SitesBLAST
Comparing SM_b21184 SM_b21184 acetate kinase 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)
1tuuA Acetate kinase crystallized with atpgs (see paper)
39% identity, 99% coverage: 4:392/392 of query aligns to 3:399/399 of 1tuuA
- active site: N7 (= N8), R91 (= R91), H180 (= H179), R241 (= R239), E384 (= E377)
- binding adenosine-5'-diphosphate: K14 (= K15), G210 (= G208), D283 (= D281), F284 (≠ M282), R285 (= R283), G331 (= G326), I332 (= I327), N335 (= N330)
- binding sulfate ion: R91 (= R91), H180 (= H179), G212 (= G210)
1tuuB Acetate kinase crystallized with atpgs (see paper)
39% identity, 99% coverage: 4:390/392 of query aligns to 3:397/398 of 1tuuB
- active site: N7 (= N8), R91 (= R91), H180 (= H179), R241 (= R239), E384 (= E377)
- binding adenosine monophosphate: D283 (= D281), R285 (= R283), G331 (= G326), I332 (= I327), N335 (= N330), S336 (= S331)
- binding trihydrogen thiodiphosphate: H180 (= H179), G212 (= G210), R241 (= R239)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
39% identity, 99% coverage: 4:392/392 of query aligns to 3:399/408 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 (= S13) 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 (= 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 (= F178) mutation to A: Decreases affinity for acetate.
- N211 (≠ S209) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A230) mutation to A: Decreases affinity for acetate.
- R241 (= R239) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E377) 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
41% identity, 98% coverage: 4:386/392 of query aligns to 4:389/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
41% identity, 98% coverage: 4:386/392 of query aligns to 4:389/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
38% identity, 99% coverage: 1:388/392 of query aligns to 1:376/376 of 4ijnA
- active site: N8 (= N8), R72 (= R91), H161 (= H179), R222 (= R239), E365 (= E377)
- binding adenosine monophosphate: G191 (= G208), N192 (≠ S209), D263 (≠ N280), F264 (vs. gap), R265 (vs. gap), G311 (= G326), V312 (≠ I327), N315 (= N330), V316 (≠ S331)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding cytidine-5'-triphosphate: G202 (= G208), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: V21 (≠ I21), C24 (≠ A24), H115 (= H123), N203 (≠ S209), T232 (= T238), R233 (= R239), K262 (≠ H268)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding cytidine-5'-monophosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding guanosine-5'-triphosphate: H172 (= H179), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), E280 (vs. gap), G323 (= G326), I324 (= I327), N327 (= N330)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding 1,2-ethanediol: S11 (= S11), H115 (= H123), K262 (≠ H268)
- binding guanosine-5'-diphosphate: N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), E280 (vs. gap), G323 (= G326), I324 (= I327), N327 (= N330), S328 (= S331)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwoA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding guanosine-5'-monophosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), E280 (vs. gap), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: E100 (≠ T108), N104 (≠ R112)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwnA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding adenosine-5'-tetraphosphate: H172 (= H179), H200 (= H206), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwmA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding adenosine-5'-triphosphate: H172 (= H179), H200 (= H206), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: H172 (= H179), R233 (= R239)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 4fwkA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding adenosine monophosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
- binding 1,2-ethanediol: D103 (= D111), N104 (≠ R112), R107 (≠ S115)
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: 4:382/392 of query aligns to 4:383/394 of 2e1zA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N8), R83 (= R91), H115 (= H123), G202 (= G208), N203 (≠ S209), G204 (= G210), P224 (≠ A230), R233 (= R239), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 1x3nA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G208), N203 (≠ S209), G204 (= G210), D275 (= D281), L276 (≠ M282), R277 (= R283), G323 (= G326), I324 (= I327), N327 (= N330)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 4:382/392 of query aligns to 4:383/394 of 1x3mA
- active site: N8 (= N8), R83 (= R91), H172 (= H179), R233 (= R239), E378 (= E377)
- binding adenosine-5'-diphosphate: G202 (= G208), N203 (≠ S209), D275 (= D281), L276 (≠ M282), R277 (= R283), G322 (≠ A325), G323 (= G326), I324 (= I327), N327 (= N330)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
39% identity, 98% coverage: 4:389/392 of query aligns to 6:379/381 of 4iz9A
- active site: N10 (= N8), R74 (= R91), H163 (= H179), R224 (= R239), E367 (= E377)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K15), G193 (= G208), N194 (≠ S209), D265 (≠ N280), F266 (vs. gap), R267 (vs. gap), G313 (= G326), I314 (= I327), N317 (= N330), D318 (≠ S331)
Query Sequence
>SM_b21184 SM_b21184 acetate kinase
MEALLVINAGSSSLKFQIFGIATAGLERQVRAKLDGIATQPRLKATAADGTELINRRLDA
TAVPDLPEALSVARDWLATLRGFDLRAIGHRVVHGGPDYVRPVLIETTVLDRLASYQDLA
PLHQPNNLAPIRLAMDIKPDVPQVACFDTAFHRGRTEHTDCYALPRTFYEQGVRRYGFHG
ISYEYIAGRLREVAPEVARGRVIVAHLGSGASMCALKDGRSVETTMGFTALDGLPMGTRP
GQLDPGVVLHLLTDQGMSAQAVSDLLYHRSGLKGLSGISNDMRELLGSDDPRASFAIDHF
VHRCALDAGMLAAALGGLDAFVFTAGIGENSAPIRARVSEGLAWLGAELDPAANDAGASV
ISKAGSRVALHVMPTDEELMIARHTLAIIRAR
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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