SitesBLAST
Comparing WP_072781751.1 NCBI__GCF_900143065.1:WP_072781751.1 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)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
54% identity, 99% coverage: 2:537/543 of query aligns to 1:535/539 of P0DX84
- H231 (= H233) mutation to A: Retains 74% of wild-type activity.
- W235 (= W237) mutation to A: Almost completely abolishes the activity.
- G302 (= G304) mutation to P: Almost completely abolishes the activity.
- G303 (= G305) mutation to P: Almost completely abolishes the activity.
- W326 (= W328) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P335) mutation to A: Retains 69% of wild-type activity.
- R432 (= R434) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K436) mutation to A: Retains 36% of wild-type activity.
- D435 (= D437) mutation to A: Retains 76% of wild-type activity.
- K438 (= K440) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G442) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G443) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E444) mutation to A: Retains 27% of wild-type activity.
- W443 (= W445) mutation to A: Retains 60% of wild-type activity.
- E474 (= E476) mutation to A: Retains 33% of wild-type activity.
- K523 (= K525) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K528) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
53% identity, 99% coverage: 2:537/543 of query aligns to 1:535/538 of 6ijbB
- active site: T185 (= T187), H205 (= H207), H231 (= H233), S329 (≠ T331), E330 (= E332), K438 (= K440), W443 (= W445), A523 (≠ K525)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W237), G303 (= G305), A325 (≠ G327), W326 (= W328), G327 (= G329), M328 (= M330)
- binding adenosine monophosphate: G303 (= G305), A304 (≠ S306), A305 (= A307), H324 (= H326), W326 (= W328), G327 (= G329), M328 (= M330), S329 (≠ T331), Q359 (= Q361), D417 (= D419)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
53% identity, 99% coverage: 2:537/543 of query aligns to 1:532/533 of 6ihkB
- active site: T185 (= T187), H202 (= H207), H228 (= H233), S326 (≠ T331), E327 (= E332), K435 (= K440), W440 (= W445), K520 (= K525)
- binding adenosine-5'-diphosphate: H228 (= H233), G300 (= G305), A301 (≠ S306), A302 (= A307), H321 (= H326), A322 (≠ G327), W323 (= W328), G324 (= G329), M325 (= M330), S326 (≠ T331), Q356 (= Q361), D414 (= D419), R429 (= R434), K520 (= K525)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
46% identity, 98% coverage: 6:538/543 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T187) binding Mg(2+)
- G302 (= G305) binding tetradecanoyl-AMP
- Q322 (≠ H326) binding tetradecanoyl-AMP
- G323 (= G327) binding tetradecanoyl-AMP
- T327 (= T331) binding tetradecanoyl-AMP
- E328 (= E332) binding Mg(2+)
- D418 (= D419) binding tetradecanoyl-AMP
- K435 (= K436) binding tetradecanoyl-AMP
- K439 (= K440) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
45% identity, 98% coverage: 6:538/543 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T187), H197 (= H207), H223 (= H233), T320 (= T331), E321 (= E332), K432 (= K440), W437 (= W445)
- binding adenosine monophosphate: G295 (= G305), S296 (= S306), A297 (= A307), G316 (= G327), Y317 (≠ W328), G318 (= G329), L319 (≠ M330), T320 (= T331), D411 (= D419), K428 (= K436), K432 (= K440), W437 (= W445)
- binding magnesium ion: T177 (= T187), E321 (= E332)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
44% identity, 98% coverage: 6:538/543 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T187), H197 (= H207), H223 (= H233), T320 (= T331), E321 (= E332), K432 (= K440), W437 (= W445)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H233), V224 (= V234), G295 (= G305), S296 (= S306), A297 (= A307), Y317 (≠ W328), G318 (= G329), L319 (≠ M330), T320 (= T331), D411 (= D419), I423 (= I431), K432 (= K440), W437 (= W445)
- binding magnesium ion: T177 (= T187), E321 (= E332)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
37% identity, 96% coverage: 11:533/543 of query aligns to 10:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G304), G293 (= G305), A294 (≠ S306), A295 (= A307), G314 (= G327), Y315 (≠ W328), M317 (= M330), S318 (≠ T331), D408 (= D419), R423 (= R434)
- binding 4'-phosphopantetheine: R93 (= R98), P220 (= P230), H223 (= H233)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
37% identity, 96% coverage: 11:533/543 of query aligns to 10:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
37% identity, 96% coverage: 11:533/543 of query aligns to 10:527/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
38% identity, 91% coverage: 40:533/543 of query aligns to 35:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G304), G293 (= G305), A295 (= A307), G314 (= G327), Y315 (≠ W328), G316 (= G329), M317 (= M330), S318 (≠ T331), D408 (= D419), K429 (= K440)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H233), W227 (= W237), G292 (= G304), G316 (= G329), P322 (= P335)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R98), P220 (= P230), H223 (= H233), I269 (≠ V280), G432 (= G443)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
