SitesBLAST
Comparing WP_028998686.1 NCBI__GCF_000430725.1:WP_028998686.1 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)
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)
38% identity, 95% coverage: 25:543/548 of query aligns to 22:536/541 of Q5SKN9
- T184 (= T193) binding Mg(2+)
- G302 (= G308) binding tetradecanoyl-AMP
- Q322 (≠ H328) binding tetradecanoyl-AMP
- G323 (≠ V329) binding tetradecanoyl-AMP
- T327 (= T333) binding tetradecanoyl-AMP
- E328 (= E334) binding Mg(2+)
- D418 (= D425) binding tetradecanoyl-AMP
- K435 (= K442) binding tetradecanoyl-AMP
- K439 (≠ I446) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 93% coverage: 25:533/548 of query aligns to 15:502/510 of 1v26B
- active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
- binding adenosine monophosphate: G295 (= G308), S296 (≠ A309), A297 (≠ P310), G316 (≠ V329), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), K428 (= K442), K432 (≠ I446), W437 (≠ N451)
- binding magnesium ion: T177 (= T193), E321 (= E334)
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)
33% identity, 95% coverage: 25:544/548 of query aligns to 14:536/539 of P0DX84
- H231 (= H237) mutation to A: Retains 74% of wild-type activity.
- W235 (= W241) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A307) mutation to P: Almost completely abolishes the activity.
- G303 (= G308) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y330) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G337) mutation to A: Retains 69% of wild-type activity.
- R432 (= R440) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K442) mutation to A: Retains 36% of wild-type activity.
- D435 (= D443) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I446) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G448) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G449) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E450) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N451) mutation to A: Retains 60% of wild-type activity.
- E474 (= E482) mutation to A: Retains 33% of wild-type activity.
- K523 (= K531) 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 (= K534) 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)
32% identity, 95% coverage: 25:544/548 of query aligns to 14:536/538 of 6ijbB
- active site: T185 (= T193), H205 (≠ N213), H231 (= H237), S329 (≠ T333), E330 (= E334), K438 (≠ I446), W443 (≠ N451), A523 (≠ K531)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W241), G303 (= G308), A325 (≠ V329), W326 (≠ Y330), G327 (= G331), M328 (≠ L332)
- binding adenosine monophosphate: G303 (= G308), A304 (= A309), A305 (≠ P310), H324 (= H328), W326 (≠ Y330), G327 (= G331), M328 (≠ L332), S329 (≠ T333), Q359 (= Q363), D417 (= D425)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
37% identity, 85% coverage: 25:488/548 of query aligns to 15:464/491 of 1v25A
- active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H237), V224 (≠ C238), G295 (= G308), S296 (≠ A309), A297 (≠ P310), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), I423 (= I437), K432 (≠ I446), W437 (≠ N451)
- binding magnesium ion: T177 (= T193), E321 (= E334)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 95% coverage: 25:544/548 of query aligns to 14:533/533 of 6ihkB
- active site: T185 (= T193), H202 (≠ N213), H228 (= H237), S326 (≠ T333), E327 (= E334), K435 (≠ I446), W440 (≠ N451), K520 (= K531)
- binding adenosine-5'-diphosphate: H228 (= H237), G300 (= G308), A301 (= A309), A302 (≠ P310), H321 (= H328), A322 (≠ V329), W323 (≠ Y330), G324 (= G331), M325 (≠ L332), S326 (≠ T333), Q356 (= Q363), D414 (= D425), R429 (= R440), K520 (= K531)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
31% identity, 95% coverage: 21:539/548 of query aligns to 17:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T193), G174 (= G195), T175 (= T196), T176 (= T197), K180 (= K201), G293 (= G308), A294 (= A309), A295 (≠ P310), Y315 (= Y330), M317 (≠ L332), S318 (≠ T333), D408 (= D425), R423 (= R440)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 95% coverage: 21:539/548 of query aligns to 15:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G308), A293 (≠ P310), G312 (≠ V329), Y313 (= Y330), G314 (= G331), M315 (≠ L332), S316 (≠ T333), D406 (= D425), R421 (= R440)
- binding magnesium ion: M315 (≠ L332), S316 (≠ T333), E317 (= E334)
8i51A Acyl-acp synthetase structure bound to amp-mc7
31% identity, 95% coverage: 21:539/548 of query aligns to 15:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G308), A293 (≠ P310), Y313 (= Y330), M315 (≠ L332), S316 (≠ T333), D406 (= D425), R421 (= R440)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W241), G290 (≠ A307), G312 (≠ V329), G314 (= G331), M315 (≠ L332), P320 (≠ G337), I321 (≠ P338)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
31% identity, 95% coverage: 21:539/548 of query aligns to 17:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A307), G293 (= G308), A294 (= A309), A295 (≠ P310), G314 (≠ V329), Y315 (= Y330), M317 (≠ L332), S318 (≠ T333), D408 (= D425), R423 (= R440)
- binding 4'-phosphopantetheine: R93 (= R104), P220 (= P234), H223 (= H237)
8i49A Acyl-acp synthetase structure bound to atp
31% identity, 95% coverage: 21:539/548 of query aligns to 17:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
31% identity, 95% coverage: 21:539/548 of query aligns to 17:527/530 of 8i22A
