SitesBLAST
Comparing GFF2838 FitnessBrowser__Phaeo:GFF2838 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 18 hits to proteins with known functional sites (download)
1tuuB Acetate kinase crystallized with atpgs (see paper)
38% identity, 98% coverage: 8:385/386 of query aligns to 2:398/398 of 1tuuB
- active site: N7 (= N13), R91 (= R87), H180 (= H175), R241 (= R235), E384 (= E371)
- binding adenosine monophosphate: D283 (= D275), R285 (= R277), G331 (= G320), I332 (= I321), N335 (= N324), S336 (≠ A325)
- binding trihydrogen thiodiphosphate: H180 (= H175), G212 (= G206), R241 (= R235)
1tuuA Acetate kinase crystallized with atpgs (see paper)
38% identity, 98% coverage: 8:385/386 of query aligns to 2:398/399 of 1tuuA
- active site: N7 (= N13), R91 (= R87), H180 (= H175), R241 (= R235), E384 (= E371)
- binding adenosine-5'-diphosphate: K14 (= K20), G210 (= G204), D283 (= D275), F284 (≠ M276), R285 (= R277), G331 (= G320), I332 (= I321), N335 (= N324)
- binding sulfate ion: R91 (= R87), H180 (= H175), G212 (= G206)
P38502 Acetate kinase; Acetokinase; EC 2.7.2.1 from Methanosarcina thermophila (see 5 papers)
38% identity, 98% coverage: 8:385/386 of query aligns to 2:398/408 of P38502
- N7 (= N13) 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 (= S16) mutation S->A,T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
- S12 (= S18) 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 (= K20) 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 (= F174) mutation to A: Decreases affinity for acetate.
- N211 (= N205) mutation to A: Slightly reduced enzyme activity.
- P232 (= P226) mutation to A: Decreases affinity for acetate.
- R241 (= R235) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E371) mutation to A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity.
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwsA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding cytidine-5'-triphosphate: G202 (= G204), N203 (= N205), G204 (= G206), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
- binding 1,2-ethanediol: V21 (≠ T26), C24 (≠ L28), H115 (= H119), N203 (= N205), T232 (= T234), R233 (= R235), K262 (≠ N262)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwrA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding cytidine-5'-monophosphate: G202 (= G204), N203 (= N205), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwqA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding guanosine-5'-triphosphate: H172 (= H175), N203 (= N205), G204 (= G206), D275 (= D275), L276 (≠ M276), R277 (= R277), E280 (vs. gap), G323 (= G320), I324 (= I321), N327 (= N324)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwpA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding 1,2-ethanediol: S11 (= S16), H115 (= H119), K262 (≠ N262)
- binding guanosine-5'-diphosphate: N203 (= N205), D275 (= D275), L276 (≠ M276), R277 (= R277), E280 (vs. gap), G323 (= G320), I324 (= I321), N327 (= N324), S328 (≠ A325)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwoA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding guanosine-5'-monophosphate: G202 (= G204), N203 (= N205), D275 (= D275), L276 (≠ M276), R277 (= R277), E280 (vs. gap), G323 (= G320), I324 (= I321), N327 (= N324)
- binding 1,2-ethanediol: E100 (= E104), N104 (≠ E108)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwnA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding adenosine-5'-tetraphosphate: H172 (= H175), H200 (= H202), N203 (= N205), G204 (= G206), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwmA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding adenosine-5'-triphosphate: H172 (= H175), H200 (= H202), N203 (= N205), G204 (= G206), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
- binding 1,2-ethanediol: H172 (= H175), R233 (= R235)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 4fwkA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding adenosine monophosphate: G202 (= G204), N203 (= N205), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
- binding 1,2-ethanediol: D103 (≠ A107), N104 (≠ E108), R107 (≠ D111)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 2e1zA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N13), R83 (= R87), H115 (= H119), G202 (= G204), N203 (= N205), G204 (= G206), P224 (= P226), R233 (= R235), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 1x3nA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G204), N203 (= N205), G204 (= G206), D275 (= D275), L276 (≠ M276), R277 (= R277), G323 (= G320), I324 (= I321), N327 (= N324)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
40% identity, 96% coverage: 9:379/386 of query aligns to 4:386/394 of 1x3mA
- active site: N8 (= N13), R83 (= R87), H172 (= H175), R233 (= R235), E378 (= E371)
- binding adenosine-5'-diphosphate: G202 (= G204), N203 (= N205), D275 (= D275), L276 (≠ M276), R277 (= R277), G322 (= G319), G323 (= G320), I324 (= I321), N327 (= N324)
7fj9A Kpacka (pduw) with amppnp complex structure
40% identity, 97% coverage: 8:382/386 of query aligns to 3:391/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
40% identity, 97% coverage: 8:382/386 of query aligns to 3:391/395 of 7fj8A
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
37% identity, 96% coverage: 8:376/386 of query aligns to 3:370/376 of 4ijnA
- active site: N8 (= N13), R72 (= R87), H161 (= H175), R222 (= R235), E365 (= E371)
- binding adenosine monophosphate: G191 (= G204), N192 (= N205), D263 (= D275), F264 (≠ M276), R265 (= R277), G311 (= G320), V312 (≠ I321), N315 (= N324), V316 (≠ A325)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
36% identity, 98% coverage: 6:384/386 of query aligns to 3:380/381 of 4iz9A
- active site: N10 (= N13), R74 (= R87), H163 (= H175), R224 (= R235), E367 (= E371)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K20), G193 (= G204), N194 (= N205), D265 (≠ S274), F266 (≠ D275), R267 (≠ M276), G313 (= G320), I314 (= I321), N317 (= N324), D318 (≠ A325)
Query Sequence
>GFF2838 FitnessBrowser__Phaeo:GFF2838
MSPRSADNILILNAGSSSIKFAIFDTDLNQRLAGLAEGIGTPQSRLRIADTSRDSQLPTH
AEALAAILAALPDHGLDPTQLAAVGHRVVHGGRKLTKPVRITPEIRAEIADCTPLAPLHN
PHSLAAIDTMATTAPDLPQFASFDTSFHATNPEVATRYAIPRVEETKGIRRYGFHGLSYA
SLVRRLPEISGAALPSRLLAFHLGNGASLCAIRNGQSVATTMGYSPLDGLTMGTRSGGID
ANAVLRLVEDNGLDRTKAILNNESGLLGLSGGKSDMRNLMLDPSADSAFAIEHFCYWSLR
HAGSLIAAMEGLDAIAFTGGIGENAVGVRARILRGLEWIGARMDVDANHARKSRLHAGSS
KVAIWVVEAEEERQIAMDAQTLMGTP
Or try a new SitesBLAST search
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