SitesBLAST
Comparing WP_050461168.1 NCBI__GCF_001189915.1:WP_050461168.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
1tuuA Acetate kinase crystallized with atpgs (see paper)
37% identity, 98% coverage: 5:396/399 of query aligns to 3:399/399 of 1tuuA
- active site: N7 (= N9), R91 (= R93), H180 (= H181), R241 (= R241), E384 (= E381)
- binding adenosine-5'-diphosphate: K14 (= K16), G210 (= G210), D283 (= D283), F284 (≠ P284), R285 (= R285), G331 (= G330), I332 (= I331), N335 (= N334)
- binding sulfate ion: R91 (= R93), H180 (= H181), G212 (= G212)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
37% identity, 98% coverage: 5:396/399 of query aligns to 3:399/408 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 (= R93) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V95) mutation to A: Decreases affinity for acetate.
- L122 (= L124) mutation to A: Decreases affinity for acetate.
- D148 (= D150) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F180) mutation to A: Decreases affinity for acetate.
- N211 (≠ S211) mutation to A: Slightly reduced enzyme activity.
- P232 (≠ A232) mutation to A: Decreases affinity for acetate.
- R241 (= R241) 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.
1tuuB Acetate kinase crystallized with atpgs (see paper)
37% identity, 97% coverage: 5:393/399 of query aligns to 3:396/398 of 1tuuB
- active site: N7 (= N9), R91 (= R93), H180 (= H181), R241 (= R241), E384 (= E381)
- binding adenosine monophosphate: D283 (= D283), R285 (= R285), G331 (= G330), I332 (= I331), N335 (= N334), S336 (≠ N335)
- binding trihydrogen thiodiphosphate: H180 (= H181), G212 (= G212), R241 (= R241)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwsA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding cytidine-5'-triphosphate: G202 (= G210), N203 (≠ S211), G204 (= G212), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: V21 (≠ A22), C24 (≠ E25), H115 (= H125), N203 (≠ S211), T232 (= T240), R233 (= R241), K262 (≠ R270)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwrA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding cytidine-5'-monophosphate: G202 (= G210), N203 (≠ S211), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwqA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding guanosine-5'-triphosphate: H172 (= H181), N203 (≠ S211), G204 (= G212), D275 (= D283), L276 (≠ P284), R277 (= R285), E280 (≠ L288), G323 (= G330), I324 (= I331), N327 (= N334)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwpA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding 1,2-ethanediol: S11 (= S12), H115 (= H125), K262 (≠ R270)
- binding guanosine-5'-diphosphate: N203 (≠ S211), D275 (= D283), L276 (≠ P284), R277 (= R285), E280 (≠ L288), G323 (= G330), I324 (= I331), N327 (= N334), S328 (≠ N335)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwoA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding guanosine-5'-monophosphate: G202 (= G210), N203 (≠ S211), D275 (= D283), L276 (≠ P284), R277 (= R285), E280 (≠ L288), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: E100 (≠ A110), N104 (≠ D114)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwnA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding adenosine-5'-tetraphosphate: H172 (= H181), H200 (= H208), N203 (≠ S211), G204 (= G212), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwmA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding adenosine-5'-triphosphate: H172 (= H181), H200 (= H208), N203 (≠ S211), G204 (= G212), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: H172 (= H181), R233 (= R241)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 4fwkA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding adenosine monophosphate: G202 (= G210), N203 (≠ S211), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: D103 (≠ E113), N104 (≠ D114), R107 (≠ S117)
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, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 2e1zA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N9), R83 (= R93), H115 (= H125), G202 (= G210), N203 (≠ S211), G204 (= G212), P224 (≠ A232), R233 (= R241), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 1x3nA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G210), N203 (≠ S211), G204 (= G212), D275 (= D283), L276 (≠ P284), R277 (= R285), G323 (= G330), I324 (= I331), N327 (= N334)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 98% coverage: 4:396/399 of query aligns to 3:393/394 of 1x3mA
- active site: N8 (= N9), R83 (= R93), H172 (= H181), R233 (= R241), E378 (= E381)
- binding adenosine-5'-diphosphate: G202 (= G210), N203 (≠ S211), D275 (= D283), L276 (≠ P284), R277 (= R285), G322 (≠ A329), G323 (= G330), I324 (= I331), N327 (= N334)
7fj9A Kpacka (pduw) with amppnp complex structure
39% identity, 97% coverage: 5:392/399 of query aligns to 4:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
39% identity, 97% coverage: 5:392/399 of query aligns to 4:391/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
36% identity, 95% coverage: 5:382/399 of query aligns to 4:366/376 of 4ijnA
- active site: N8 (= N9), R72 (= R93), H161 (= H181), R222 (= R241), E365 (= E381)
- binding adenosine monophosphate: G191 (= G210), N192 (≠ S211), D263 (≠ S282), F264 (≠ D283), R265 (≠ P284), G311 (= G330), V312 (≠ I331), N315 (= N334), V316 (≠ N335)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
36% identity, 97% coverage: 5:393/399 of query aligns to 6:379/381 of 4iz9A
- active site: N10 (= N9), R74 (= R93), H163 (= H181), R224 (= R241), E367 (= E381)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K16), G193 (= G210), N194 (≠ S211), D265 (≠ S282), F266 (≠ D283), R267 (≠ P284), G313 (= G330), I314 (= I331), N317 (= N334), D318 (≠ N335)
Query Sequence
>WP_050461168.1 NCBI__GCF_001189915.1:WP_050461168.1
MNELILVLNCGSSSIKFGLFEAGPEQLARQAIWRGKADGIGSHNAVLEIHGSATSALTLS
AENPYHDALGAIRTEVLAYLTHTGSRLLSIAHRVVHGGAKYFAPVRVDHAVLEDLRSYIP
LAPLHQPFALEAIEALLNSHPELPQVACFDTAFHHTVPRVEQMLPLPQAAWDRGLRRYGF
HGLSYEYQSLVLAERYGDAARGKTIVAHLGSGASLCAMQDLRSVATTMGFSALDGLMMGT
RCGTLDPGAVLYLLEIEKQTPQQIGQLLYRESGLLGVSGVSSDPRILLQQEQDNPAVRDA
LDLYVRRIVREIGALTAVLGGLDLLVFTAGIGENNAEIRSRICHALCFLGIGLDNVANAG
NAAVISRSGRQPLVAVEATNEEWIAASHARQLLTVQQHH
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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