SitesBLAST
Comparing WP_024889080.1 NCBI__GCF_000559025.1:WP_024889080.1 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)
7fj9A Kpacka (pduw) with amppnp complex structure
41% identity, 88% coverage: 46:426/433 of query aligns to 4:385/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
41% identity, 88% coverage: 46:426/433 of query aligns to 4:385/395 of 7fj8A
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
36% identity, 89% coverage: 46:430/433 of query aligns to 3:393/408 of P38502
- N7 (= N50) 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 (= S53) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S55) 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 (= K57) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R132) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V134) mutation to A: Decreases affinity for acetate.
- L122 (= L163) mutation to A: Decreases affinity for acetate.
- D148 (= D189) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F219) mutation to A: Decreases affinity for acetate.
- N211 (≠ S251) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A272) mutation to A: Decreases affinity for acetate.
- R241 (= R281) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E421) 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)
36% identity, 89% coverage: 46:430/433 of query aligns to 3:393/398 of 1tuuB
- active site: N7 (= N50), R91 (= R132), H180 (= H220), R241 (= R281), E384 (= E421)
- binding adenosine monophosphate: D283 (= D323), R285 (= R325), G331 (= G370), I332 (= I371), N335 (≠ H374), S336 (= S375)
- binding trihydrogen thiodiphosphate: H180 (= H220), G212 (= G252), R241 (= R281)
1tuuA Acetate kinase crystallized with atpgs (see paper)
36% identity, 89% coverage: 46:430/433 of query aligns to 3:393/399 of 1tuuA
- active site: N7 (= N50), R91 (= R132), H180 (= H220), R241 (= R281), E384 (= E421)
- binding adenosine-5'-diphosphate: K14 (= K57), G210 (= G250), D283 (= D323), F284 (≠ P324), R285 (= R325), G331 (= G370), I332 (= I371), N335 (≠ H374)
- binding sulfate ion: R91 (= R132), H180 (= H220), G212 (= G252)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwsA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding cytidine-5'-triphosphate: G202 (= G250), N203 (≠ S251), G204 (= G252), D275 (= D323), L276 (≠ P324), R277 (= R325), G323 (= G370), I324 (= I371), N327 (≠ H374)
- binding 1,2-ethanediol: V21 (≠ A63), C24 (≠ D66), H115 (= H164), N203 (≠ S251), T232 (= T280), R233 (= R281), K262 (≠ H310)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwrA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding cytidine-5'-monophosphate: G202 (= G250), N203 (≠ S251), D275 (= D323), L276 (≠ P324), R277 (= R325), G323 (= G370), I324 (= I371), N327 (≠ H374)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwqA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding guanosine-5'-triphosphate: H172 (= H220), N203 (≠ S251), G204 (= G252), D275 (= D323), L276 (≠ P324), R277 (= R325), E280 (vs. gap), G323 (= G370), I324 (= I371), N327 (≠ H374)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwpA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding 1,2-ethanediol: S11 (= S53), H115 (= H164), K262 (≠ H310)
- binding guanosine-5'-diphosphate: N203 (≠ S251), D275 (= D323), L276 (≠ P324), R277 (= R325), E280 (vs. gap), G323 (= G370), I324 (= I371), N327 (≠ H374), S328 (= S375)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwoA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding guanosine-5'-monophosphate: G202 (= G250), N203 (≠ S251), D275 (= D323), L276 (≠ P324), R277 (= R325), E280 (vs. gap), G323 (= G370), I324 (= I371), N327 (≠ H374)
- binding 1,2-ethanediol: E100 (≠ G149), N104 (≠ D153)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwnA
- active site: N8 (= N50), R83 (= R132), H172 (= H220), R233 (= R281), E378 (= E421)
- binding adenosine-5'-tetraphosphate: H172 (= H220), H200 (= H248), N203 (≠ S251), G204 (= G252), D275 (= D323), L276 (≠ P324), R277 (= R325), G323 (= G370), I324 (= I371), N327 (≠ H374)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
38% identity, 88% coverage: 45:426/433 of query aligns to 3:383/394 of 4fwmA