SitesBLAST
Comparing WP_090447849.1 NCBI__GCF_900100495.1:WP_090447849.1 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)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwsA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding cytidine-5'-triphosphate: G202 (= G206), N203 (= N207), G204 (= G208), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
- binding 1,2-ethanediol: V21 (≠ E23), C24 (≠ S26), H115 (= H119), N203 (= N207), T232 (= T236), R233 (= R237), K262 (≠ Q266)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwrA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding cytidine-5'-monophosphate: G202 (= G206), N203 (= N207), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwqA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding guanosine-5'-triphosphate: H172 (= H176), N203 (= N207), G204 (= G208), D275 (= D279), L276 (≠ M280), R277 (= R281), E280 (= E284), G323 (= G327), I324 (= I328), N327 (= N331)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwpA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding 1,2-ethanediol: S11 (= S13), H115 (= H119), K262 (≠ Q266)
- binding guanosine-5'-diphosphate: N203 (= N207), D275 (= D279), L276 (≠ M280), R277 (= R281), E280 (= E284), G323 (= G327), I324 (= I328), N327 (= N331), S328 (= S332)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwoA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding guanosine-5'-monophosphate: G202 (= G206), N203 (= N207), D275 (= D279), L276 (≠ M280), R277 (= R281), E280 (= E284), G323 (= G327), I324 (= I328), N327 (= N331)
- binding 1,2-ethanediol: E100 (≠ A104), N104 (≠ A108)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwnA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding adenosine-5'-tetraphosphate: H172 (= H176), H200 (= H204), N203 (= N207), G204 (= G208), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwmA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding adenosine-5'-triphosphate: H172 (= H176), H200 (= H204), N203 (= N207), G204 (= G208), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
- binding 1,2-ethanediol: H172 (= H176), R233 (= R237)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 4fwkA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding adenosine monophosphate: G202 (= G206), N203 (= N207), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
- binding 1,2-ethanediol: D103 (≠ Q107), N104 (≠ A108), R107 (≠ A111)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 2e1zA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N10), R83 (= R87), H115 (= H119), G202 (= G206), N203 (= N207), G204 (= G208), P224 (= P228), R233 (= R237), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 1x3nA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G206), N203 (= N207), G204 (= G208), D275 (= D279), L276 (≠ M280), R277 (= R281), G323 (= G327), I324 (= I328), N327 (= N331)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
49% identity, 98% coverage: 6:392/394 of query aligns to 4:389/394 of 1x3mA
- active site: N8 (= N10), R83 (= R87), H172 (= H176), R233 (= R237), E378 (= E381)
- binding adenosine-5'-diphosphate: G202 (= G206), N203 (= N207), D275 (= D279), L276 (≠ M280), R277 (= R281), G322 (= G326), G323 (= G327), I324 (= I328), N327 (= N331)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
43% identity, 99% coverage: 5:393/394 of query aligns to 2:396/408 of P38502
- N7 (= N10) 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 (= S13) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S15) 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 (= K17) mutation to A: Strongly decreases enzyme activity.; mutation to R: Reduces enzyme activity.
- R91 (= R87) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V89) mutation to A: Decreases affinity for acetate.
- L122 (= L118) mutation to A: Decreases affinity for acetate.
- D148 (= D144) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F175) mutation to A: Decreases affinity for acetate.
- N211 (= N207) mutation to A: Slightly reduced enzyme activity.
- P232 (= P228) mutation to A: Decreases affinity for acetate.
- R241 (= R237) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E381) 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)
43% identity, 99% coverage: 5:393/394 of query aligns to 2:396/399 of 1tuuA
- active site: N7 (= N10), R91 (= R87), H180 (= H176), R241 (= R237), E384 (= E381)
- binding adenosine-5'-diphosphate: K14 (= K17), G210 (= G206), D283 (= D279), F284 (≠ M280), R285 (= R281), G331 (= G327), I332 (= I328), N335 (= N331)
- binding sulfate ion: R91 (= R87), H180 (= H176), G212 (= G208)
1tuuB Acetate kinase crystallized with atpgs (see paper)
43% identity, 99% coverage: 5:393/394 of query aligns to 2:396/398 of 1tuuB
- active site: N7 (= N10), R91 (= R87), H180 (= H176), R241 (= R237), E384 (= E381)
- binding adenosine monophosphate: D283 (= D279), R285 (= R281), G331 (= G327), I332 (= I328), N335 (= N331), S336 (= S332)
- binding trihydrogen thiodiphosphate: H180 (= H176), G212 (= G208), R241 (= R237)
7fj9A Kpacka (pduw) with amppnp complex structure
44% identity, 98% coverage: 5:392/394 of query aligns to 3:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
44% identity, 98% coverage: 5:392/394 of query aligns to 3:391/395 of 7fj8A
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
44% identity, 99% coverage: 3:393/394 of query aligns to 3:379/381 of 4iz9A
- active site: N10 (= N10), R74 (= R87), H163 (= H176), R224 (= R237), E367 (= E381)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K17), G193 (= G206), N194 (= N207), D265 (= D279), F266 (≠ M280), R267 (= R281), G313 (= G327), I314 (= I328), N317 (= N331), D318 (≠ S332)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
43% identity, 97% coverage: 5:386/394 of query aligns to 3:370/376 of 4ijnA
- active site: N8 (= N10), R72 (= R87), H161 (= H176), R222 (= R237), E365 (= E381)
- binding adenosine monophosphate: G191 (= G206), N192 (= N207), D263 (= D279), F264 (≠ M280), R265 (= R281), G311 (= G327), V312 (≠ I328), N315 (= N331), V316 (≠ S332)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
25% identity, 40% coverage: 171:328/394 of query aligns to 149:305/375 of 1sazA
Sites not aligning to the query:
Query Sequence
>WP_090447849.1 NCBI__GCF_900100495.1:WP_090447849.1
MPARNILVINCGSSSIKFALVNEAHSQFTLSGLAERLGSHDAVLHWQRGGERDSLMIANA
DHRAALAQLLPLVQAAAGGQLHGIGHRVVHGGEHFTAASRLDEAALQAIRATAPLAPLHN
PANLLGIEAAIKLFPKLPQVAVFDTAFHQTLPEHAFRYALPDSLYREHGVRRYGFHGTSH
RFVSHRAAELAGLAVGDSSWLVAHLGNGCSTCAIEGGQSRDTSMGLTPLEGLVMGTRSGD
VDPNLHSHLARTLGWNLERIERLLNQESGLLGLSGLSNDMRSLEQAREQGHAGATLAIEV
FCYRLAKSLAAMSCALSQLDGLVFTGGIGENSPLIRSKTVAHLKLLNLALDKQANARTIR
GVGGAIHAHGHPRVLVVPTNEERQIALDTLALLA
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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