SitesBLAST
Comparing GFF1535 FitnessBrowser__Marino:GFF1535 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)
45% identity, 99% coverage: 5:397/398 of query aligns to 3:401/408 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 (= R86) mutation R->A,L: Decreases catalytic activity. Decreases affinity for acetate.
- V93 (= V88) mutation to A: Decreases affinity for acetate.
- L122 (= L117) mutation to A: Decreases affinity for acetate.
- D148 (= D143) 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 (= N206) mutation to A: Slightly reduced enzyme activity.
- P232 (= P227) mutation to A: Decreases affinity for acetate.
- R241 (= R236) mutation R->K,L: Decreases catalytic activity. Strongly reduced affinity for ATP.
- E384 (= E380) 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)
45% identity, 98% coverage: 5:395/398 of query aligns to 3:399/399 of 1tuuA
- active site: N7 (= N9), R91 (= R86), H180 (= H175), R241 (= R236), E384 (= E380)
- binding adenosine-5'-diphosphate: K14 (= K16), G210 (= G205), D283 (= D277), F284 (≠ M278), R285 (= R279), G331 (= G325), I332 (= I326), N335 (= N329)
- binding sulfate ion: R91 (= R86), H180 (= H175), G212 (= G207)
1tuuB Acetate kinase crystallized with atpgs (see paper)
45% identity, 97% coverage: 5:391/398 of query aligns to 3:395/398 of 1tuuB
- active site: N7 (= N9), R91 (= R86), H180 (= H175), R241 (= R236), E384 (= E380)
- binding adenosine monophosphate: D283 (= D277), R285 (= R279), G331 (= G325), I332 (= I326), N335 (= N329), S336 (= S330)
- binding trihydrogen thiodiphosphate: H180 (= H175), G212 (= G207), R241 (= R236)
7fj9A Kpacka (pduw) with amppnp complex structure
45% identity, 97% coverage: 5:392/398 of query aligns to 4:392/395 of 7fj9A
7fj8A Kpacka (pduw) with amp complex structure
45% identity, 97% coverage: 5:392/398 of query aligns to 4:392/395 of 7fj8A
4fwsA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with ctp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwsA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding cytidine-5'-triphosphate: G202 (= G205), N203 (= N206), G204 (= G207), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
- binding 1,2-ethanediol: V21 (vs. gap), C24 (≠ H24), H115 (= H118), N203 (= N206), T232 (= T235), R233 (= R236), K262 (≠ Q264)
4fwrA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with cmp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwrA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding cytidine-5'-monophosphate: G202 (= G205), N203 (= N206), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
4fwqA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gtp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwqA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding guanosine-5'-triphosphate: H172 (= H175), N203 (= N206), G204 (= G207), D275 (= D277), L276 (≠ M278), R277 (= R279), E280 (≠ C282), G323 (= G325), I324 (= I326), N327 (= N329)
4fwpA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gdp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwpA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding 1,2-ethanediol: S11 (= S12), H115 (= H118), K262 (≠ Q264)
- binding guanosine-5'-diphosphate: N203 (= N206), D275 (= D277), L276 (≠ M278), R277 (= R279), E280 (≠ C282), G323 (= G325), I324 (= I326), N327 (= N329), S328 (= S330)
4fwoA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with gmp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwoA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding guanosine-5'-monophosphate: G202 (= G205), N203 (= N206), D275 (= D277), L276 (≠ M278), R277 (= R279), E280 (≠ C282), G323 (= G325), I324 (= I326), N327 (= N329)
- binding 1,2-ethanediol: E100 (≠ D103), N104 (≠ A107)
