SitesBLAST
Comparing 3607216 Dshi_0632 acetate kinase (RefSeq) 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)
7fj9A Kpacka (pduw) with amppnp complex structure
42% identity, 98% coverage: 4:376/382 of query aligns to 4:388/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
42% identity, 98% coverage: 4:376/382 of query aligns to 4:388/395 of 7fj8A
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
38% identity, 97% coverage: 4:374/382 of query aligns to 3:390/408 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 (= R85) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V87) mutation to A: Decreases affinity for acetate.
- L122 (= L116) mutation to A: Decreases affinity for acetate.
- D148 (= D142) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F172) mutation to A: Decreases affinity for acetate.
- N211 (= N203) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A224) mutation to A: Decreases affinity for acetate.
- R241 (= R233) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E368) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
1tuuA Acetate kinase crystallized with atpgs (see paper)
38% identity, 97% coverage: 4:374/382 of query aligns to 3:390/399 of 1tuuA
- active site: N7 (= N8), R91 (= R85), H180 (= H173), R241 (= R233), E384 (= E368)
- binding adenosine-5'-diphosphate: K14 (= K15), G210 (= G202), D283 (= D274), F284 (≠ M275), R285 (= R276), G331 (= G319), I332 (= I320), N335 (= N323)
- binding sulfate ion: R91 (= R85), H180 (= H173), G212 (= G204)
1tuuB Acetate kinase crystallized with atpgs (see paper)
38% identity, 97% coverage: 4:374/382 of query aligns to 3:390/398 of 1tuuB
- active site: N7 (= N8), R91 (= R85), H180 (= H173), R241 (= R233), E384 (= E368)
- binding adenosine monophosphate: D283 (= D274), R285 (= R276), G331 (= G319), I332 (= I320), N335 (= N323), S336 (≠ A324)
- binding trihydrogen thiodiphosphate: H180 (= H173), G212 (= G204), R241 (= R233)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwsA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding cytidine-5'-triphosphate: G202 (= G202), N203 (= N203), G204 (= G204), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
- binding 1,2-ethanediol: V21 (≠ A21), C24 (≠ A24), H115 (= H117), N203 (= N203), T232 (= T232), R233 (= R233), K262 (≠ E261)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwrA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding cytidine-5'-monophosphate: G202 (= G202), N203 (= N203), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwqA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding guanosine-5'-triphosphate: H172 (= H173), N203 (= N203), G204 (= G204), D275 (= D274), L276 (≠ M275), R277 (= R276), E280 (≠ Q279), G323 (= G319), I324 (= I320), N327 (= N323)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwpA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding 1,2-ethanediol: S11 (= S11), H115 (= H117), K262 (≠ E261)
- binding guanosine-5'-diphosphate: N203 (= N203), D275 (= D274), L276 (≠ M275), R277 (= R276), E280 (≠ Q279), G323 (= G319), I324 (= I320), N327 (= N323), S328 (≠ A324)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwoA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding guanosine-5'-monophosphate: G202 (= G202), N203 (= N203), D275 (= D274), L276 (≠ M275), R277 (= R276), E280 (≠ Q279), G323 (= G319), I324 (= I320), N327 (= N323)
- binding 1,2-ethanediol: E100 (≠ D102), N104 (≠ A106)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwnA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding adenosine-5'-tetraphosphate: H172 (= H173), H200 (= H200), N203 (= N203), G204 (= G204), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwmA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding adenosine-5'-triphosphate: H172 (= H173), H200 (= H200), N203 (= N203), G204 (= G204), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
- binding 1,2-ethanediol: H172 (= H173), R233 (= R233)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 4fwkA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding adenosine monophosphate: G202 (= G202), N203 (= N203), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
- binding 1,2-ethanediol: D103 (≠ E105), N104 (≠ A106), R107 (≠ A109)
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: 3:373/382 of query aligns to 3:383/394 of 2e1zA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N8), R83 (= R85), H115 (= H117), G202 (= G202), N203 (= N203), G204 (= G204), P224 (≠ A224), R233 (= R233), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 1x3nA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G202), N203 (= N203), G204 (= G204), D275 (= D274), L276 (≠ M275), R277 (= R276), G323 (= G319), I324 (= I320), N327 (= N323)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 97% coverage: 3:373/382 of query aligns to 3:383/394 of 1x3mA
- active site: N8 (= N8), R83 (= R85), H172 (= H173), R233 (= R233), E378 (= E368)
- binding adenosine-5'-diphosphate: G202 (= G202), N203 (= N203), D275 (= D274), L276 (≠ M275), R277 (= R276), G322 (= G318), G323 (= G319), I324 (= I320), N327 (= N323)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
38% identity, 98% coverage: 1:375/382 of query aligns to 1:372/376 of 4ijnA
- active site: N8 (= N8), R72 (= R85), H161 (= H173), R222 (= R233), E365 (= E368)
- binding adenosine monophosphate: G191 (= G202), N192 (= N203), D263 (vs. gap), F264 (vs. gap), R265 (≠ H273), G311 (= G319), V312 (≠ I320), N315 (= N323), V316 (≠ A324)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
37% identity, 97% coverage: 4:374/382 of query aligns to 6:373/381 of 4iz9A
- active site: N10 (= N8), R74 (= R85), H163 (= H173), R224 (= R233), E367 (= E368)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K15), G193 (= G202), N194 (= N203), D265 (vs. gap), F266 (vs. gap), R267 (≠ H273), G313 (= G319), I314 (= I320), N317 (= N323), D318 (≠ A324)
Query Sequence
>3607216 Dshi_0632 acetate kinase (RefSeq)
MSVLLTLNAGSSSVKFAVYEAANAPLLIVAGEVDGLGPAARLIVNTNPATKRDLGPTDHA
AALHAILAALRPILSGRQVVGVGHRIVHGGGAFTAPVELTPDVIEALEAFVPLAPLHQPH
NLAMVAAARQAFPDAVQIGCFDTAFHAGHPWVNDTFALPRRFYEAGVRRYGFHGLSYDYI
TDKLRADCPELAAGRVVIAHLGNGASMCAVRDGRSVGSTMGFSALDGLPMGTRCGQLDPG
VLLYMMEQGMSREEITSILYEESGLQGLSGFSHDMRTLQASDDPRAAEAIDYYVFRIRRE
LGAMTAVLGGIDALVFCGGIGENAAVIRARVIEGMDYLGLSLDAEANARNATRVATGPVP
ILVIPTNEELVIARAVSAALHP
Or try a new SitesBLAST search
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