SitesBLAST
Comparing WP_011384935.1 AMB_RS12860 acetate/propionate family kinase 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 19 hits to proteins with known functional sites (download)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
39% identity, 98% coverage: 5:394/397 of query aligns to 3:398/408 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 (= R94) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V96) mutation to A: Decreases affinity for acetate.
- L122 (= L125) mutation to A: Decreases affinity for acetate.
- D148 (= D151) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F181) mutation to A: Decreases affinity for acetate.
- N211 (≠ S212) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A233) mutation to A: Decreases affinity for acetate.
- R241 (= R242) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E380) 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)
39% identity, 98% coverage: 5:394/397 of query aligns to 3:398/398 of 1tuuB
- active site: N7 (= N9), R91 (= R94), H180 (= H182), R241 (= R242), E384 (= E380)
- binding adenosine monophosphate: D283 (= D284), R285 (= R286), G331 (= G329), I332 (= I330), N335 (≠ R333), S336 (= S334)
- binding trihydrogen thiodiphosphate: H180 (= H182), G212 (= G213), R241 (= R242)
1tuuA Acetate kinase crystallized with atpgs (see paper)
39% identity, 98% coverage: 5:394/397 of query aligns to 3:398/399 of 1tuuA
- active site: N7 (= N9), R91 (= R94), H180 (= H182), R241 (= R242), E384 (= E380)
- binding adenosine-5'-diphosphate: K14 (= K16), G210 (= G211), D283 (= D284), F284 (≠ M285), R285 (= R286), G331 (= G329), I332 (= I330), N335 (≠ R333)
- binding sulfate ion: R91 (= R94), H180 (= H182), G212 (= G213)
7fj9A Kpacka (pduw) with amppnp complex structure
40% identity, 97% coverage: 5:391/397 of query aligns to 4:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
40% identity, 97% coverage: 5:391/397 of query aligns to 4:391/395 of 7fj8A
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwsA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding cytidine-5'-triphosphate: G202 (= G211), N203 (≠ S212), G204 (= G213), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
- binding 1,2-ethanediol: V21 (≠ I21), C24 (≠ G24), H115 (= H126), N203 (≠ S212), T232 (= T241), R233 (= R242), K262 (= K271)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwrA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding cytidine-5'-monophosphate: G202 (= G211), N203 (≠ S212), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwqA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding guanosine-5'-triphosphate: H172 (= H182), N203 (≠ S212), G204 (= G213), D275 (= D284), L276 (≠ M285), R277 (= R286), E280 (≠ L289), G323 (= G329), I324 (= I330), N327 (≠ R333)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwpA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding 1,2-ethanediol: S11 (= S12), H115 (= H126), K262 (= K271)
- binding guanosine-5'-diphosphate: N203 (≠ S212), D275 (= D284), L276 (≠ M285), R277 (= R286), E280 (≠ L289), G323 (= G329), I324 (= I330), N327 (≠ R333), S328 (= S334)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwoA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding guanosine-5'-monophosphate: G202 (= G211), N203 (≠ S212), D275 (= D284), L276 (≠ M285), R277 (= R286), E280 (≠ L289), G323 (= G329), I324 (= I330), N327 (≠ R333)
- binding 1,2-ethanediol: E100 (= E111), N104 (≠ E115)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwnA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding adenosine-5'-tetraphosphate: H172 (= H182), H200 (= H209), N203 (≠ S212), G204 (= G213), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwmA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding adenosine-5'-triphosphate: H172 (= H182), H200 (= H209), N203 (≠ S212), G204 (= G213), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
- binding 1,2-ethanediol: H172 (= H182), R233 (= R242)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 4fwkA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding adenosine monophosphate: G202 (= G211), N203 (≠ S212), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
- binding 1,2-ethanediol: D103 (≠ E114), N104 (≠ E115), R107 (≠ K118)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 2e1zA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N9), R83 (= R94), H115 (= H126), G202 (= G211), N203 (≠ S212), G204 (= G213), P224 (≠ A233), R233 (= R242), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 1x3nA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G211), N203 (≠ S212), G204 (= G213), D275 (= D284), L276 (≠ M285), R277 (= R286), G323 (= G329), I324 (= I330), N327 (≠ R333)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 4:383/394 of 1x3mA
- active site: N8 (= N9), R83 (= R94), H172 (= H182), R233 (= R242), E378 (= E380)
- binding adenosine-5'-diphosphate: G202 (= G211), N203 (≠ S212), D275 (= D284), L276 (≠ M285), R277 (= R286), G322 (≠ A328), G323 (= G329), I324 (= I330), N327 (≠ R333)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
38% identity, 96% coverage: 5:386/397 of query aligns to 4:371/376 of 4ijnA
- active site: N8 (= N9), R72 (= R94), H161 (= H182), R222 (= R242), E365 (= E380)
- binding adenosine monophosphate: G191 (= G211), N192 (≠ S212), D263 (≠ N283), F264 (vs. gap), R265 (vs. gap), G311 (= G329), V312 (≠ I330), N315 (≠ R333), V316 (≠ S334)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
35% identity, 98% coverage: 5:392/397 of query aligns to 6:379/381 of 4iz9A
- active site: N10 (= N9), R74 (= R94), H163 (= H182), R224 (= R242), E367 (= E380)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K16), G193 (= G211), N194 (≠ S212), D265 (≠ N283), F266 (≠ D284), R267 (≠ M285), G313 (= G329), I314 (= I330), N317 (≠ R333), D318 (≠ S334)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
24% identity, 41% coverage: 181:342/397 of query aligns to 153:321/375 of 1sazA
- active site: R214 (= R242)
- binding phosphomethylphosphonic acid adenylate ester: H154 (= H182), G184 (= G211), G185 (≠ S212), G186 (= G213), S254 (= S282), D255 (≠ N283), A256 (≠ D284), R257 (≠ M285), G304 (= G329), L305 (≠ I330), H307 (≠ E332)
Query Sequence
>WP_011384935.1 AMB_RS12860 acetate/propionate family kinase
MREGILVINAGSSSIKFSLYISNGDEKPLLSCKGQVEGINVAPHFIAKSPHGGVLNEQRW
PDQPNMSHEALFKYMIEWIEAQLGDAELKAAGHRVVHGGSQYSQPLLVNDELMEELEKLI
PLAPLHQPHNLAPIRALTKVHPGLTQVACFDTAFHRSNPWTAQSFALPRKITGEGVKRYG
FHGLSYEFIARQMRQLSPAAARGKVVVCHLGSGASMCAIDGGKSVASTMGFTAVDGLPMG
TRTGTMDAGVILYLLQQKGMTPKEIEDLLYKQSGLLGVSGVSNDMRILLESSEPHAAEAV
ELFVYRISRELGSLAAAMGGLDALVFTAGIGERSPQIRERVCAHAEWLGVEMDQEANQRD
SLLISAADSPVSVWVIPTDEEMMIAKHTRELLRSLRD
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