8jylA Acyl-acp synthetase structure bound to c10-ams
31% identity, 95% coverage: 21:539/548 of query aligns to 15:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T333), E317 (= E334)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W241), G290 (≠ A307), G291 (= G308), A292 (= A309), A293 (≠ P310), G312 (≠ V329), Y313 (= Y330), G314 (= G331), M315 (≠ L332), S316 (≠ T333), I321 (≠ P338), D406 (= D425), R421 (= R440), K427 (≠ I446), W432 (≠ N451)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
31% identity, 95% coverage: 21:539/548 of query aligns to 17:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A307), G293 (= G308), A295 (≠ P310), G314 (≠ V329), Y315 (= Y330), G316 (= G331), M317 (≠ L332), S318 (≠ T333), D408 (= D425), K429 (≠ I446)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H237), W227 (= W241), G292 (≠ A307), G316 (= G331), P322 (≠ G337)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R104), P220 (= P234), H223 (= H237), I269 (≠ V283), G432 (= G449)
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)
32% identity, 94% coverage: 26:540/548 of query aligns to 7:496/503 of P9WQ37
- R9 (≠ E28) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ Q36) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K201) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H226) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C238) 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 (≠ G240) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F243) 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 (≠ G273) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G331) 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 (= W420) 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 (= D425) 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 (= R440) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S447) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G449) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K531) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 94% coverage: 26:540/548 of query aligns to 10:496/502 of 3r44A
Sites not aligning to the query:
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 94% coverage: 26:539/548 of query aligns to 9:501/504 of 5ie3A
- active site: T163 (= T193), S183 (≠ N213), H207 (= H237), T308 (= T333), E309 (= E334), N408 (≠ I446), K413 (≠ N451), K493 (= K531)
- binding adenosine monophosphate: S164 (= S194), S282 (≠ I306), A283 (= A307), S284 (≠ G308), Y305 (= Y330), A306 (≠ G331), M307 (≠ L332), T308 (= T333), D387 (= D425), L399 (≠ I437), R402 (= R440), K493 (= K531)
- binding oxalic acid: V208 (≠ C238), S282 (≠ I306), A306 (≠ G331), M307 (≠ L332), H312 (≠ G337), K493 (= K531)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 94% coverage: 26:539/548 of query aligns to 9:503/506 of 5ie2A
- active site: T165 (= T193), S185 (≠ N213), H209 (= H237), T310 (= T333), E311 (= E334), N410 (≠ I446), K415 (≠ N451), K495 (= K531)
- binding adenosine-5'-triphosphate: T165 (= T193), S166 (= S194), G167 (= G195), T168 (= T196), T169 (= T197), S284 (≠ I306), A285 (= A307), S286 (≠ G308), Y307 (= Y330), A308 (≠ G331), M309 (≠ L332), T310 (= T333), D389 (= D425), L401 (≠ I437), R404 (= R440), K495 (= K531)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 95% coverage: 26:544/548 of query aligns to 8:479/484 of 5gtdA
- active site: T151 (= T193), S171 (≠ N213), H195 (= H237), T288 (= T333), E289 (= E334)
- binding adenosine-5'-monophosphate: G263 (= G308), G264 (≠ A309), Y285 (= Y330), G286 (= G331), M287 (≠ L332), T288 (= T333), D366 (= D425), V378 (≠ I437)
- binding magnesium ion: F314 (≠ Q370), S315 (≠ Q371)
- binding 2-succinylbenzoate: H195 (= H237), S197 (≠ N239), A237 (≠ G279), L260 (= L305), G262 (≠ A307), G263 (= G308), G286 (= G331), M287 (≠ L332), S292 (≠ A343), Q293 (≠ K344)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
29% identity, 95% coverage: 26:544/548 of query aligns to 8:479/485 of 5x8fB
- active site: T151 (= T193), S171 (≠ N213), H195 (= H237), T288 (= T333), E289 (= E334), I387 (= I446), N392 (= N451), K470 (= K531)
- binding magnesium ion: Y23 (= Y42), E24 (≠ G43), H70 (≠ F89), N178 (≠ A220), L202 (≠ P244), L214 (≠ C256), T296 (≠ H347), L297 (≠ W348), S298 (≠ A349)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R104), L191 (= L233), P192 (= P234), H195 (= H237), I196 (≠ C238), S197 (≠ N239), A237 (≠ G279), V238 (= V283), L260 (= L305), G262 (≠ A307), G286 (= G331), M287 (≠ L332), S292 (≠ A343), Q293 (≠ K344), S388 (= S447), G389 (= G448), G390 (= G449), E391 (= E450), K420 (= K479), W421 (= W480), K450 (≠ R512), Y451 (≠ F513)
Query Sequence
>WP_028998686.1 NCBI__GCF_000430725.1:WP_028998686.1
MTRINPYSLGLDRNAANFVALSPLSFIERAALVYPQRTAIVYGALRQDWKSTYERCRRLA
SALVKQGVGTGDTVAAMLPNVPAMFEAHFGVPMSGAVLNTLNTRLDAEAIAFMLQHGEAK
VLLTDREFAPVVARALELLGDKRPLVIEVEDETAPAGARLGEIGYEALLASGDPHFAWKL
PADEWDAIALNYTSGTTGNPKGVVTHHRGAYLNAANNVIAWSLPHHPVYLWTLPMFHCNG
WCFPWTMALVAGTSVCLRKVDPLQIWPLMREHGVTHLCGAPIVYSMLINAPAELRQGLGR
VVRGLIAGAPPPAVVIEGCESAGIEITHVYGLTEVYGPAAVCAKQEHWAALPAQERAQLN
GRQGVAYPLQQAVVVLDPDTLQPVPADGETMGEICFRGNVVMKGYLKNPGATEEAFAGGW
FHTGDLAVVHPDGYVKIKDRSKDIIISGGENISSIEVEDVLHRHPDVMLASVVALPDEKW
GEVPCAFVELKPGAPTVTEQELIEFCRTHLARFKVPKRIVFAEVPKTSTGKIQKFLLRQR
AKSASAIE
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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