SitesBLAST
Comparing BWI76_RS23200 FitnessBrowser__Koxy:BWI76_RS23200 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7fj9A Kpacka (pduw) with amppnp complex structure
83% identity, 98% coverage: 2:395/404 of query aligns to 1:394/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
83% identity, 98% coverage: 2:395/404 of query aligns to 1:394/395 of 7fj8A
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
47% identity, 96% coverage: 4:392/404 of query aligns to 2:395/408 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 (= R90) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (≠ A92) mutation to A: Decreases affinity for acetate.
- L122 (= L121) mutation to A: Decreases affinity for acetate.
- D148 (= D147) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F178) mutation to A: Decreases affinity for acetate.
- N211 (= N210) mutation to A: Slightly reduced enzyme activity.
- P232 (= P231) mutation to A: Decreases affinity for acetate.
- R241 (= R240) 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)
47% identity, 96% coverage: 4:392/404 of query aligns to 2:395/398 of 1tuuB
- active site: N7 (= N9), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E381)
- binding adenosine monophosphate: D283 (= D282), R285 (= R284), G331 (= G330), I332 (= I331), N335 (= N334), S336 (= S335)
- binding trihydrogen thiodiphosphate: H180 (= H179), G212 (= G211), R241 (= R240)
1tuuA Acetate kinase crystallized with atpgs (see paper)
47% identity, 96% coverage: 4:392/404 of query aligns to 2:395/399 of 1tuuA
- active site: N7 (= N9), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E381)
- binding adenosine-5'-diphosphate: K14 (= K16), G210 (= G209), D283 (= D282), F284 (≠ Y283), R285 (= R284), G331 (= G330), I332 (= I331), N335 (= N334)
- binding sulfate ion: R91 (= R90), H180 (= H179), G212 (= G211)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwsA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding cytidine-5'-triphosphate: G202 (= G209), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: V21 (≠ M22), C24 (≠ G25), H115 (= H122), N203 (= N210), T232 (= T239), R233 (= R240), K262 (≠ N269)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwrA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding cytidine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwqA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding guanosine-5'-triphosphate: H172 (= H179), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ Y283), R277 (= R284), E280 (= E287), G323 (= G330), I324 (= I331), N327 (= N334)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwpA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding 1,2-ethanediol: S11 (= S12), H115 (= H122), K262 (≠ N269)
- binding guanosine-5'-diphosphate: N203 (= N210), D275 (= D282), L276 (≠ Y283), R277 (= R284), E280 (= E287), G323 (= G330), I324 (= I331), N327 (= N334), S328 (= S335)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwoA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding guanosine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ Y283), R277 (= R284), E280 (= E287), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: E100 (= E107), N104 (≠ E111)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwnA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding adenosine-5'-tetraphosphate: H172 (= H179), H200 (= H207), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwmA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding adenosine-5'-triphosphate: H172 (= H179), H200 (= H207), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: H172 (= H179), R233 (= R240)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 4fwkA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding adenosine monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
- binding 1,2-ethanediol: D103 (≠ A110), N104 (≠ E111), R107 (= R114)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 2e1zA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N9), R83 (= R90), H115 (= H122), G202 (= G209), N203 (= N210), G204 (= G211), P224 (= P231), R233 (= R240), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 1x3nA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G209), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ Y283), R277 (= R284), G323 (= G330), I324 (= I331), N327 (= N334)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
44% identity, 96% coverage: 5:392/404 of query aligns to 4:389/394 of 1x3mA
- active site: N8 (= N9), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E381)
- binding adenosine-5'-diphosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ Y283), R277 (= R284), G322 (= G329), G323 (= G330), I324 (= I331), N327 (= N334)
9dv9A The amp-bound structure of acka from treponema vincentii (see paper)
39% identity, 96% coverage: 5:392/404 of query aligns to 7:403/453 of 9dv9A
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
41% identity, 96% coverage: 4:392/404 of query aligns to 5:378/381 of 4iz9A
- active site: N10 (= N9), R74 (= R90), H163 (= H179), R224 (= R240), E367 (= E381)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K16), G193 (= G209), N194 (= N210), D265 (= D282), F266 (≠ Y283), R267 (= R284), G313 (= G330), I314 (= I331), N317 (= N334), D318 (≠ S335)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
39% identity, 95% coverage: 5:387/404 of query aligns to 4:371/376 of 4ijnA
- active site: N8 (= N9), R72 (= R90), H161 (= H179), R222 (= R240), E365 (= E381)
- binding adenosine monophosphate: G191 (= G209), N192 (= N210), D263 (= D282), F264 (≠ Y283), R265 (= R284), G311 (= G330), V312 (≠ I331), N315 (= N334), V316 (≠ S335)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
25% identity, 44% coverage: 174:349/404 of query aligns to 149:323/375 of 1sazA
- active site: R214 (= R240)
- binding phosphomethylphosphonic acid adenylate ester: H154 (= H179), G184 (= G209), G185 (≠ N210), G186 (= G211), S254 (= S280), D255 (= D282), A256 (≠ Y283), R257 (= R284), G304 (= G330), L305 (≠ I331), H307 (≠ E333)
Query Sequence
>BWI76_RS23200 FitnessBrowser__Koxy:BWI76_RS23200
MSYKIMAINAGSSSLKFQLLEMPQGETLCQGLIERIGMANAQVTLKTPAQKWQESAPIAD
HREAVTLLLEKLLGYRIIESLQDIDGVGHRVAHGGERFKDSTPVTDESLAEIERLAELAP
LHNPVNALGIKVFRQLLPDTPSVAVFDTAFHQTLDERAFIYPLPWRYYSELGIRRYGFHG
TSHKYVSATLAEKLGVPLSALRVVCCHLGNGSSVCAIKGGRSVNTSMGFTPQSGVMMGTR
SGDIDPSILPWLALHEGQTPEQLNQLLNNESGLLGVSGVSHDYRDVEQAADGGNRRAALA
LALFAERIRATIGSYIMQMGGIDALIFTGGIGENSARARSAICHNLNFLGLSVDEEKNQH
NATFIQAEHALVKVAVINTNEELMIARDVMRLALPAAETLTVSA
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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