4fwnA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with adenosine tetraphosphate (ap4) (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwnA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding adenosine-5'-tetraphosphate: H172 (= H175), H200 (= H203), N203 (= N206), G204 (= G207), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
4fwmA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with atp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwmA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding adenosine-5'-triphosphate: H172 (= H175), H200 (= H203), N203 (= N206), G204 (= G207), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
- binding 1,2-ethanediol: H172 (= H175), R233 (= R236)
4fwkA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with amp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 4fwkA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding adenosine monophosphate: G202 (= G205), N203 (= N206), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
- binding 1,2-ethanediol: D103 (≠ K106), N104 (≠ A107), R107 (≠ S110)
2e1zA Crystal structure of salmonella typhimurium propionate kinase (tdcd) in complex with diadenosine tetraphosphate (ap4a) obtained after co- crystallization with atp (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 2e1zA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding bis(adenosine)-5'-tetraphosphate: N8 (= N9), R83 (= R86), H115 (= H118), G202 (= G205), N203 (= N206), G204 (= G207), P224 (= P227), R233 (= R236), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
1x3nA Crystal structure of amppnp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 1x3nA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G205), N203 (= N206), G204 (= G207), D275 (= D277), L276 (≠ M278), R277 (= R279), G323 (= G325), I324 (= I326), N327 (= N329)
1x3mA Crystal structure of adp bound propionate kinase (tdcd) from salmonella typhimurium (see paper)
45% identity, 97% coverage: 4:391/398 of query aligns to 3:389/394 of 1x3mA
- active site: N8 (= N9), R83 (= R86), H172 (= H175), R233 (= R236), E378 (= E380)
- binding adenosine-5'-diphosphate: G202 (= G205), N203 (= N206), D275 (= D277), L276 (≠ M278), R277 (= R279), G322 (= G324), G323 (= G325), I324 (= I326), N327 (= N329)
4ijnA Crystal structure of an acetate kinase from mycobacterium smegmatis bound to amp and sulfate (see paper)
43% identity, 96% coverage: 4:386/398 of query aligns to 3:371/376 of 4ijnA
- active site: N8 (= N9), R72 (= R86), H161 (= H175), R222 (= R236), E365 (= E380)
- binding adenosine monophosphate: G191 (= G205), N192 (= N206), D263 (= D277), F264 (≠ M278), R265 (= R279), G311 (= G325), V312 (≠ I326), N315 (= N329), V316 (≠ S330)
4iz9A Crystal structure of an acetate kinase from mycobacterium avium bound to an unknown acid-apcpp conjugate and manganese (see paper)
42% identity, 98% coverage: 5:393/398 of query aligns to 6:380/381 of 4iz9A
- active site: N10 (= N9), R74 (= R86), H163 (= H175), R224 (= R236), E367 (= E380)
- binding diphosphomethylphosphonic acid adenosyl ester: K17 (= K16), G193 (= G205), N194 (= N206), D265 (= D277), F266 (≠ M278), R267 (= R279), G313 (= G325), I314 (= I326), N317 (= N329), D318 (≠ S330)
1sazA Membership in the askha superfamily: enzymological properties and crystal structure of butyrate kinase 2 from thermotoga maritima (see paper)
28% identity, 39% coverage: 170:326/398 of query aligns to 149:305/375 of 1sazA
Sites not aligning to the query:
Query Sequence
>GFF1535 FitnessBrowser__Marino:GFF1535
MEDTVLVVNCGSSSLKLALFNNQHRKLVSALAERLGQSDAFAHIDGQEGTIPLDAGAGHD
QALETLVTAFRDLGLMTTAPSAIGHRVVHGGETFHEAVLIDGDVLKAIESCAGLAPLHNP
VNLSGIRATLAQFPDVPQTAVFDTAFHQTLPRRAFLYALPEAWYRDWGIRRYGFHGTSHA
FMASEAARLLGKTPATTSVISAHLGNGCSITAIRDGISVDTSMGLTPLEGLVMGTRSGDV
DPGLFDFLRSKGIAADEVHRVLNQESGLLGLSGQTNDMRSLCELADHGHEPSQTAIDVFC
FRLARYVGAMMASLSQLDALVFTGGIGENSPRIREETIRHLKLTGFELSQDLNIHHGQFS
DGHIESPDSRFPVLVIPTNEELVIAREATRLAGSDIQA
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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