SitesBLAST
Comparing WP_012101780.1 NCBI__GCF_000016505.1:WP_012101780.1 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)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
60% identity, 100% coverage: 1:404/405 of query aligns to 1:404/408 of P38502
- N7 (= N7) 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 (= S10) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S12) 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 (= K14) 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 (= V92) 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 (= E384) 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)
61% identity, 98% coverage: 1:397/405 of query aligns to 1:397/399 of 1tuuA
- active site: N7 (= N7), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E384)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G209), D283 (= D282), F284 (= F283), R285 (= R284), G331 (= G331), I332 (≠ V332), N335 (= N335)
- binding sulfate ion: R91 (= R90), H180 (= H179), G212 (= G211)
1tuuB Acetate kinase crystallized with atpgs (see paper)
61% identity, 98% coverage: 1:397/405 of query aligns to 1:397/398 of 1tuuB
- active site: N7 (= N7), R91 (= R90), H180 (= H179), R241 (= R240), E384 (= E384)
- binding adenosine monophosphate: D283 (= D282), R285 (= R284), G331 (= G331), I332 (≠ V332), N335 (= N335), S336 (= S336)
- binding trihydrogen thiodiphosphate: H180 (= H179), G212 (= G211), R241 (= R240)
7fj9A Kpacka (pduw) with amppnp complex structure
49% identity, 98% coverage: 2:396/405 of query aligns to 3:392/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
49% identity, 98% coverage: 2:396/405 of query aligns to 3:392/395 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, 96% coverage: 2:391/405 of query aligns to 5:374/381 of 4iz9A
- active site: N10 (= N7), R74 (= R90), H163 (= H179), R224 (= R240), E367 (= E384)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K14), G193 (= G209), N194 (= N210), D265 (= D282), F266 (= F283), R267 (= R284), G313 (= G331), I314 (≠ V332), N317 (= N335), D318 (≠ S336)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
43% identity, 96% coverage: 1:390/405 of query aligns to 2:371/376 of 4ijnA
- active site: N8 (= N7), R72 (= R90), H161 (= H179), R222 (= R240), E365 (= E384)
- binding adenosine monophosphate: G191 (= G209), N192 (= N210), D263 (= D282), F264 (= F283), R265 (= R284), G311 (= G331), V312 (= V332), N315 (= N335), V316 (≠ S336)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwsA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding cytidine-5'-triphosphate: G202 (= G209), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
- binding 1,2-ethanediol: V21 (≠ M20), C24 (≠ E23), 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)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwrA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding cytidine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwqA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding guanosine-5'-triphosphate: H172 (= H179), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ F283), R277 (= R284), E280 (= E287), G323 (= G331), I324 (≠ V332), N327 (= N335)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwpA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H122), K262 (≠ N269)
- binding guanosine-5'-diphosphate: N203 (= N210), D275 (= D282), L276 (≠ F283), R277 (= R284), E280 (= E287), G323 (= G331), I324 (≠ V332), N327 (= N335), S328 (= S336)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwoA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding guanosine-5'-monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ F283), R277 (= R284), E280 (= E287), G323 (= G331), I324 (≠ V332), N327 (= N335)
- binding 1,2-ethanediol: E100 (≠ K107), N104 (≠ S111)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwnA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding adenosine-5'-tetraphosphate: H172 (= H179), H200 (= H207), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwmA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding adenosine-5'-triphosphate: H172 (= H179), H200 (= H207), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
- binding 1,2-ethanediol: H172 (= H179), R233 (= R240)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 4fwkA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding adenosine monophosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
- binding 1,2-ethanediol: D103 (≠ E110), N104 (≠ S111), R107 (≠ D114)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 2e1zA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N7), R83 (= R90), H115 (= H122), G202 (= G209), N203 (= N210), G204 (= G211), P224 (= P231), R233 (= R240), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 1x3nA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G209), N203 (= N210), G204 (= G211), D275 (= D282), L276 (≠ F283), R277 (= R284), G323 (= G331), I324 (≠ V332), N327 (= N335)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
41% identity, 97% coverage: 3:395/405 of query aligns to 4:389/394 of 1x3mA
- active site: N8 (= N7), R83 (= R90), H172 (= H179), R233 (= R240), E378 (= E384)
- binding adenosine-5'-diphosphate: G202 (= G209), N203 (= N210), D275 (= D282), L276 (≠ F283), R277 (= R284), G322 (≠ A330), G323 (= G331), I324 (≠ V332), N327 (= N335)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
30% identity, 39% coverage: 174:332/405 of query aligns to 149:305/375 of 1sazA
Sites not aligning to the query:
Query Sequence
>WP_012101780.1 NCBI__GCF_000016505.1:WP_012101780.1
MKILEVNCGSSSLKYQLIDMEDEKVLAKGLVERIGIDGSILTHKVNGEKHVVSEPIKDHR
VAVKLVLEALVDKQHGVIKDMSEISAVGHRVVHGGEQYSDAVIIDDKVMESLKDCSKLAP
LHNPPNIIGINACKAIMPNTPMVAVFDTAFHHTMPKYAYIYPLPYELYERYGIRKYGFHG
TSHRFVSEEAARLMGKDISELKIITCHLGNGASICAVDRGKSIDTNMGFTPLAGLAMGTR
CGDIDPAIIPFLTNEIGMSIDEISNIMNNKSGILGMSGISSDFRDVEEIASFKHDRRAQL
ALDVFYYRVKSFIGSYVAVLDGVDAIVFTAGVGENSSIGRAEICSGLTYLGITIDEEKNN
IRGKATEITTANSKTKVFVIPTNEELVIARDTKFLVQKKISHKSK
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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