 (= H171), R233 (= R232), E378 (= E374)
- binding adenosine-5'-diphosphate: G202 (= G201), N203 (= N202), D275 (= D274), L276 (≠ V275), R277 (= R276), G322 (= G321), G323 (= G322), I324 (= I323), N327 (= N326)
7fj9A Kpacka (pduw) with amppnp complex structure
38% identity, 97% coverage: 2:384/393 of query aligns to 3:394/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
38% identity, 97% coverage: 2:384/393 of query aligns to 3:394/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
37% identity, 97% coverage: 1:380/393 of query aligns to 2:371/376 of 4ijnA
- active site: N8 (= N7), R72 (= R83), H161 (= H171), R222 (= R232), E365 (= E374)
- binding adenosine monophosphate: G191 (= G201), N192 (= N202), D263 (= D274), F264 (≠ V275), R265 (= R276), G311 (= G322), V312 (≠ I323), N315 (= N326), V316 (≠ Y327)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
38% identity, 98% coverage: 2:386/393 of query aligns to 5:379/381 of 4iz9A
- active site: N10 (= N7), R74 (= R83), H163 (= H171), R224 (= R232), E367 (= E374)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K14), G193 (= G201), N194 (= N202), D265 (= D274), F266 (≠ V275), R267 (= R276), G313 (= G322), I314 (= I323), N317 (= N326), D318 (≠ Y327)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
24% identity, 51% coverage: 138:339/393 of query aligns to 126:321/375 of 1sazA
- active site: R214 (= R232)
- binding phosphomethylphosphonic acid adenylate ester: H154 (= H171), G184 (= G201), G185 (≠ N202), G186 (= G203), S254 (= S272), D255 (= D274), A256 (≠ V275), R257 (= R276), G304 (= G322), L305 (≠ I323), H307 (≠ E325)
Query Sequence
>Synpcc7942_2079 Synpcc7942_2079 acetate kinase
LQLLTFNAGSSSYKLSGFEITTAAEQTDPVWQVQIDWKTDRAATLTQPGQPVQMLDSSDR
RAWLEIALETLPDRSAIAAVVHRVVHGGQQQAPAVVTPELKATIAAAANLAPLHNPLNLA
GIEQMEQLFGLAMPQIAVFDTAFHQQMPVAAAIYGGPYHWWEQGYRRYGFHGISHQYLAE
RCAQLSDRSLSNLQLVTAHLGNGCSLAAIRNGHSVDTSMGFSPLEGLVMGSRSGTVDPGL
LLHLLQQPDCSPSQLSTVLNQQSGLLGLSGRSNDVRALAIAADAGDQRSQLALAAFTHSL
RRHLGAMLASLTRLDALVFAGGIGENYRSLWPAVCEHFAGMPIRLDPEAMAVAGDRRIST
PDSAITVWVIHSREDWQMVQLALPLLRSPQSFN
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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