SitesBLAST
Comparing WP_012469810.1 NCBI__GCF_000020385.1:WP_012469810.1 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)
1tuuA Acetate kinase crystallized with atpgs (see paper)
53% identity, 95% coverage: 1:399/421 of query aligns to 1:396/399 of 1tuuA
- active site: N7 (= N7), R91 (= R91), H180 (= H180), R241 (= R241), E384 (= E387)
- binding adenosine-5'-diphosphate: K14 (= K14), G210 (= G210), D283 (= D283), F284 (≠ R284), R285 (= R285), G331 (= G331), I332 (≠ V332), N335 (≠ M335)
- binding sulfate ion: R91 (= R91), H180 (= H180), G212 (= G212)
1tuuB Acetate kinase crystallized with atpgs (see paper)
53% identity, 95% coverage: 1:399/421 of query aligns to 1:396/398 of 1tuuB
- active site: N7 (= N7), R91 (= R91), H180 (= H180), R241 (= R241), E384 (= E387)
- binding adenosine monophosphate: D283 (= D283), R285 (= R285), G331 (= G331), I332 (≠ V332), N335 (≠ M335), S336 (≠ G336)
- binding trihydrogen thiodiphosphate: H180 (= H180), G212 (= G212), R241 (= R241)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
53% identity, 95% coverage: 1:399/421 of query aligns to 1:396/408 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 (= R91) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V93) mutation to A: Decreases affinity for acetate.
- L122 (= L122) mutation to A: Decreases affinity for acetate.
- D148 (= D148) active site, Proton donor/acceptor; mutation D->A,E,N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP.
- F179 (= F179) mutation to A: Decreases affinity for acetate.
- N211 (= N211) mutation to A: Slightly reduced enzyme activity.
- P232 (= P232) mutation to A: Decreases affinity for acetate.
- R241 (= R241) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E387) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
7fj9A Kpacka (pduw) with amppnp complex structure
44% identity, 94% coverage: 3:398/421 of query aligns to 4:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
44% identity, 94% coverage: 3:398/421 of query aligns to 4:391/395 of 7fj8A
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
43% identity, 95% coverage: 3:401/421 of query aligns to 6:381/381 of 4iz9A
- active site: N10 (= N7), R74 (= R91), H163 (= H180), R224 (= R241), E367 (= E387)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K14), G193 (= G210), N194 (= N211), D265 (= D283), F266 (≠ R284), R267 (= R285), G313 (= G331), I314 (≠ V332), N317 (≠ M335), D318 (≠ G336)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
42% identity, 94% coverage: 3:398/421 of query aligns to 4:376/376 of 4ijnA
- active site: N8 (= N7), R72 (= R91), H161 (= H180), R222 (= R241), E365 (= E387)
- binding adenosine monophosphate: G191 (= G210), N192 (= N211), D263 (= D283), F264 (≠ R284), R265 (= R285), G311 (= G331), V312 (= V332), N315 (≠ M335), V316 (≠ G336)
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwsA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding cytidine-5'-triphosphate: G202 (= G210), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
- binding 1,2-ethanediol: V21 (≠ W20), C24 (≠ K23), H115 (= H123), N203 (= N211), T232 (= T240), R233 (= R241), K262 (= K270)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwrA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding cytidine-5'-monophosphate: G202 (= G210), N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwqA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding guanosine-5'-triphosphate: H172 (= H180), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), E280 (≠ I288), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwpA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding 1,2-ethanediol: S11 (= S10), H115 (= H123), K262 (= K270)
- binding guanosine-5'-diphosphate: N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), E280 (≠ I288), G323 (= G331), I324 (≠ V332), N327 (≠ M335), S328 (≠ G336)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwoA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding guanosine-5'-monophosphate: G202 (= G210), N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), E280 (≠ I288), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
- binding 1,2-ethanediol: E100 (≠ D108), N104 (≠ A112)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwnA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding adenosine-5'-tetraphosphate: H172 (= H180), H200 (= H208), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwmA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding adenosine-5'-triphosphate: H172 (= H180), H200 (= H208), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
- binding 1,2-ethanediol: H172 (= H180), R233 (= R241)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 4fwkA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding adenosine monophosphate: G202 (= G210), N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
- binding 1,2-ethanediol: D103 (≠ N111), N104 (≠ A112), R107 (≠ D115)
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, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 2e1zA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N7), R83 (= R91), H115 (= H123), G202 (= G210), N203 (= N211), G204 (= G212), P224 (= P232), R233 (= R241), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 1x3nA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G210), N203 (= N211), G204 (= G212), D275 (= D283), L276 (≠ R284), R277 (= R285), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
39% identity, 95% coverage: 2:400/421 of query aligns to 3:391/394 of 1x3mA
- active site: N8 (= N7), R83 (= R91), H172 (= H180), R233 (= R241), E378 (= E387)
- binding adenosine-5'-diphosphate: G202 (= G210), N203 (= N211), D275 (= D283), L276 (≠ R284), R277 (= R285), G322 (≠ A330), G323 (= G331), I324 (≠ V332), N327 (≠ M335)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
26% identity, 38% coverage: 175:332/421 of query aligns to 149:305/375 of 1sazA
Sites not aligning to the query:
Query Sequence
>WP_012469810.1 NCBI__GCF_000020385.1:WP_012469810.1
MIIMALNCGSSSVKYQLFDWDKKVVVAKGMVERVIVGDSYIVHEVPGRDNYKLEQDCPDH
RAAIDLVIRTVTDRECGVLQSVAEISAVGHRVVHGGEKFTCSVRIDDDVLNAVKDVQHLA
PLHNPPNIEGIEAARALMPAIPHVAIFDTAFHQTMPEHAFLYPVPYDWYENHGVRRYGFH
GTSHLYVSKRAAMLLGKPAEQCNIITMHIGNGVSHCAIKGGVSVDTTMGLTPLEGAVMGT
RSGDIDPAIPAFMMQKENLSAKEIDSVLNKKSGILGITGRYTDRRDVIEHAAKGDHRCQL
ALDIEAYRLKKYIGAYMAAIGKLDAVVFTAGVGEMGAAIREKAIEGLEHIGIHLDRERNA
GAMTRKRESLITTDDSPVKVYVIPTDEELVFTEDVVAILNGTYTDHMQFEYSFAKPDFVR
T
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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