38% identity, 91% coverage: 40:533/543 of query aligns to 33:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G305), A293 (= A307), G312 (= G327), Y313 (≠ W328), G314 (= G329), M315 (= M330), S316 (≠ T331), D406 (= D419), R421 (= R434)
- binding magnesium ion: M315 (= M330), S316 (≠ T331), E317 (= E332)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
38% identity, 91% coverage: 40:533/543 of query aligns to 33:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G305), A293 (= A307), Y313 (≠ W328), M315 (= M330), S316 (≠ T331), D406 (= D419), R421 (= R434)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W237), G290 (= G304), G312 (= G327), G314 (= G329), M315 (= M330), P320 (= P335), I321 (≠ L336)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
37% identity, 96% coverage: 11:533/543 of query aligns to 10:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T187), G174 (= G189), T175 (= T190), T176 (= T191), K180 (= K195), G293 (= G305), A294 (≠ S306), A295 (= A307), Y315 (≠ W328), M317 (= M330), S318 (≠ T331), D408 (= D419), R423 (= R434)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
37% identity, 96% coverage: 11:533/543 of query aligns to 8:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T331), E317 (= E332)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W237), G290 (= G304), G291 (= G305), A292 (≠ S306), A293 (= A307), G312 (= G327), Y313 (≠ W328), G314 (= G329), M315 (= M330), S316 (≠ T331), I321 (≠ L336), D406 (= D419), R421 (= R434), K427 (= K440), W432 (= W445)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
29% identity, 92% coverage: 40:539/543 of query aligns to 29:501/503 of P9WQ37
- K172 (= K195) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V234) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (= A236) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L239) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ K270) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G329) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W414) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D419) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R434) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S441) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G443) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K525) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
29% identity, 91% coverage: 42:534/543 of query aligns to 31:486/486 of 8wevA
Sites not aligning to the query:
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 92% coverage: 40:539/543 of query aligns to 32:501/502 of 3r44A
Sites not aligning to the query:
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
25% identity, 92% coverage: 42:539/543 of query aligns to 50:557/561 of P69451
- Y213 (= Y186) mutation to A: Loss of activity.
- T214 (= T187) mutation to A: 10% of wild-type activity.
- G216 (= G189) mutation to A: Decreases activity.
- T217 (= T190) mutation to A: Decreases activity.
- G219 (= G192) mutation to A: Decreases activity.
- K222 (= K195) mutation to A: Decreases activity.
- E361 (= E332) mutation to A: Loss of activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
26% identity, 90% coverage: 42:532/543 of query aligns to 37:509/518 of 4wv3B
- active site: S175 (≠ T187), T320 (= T331), E321 (= E332), K418 (= K440), W423 (= W445), K502 (= K525)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H233), T221 (≠ V234), F222 (≠ N235), A293 (≠ G304), S294 (≠ G305), E295 (≠ S306), A296 (= A307), G316 (= G327), I317 (≠ W328), G318 (= G329), C319 (≠ M330), T320 (= T331), D397 (= D419), H409 (≠ I431), R412 (= R434), K502 (= K525)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
28% identity, 92% coverage: 34:534/543 of query aligns to 41:531/537 of 6e97B
- active site: S190 (≠ T187), S210 (≠ H207), H234 (≠ P230), A336 (≠ T331), E337 (= E332), N437 (≠ K440), K442 (≠ W445), K522 (= K525)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (≠ P230), N235 (≠ M231), F236 (= F232), S240 (≠ A236), G310 (= G305), A311 (≠ S306), K312 (≠ A307), V332 (≠ G327), F333 (≠ W328), G334 (= G329), M335 (= M330), A336 (≠ T331), D416 (= D419), K433 (= K436), K442 (≠ W445)
Query Sequence
>WP_072781751.1 NCBI__GCF_900143065.1:WP_072781751.1
MLMGQMMDQPLLISGILEFAARHYANSEIVSQRVEGDLHRYTFRDCAQRAKQLAKALQAL
GLQMGERVATLAWNGYRHLEAYYAVSGSGAVLHTINPRLHPEQLAYICNHAEDQYLLFDF
CFLPLVEAIAPHCKTVKGFVLLGAADRMPAQTNIPNLLCYEDLLAAQSPDYTWPTFDEHA
AATLCYTSGTTGNPKGALYSHRSTVLHAYASALPNVLNVSSRDSVMPVVPMFHVNAWGLP
YSVPLSGAKMVFPGPALDGKSVYELMEQEKVTFSAGVPTVWLGLINYAMQHQLKFSTFHR
TVIGGSACPPAMMNTLIDEFDVQVIHGWGMTEMSPLGTTGGLLSKHLELPKAAQRQILQK
QGHAIYGVDMKIVDELGEELPWDGVTSGSLLVKGPWIIASYFKGEGGDVLEDGWFPTGDV
ATIDADGFMQITDRAKDVIKSGGEWIGTIDLENIAMSHPAVMQAACIGVFHPKWDERPLL
VVVRKPGQEVSREQLLAHFDGKVAKWWLPDDVVFADALPVGGTGKIQKNKLREQYRNYVL
PTT
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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