SitesBLAST
Comparing 208544 DVU3030 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)
1tuuB Acetate kinase crystallized with atpgs (see paper)
54% identity, 100% coverage: 1:401/402 of query aligns to 1:397/398 of 1tuuB
- active site: N7 (= N7), R91 (= R95), H180 (= H184), R241 (= R245), E384 (= E388)
- binding adenosine monophosphate: D283 (= D286), R285 (= R288), G331 (= G334), I332 (= I335), N335 (= N338), S336 (≠ D339)
- binding trihydrogen thiodiphosphate: H180 (= H184), G212 (= G216), R241 (= R245)
1tuuA Acetate kinase crystallized with atpgs (see paper)
54% identity, 100% coverage: 1:401/402 of query aligns to 1:397/399 of 1tuuA
- active site: N7 (= N7), R91 (= R95), H180 (= H184), R241 (= R245), E384 (= E388)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G214), D283 (= D286), F284 (≠ M287), R285 (= R288), G331 (= G334), I332 (= I335), N335 (= N338)
- binding sulfate ion: R91 (= R95), H180 (= H184), G212 (= G216)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
54% identity, 100% coverage: 1:401/402 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 (= R95) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (≠ L97) mutation to A: Decreases affinity for acetate.
- L122 (= L126) mutation to A: Decreases affinity for acetate.
- D148 (= D152) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F183) mutation to A: Decreases affinity for acetate.
- N211 (= N215) mutation to A: Slightly reduced enzyme activity.
- P232 (= P236) mutation to A: Decreases affinity for acetate.
- R241 (= R245) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E388) 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
45% identity, 99% coverage: 3:401/402 of query aligns to 4:390/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
45% identity, 99% coverage: 3:401/402 of query aligns to 4:390/395 of 7fj8A
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
45% identity, 100% coverage: 3:402/402 of query aligns to 6:381/381 of 4iz9A
- active site: N10 (= N7), R74 (= R95), H163 (= H184), R224 (= R245), E367 (= E388)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K14), G193 (= G214), N194 (= N215), D265 (= D286), F266 (≠ M287), R267 (= R288), G313 (= G334), I314 (= I335), N317 (= N338), D318 (= D339)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
44% identity, 99% coverage: 1:399/402 of query aligns to 2:376/376 of 4ijnA
- active site: N8 (= N7), R72 (= R95), H161 (= H184), R222 (= R245), E365 (= E388)
- binding adenosine monophosphate: G191 (= G214), N192 (= N215), D263 (= D286), F264 (≠ M287), R265 (= R288), G311 (= G334), V312 (≠ I335), N315 (= N338), V316 (≠ D339)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding cytidine-5'-triphosphate: G202 (= G214), N203 (= N215), G204 (= G216), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
- binding 1,2-ethanediol: V21 (= V24), C24 (= C27), H115 (= H127), N203 (= N215), T232 (= T244), R233 (= R245), K262 (= K274)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding cytidine-5'-monophosphate: G202 (= G214), N203 (= N215), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding guanosine-5'-triphosphate: H172 (= H184), N203 (= N215), G204 (= G216), D275 (= D286), L276 (≠ M287), R277 (= R288), E280 (≠ H291), G323 (= G334), I324 (= I335), N327 (= N338)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H127), K262 (= K274)
- binding guanosine-5'-diphosphate: N203 (= N215), D275 (= D286), L276 (≠ M287), R277 (= R288), E280 (≠ H291), G323 (= G334), I324 (= I335), N327 (= N338), S328 (≠ D339)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwoA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding guanosine-5'-monophosphate: G202 (= G214), N203 (= N215), D275 (= D286), L276 (≠ M287), R277 (= R288), E280 (≠ H291), G323 (= G334), I324 (= I335), N327 (= N338)
- binding 1,2-ethanediol: E100 (≠ W112), N104 (≠ V116)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwnA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding adenosine-5'-tetraphosphate: H172 (= H184), H200 (= H212), N203 (= N215), G204 (= G216), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwmA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding adenosine-5'-triphosphate: H172 (= H184), H200 (= H212), N203 (= N215), G204 (= G216), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
- binding 1,2-ethanediol: H172 (= H184), R233 (= R245)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 4fwkA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding adenosine monophosphate: G202 (= G214), N203 (= N215), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
- binding 1,2-ethanediol: D103 (≠ G115), N104 (≠ V116), R107 (≠ D119)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 2e1zA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N7), R83 (= R95), H115 (= H127), G202 (= G214), N203 (= N215), G204 (= G216), P224 (= P236), R233 (= R245), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 1x3nA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G214), N203 (= N215), G204 (= G216), D275 (= D286), L276 (≠ M287), R277 (= R288), G323 (= G334), I324 (= I335), N327 (= N338)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
42% identity, 97% coverage: 3:393/402 of query aligns to 4:383/394 of 1x3mA
- active site: N8 (= N7), R83 (= R95), H172 (= H184), R233 (= R245), E378 (= E388)
- binding adenosine-5'-diphosphate: G202 (= G214), N203 (= N215), D275 (= D286), L276 (≠ M287), R277 (= R288), G322 (≠ A333), G323 (= G334), I324 (= I335), N327 (= N338)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
26% identity, 56% coverage: 179:402/402 of query aligns to 149:348/375 of 1sazA
- active site: R214 (= R245)
- binding phosphomethylphosphonic acid adenylate ester: H154 (= H184), G184 (= G214), G185 (≠ N215), G186 (= G216), S254 (≠ N285), D255 (= D286), A256 (≠ M287), R257 (= R288), G304 (= G334), L305 (≠ I335), H307 (≠ E337)
Query Sequence
>208544 DVU3030 acetate kinase
MNVLVINSGSSSIKYQLIDMEREVPLCSGLVERIGEPMGKLTHKIRPDAEGEEKLTFEQP
FTNHVEGMKRVVELITDADKGVIKDKSEIGAIGHRVLLGGEEIKQSVRIDDWAKGVIRDY
IPLGPLHNPANLAGIEVAEELFPGLPNVGVFDTEFHQSMPAKAYLYPLPIELYEELKIRR
YGFHGTSHRYITKRTAQYLGKPLDELNIITCHLGNGCSMAAVKNGKCVDTTMGITPLEGL
MMGTRCGDIDPAIVPFLMEKKNLSPAEADTLMNKQSGLKGMCGMNDMRDLHAARENGNER
AQLAFEMFTYRIKKYIGAYYAVLGRVDAVVFTAGIGENDDFVRAEVCAGLDSLGIAVDPA
RNAVRNGQPRHISPDGSRVAVLVVPTNEELEIAQATLDVLKG
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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