SitesBLAST
Comparing AO356_29235 FitnessBrowser__pseudo5_N2C3_1:AO356_29235 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)
35% identity, 96% coverage: 10:536/550 of query aligns to 1:533/541 of Q5SKN9
- T184 (= T191) binding
- G302 (= G304) binding
- Q322 (≠ H324) binding
- G323 (≠ V325) binding
- T327 (= T329) binding
- E328 (= E330) binding
- D418 (= D421) binding
- K435 (= K438) binding
- K439 (≠ I442) binding
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)
32% identity, 94% coverage: 19:536/550 of query aligns to 9:532/539 of P0DX84
- H231 (= H235) mutation to A: Retains 74% of wild-type activity.
- W235 (= W239) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A303) mutation to P: Almost completely abolishes the activity.
- G303 (= G304) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y326) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G333) mutation to A: Retains 69% of wild-type activity.
- R432 (= R436) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K438) mutation to A: Retains 36% of wild-type activity.
- D435 (= D439) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I442) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G444) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G445) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E446) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N447) mutation to A: Retains 60% of wild-type activity.
- E474 (= E478) mutation to A: Retains 33% of wild-type activity.
- K523 (= K527) 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 (= K530) 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, 94% coverage: 19:536/550 of query aligns to 9:532/538 of 6ijbB
- active site: T185 (= T191), H205 (≠ M211), H231 (= H235), S329 (≠ T329), E330 (= E330), K438 (≠ I442), W443 (≠ N447), A523 (≠ K527)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W239), G303 (= G304), A325 (≠ V325), W326 (≠ Y326), G327 (= G327), M328 (≠ I328)
- binding adenosine monophosphate: G303 (= G304), A304 (≠ S305), A305 (≠ P306), H324 (= H324), W326 (≠ Y326), G327 (= G327), M328 (≠ I328), S329 (≠ T329), Q359 (= Q359), D417 (= D421)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 94% coverage: 19:536/550 of query aligns to 9:529/533 of 6ihkB
- active site: T185 (= T191), H202 (≠ M211), H228 (= H235), S326 (≠ T329), E327 (= E330), K435 (≠ I442), W440 (≠ N447), K520 (= K527)
- binding adenosine-5'-diphosphate: H228 (= H235), G300 (= G304), A301 (≠ S305), A302 (≠ P306), H321 (= H324), A322 (≠ V325), W323 (≠ Y326), G324 (= G327), M325 (≠ I328), S326 (≠ T329), Q356 (= Q359), D414 (= D421), R429 (= R436), K520 (= K527)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 93% coverage: 25:536/550 of query aligns to 16:502/510 of 1v26B
- active site: T177 (= T191), H197 (≠ M211), H223 (= H235), T320 (= T329), E321 (= E330), K432 (≠ I442), W437 (≠ N447)
- binding adenosine monophosphate: G295 (= G304), S296 (= S305), A297 (≠ P306), G316 (≠ V325), Y317 (= Y326), G318 (= G327), L319 (≠ I328), T320 (= T329), D411 (= D421), K428 (= K438), K432 (≠ I442), W437 (≠ N447)
- binding magnesium ion: T177 (= T191), E321 (= E330)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 84% coverage: 25:484/550 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T191), H197 (≠ M211), H223 (= H235), T320 (= T329), E321 (= E330), K432 (≠ I442), W437 (≠ N447)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H235), V224 (≠ A236), G295 (= G304), S296 (= S305), A297 (≠ P306), Y317 (= Y326), G318 (= G327), L319 (≠ I328), T320 (= T329), D411 (= D421), I423 (= I433), K432 (≠ I442), W437 (≠ N447)
- binding magnesium ion: T177 (= T191), E321 (= E330)
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)
31% identity, 93% coverage: 25:536/550 of query aligns to 7:496/503 of P9WQ37
- R9 (≠ D27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D35) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K199) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A236) 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 (≠ G238) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T242) 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 (≠ G271) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G327) 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 (= W416) 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 (= D421) 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 (= R436) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S443) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G445) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K527) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
8i3iA Acyl-acp synthetase structure bound to amp-pnp
28% identity, 94% coverage: 18:535/550 of query aligns to 15:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T191), G174 (= G193), T175 (= T194), T176 (= T195), K180 (= K199), G293 (= G304), A294 (≠ S305), A295 (≠ P306), Y315 (= Y326), M317 (≠ I328), S318 (≠ T329), D408 (= D421), R423 (= R436)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
27% identity, 94% coverage: 18:535/550 of query aligns to 15:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A303), G293 (= G304), A294 (≠ S305), A295 (≠ P306), G314 (≠ V325), Y315 (= Y326), M317 (≠ I328), S318 (≠ T329), D408 (= D421), R423 (= R436)
- binding 4'-phosphopantetheine: R93 (= R103), P220 (= P232), H223 (= H235)
8i49A Acyl-acp synthetase structure bound to atp
27% identity, 94% coverage: 18:535/550 of query aligns to 15:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
27% identity, 94% coverage: 18:535/550 of query aligns to 15:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
27% identity, 94% coverage: 18:535/550 of query aligns to 13:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G304), A293 (≠ P306), G312 (≠ V325), Y313 (= Y326), G314 (= G327), M315 (≠ I328), S316 (≠ T329), D406 (= D421), R421 (= R436)
- binding magnesium ion: M315 (≠ I328), S316 (≠ T329), E317 (= E330)
8i51A Acyl-acp synthetase structure bound to amp-mc7
27% identity, 94% coverage: 18:535/550 of query aligns to 13:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G304), A293 (≠ P306), Y313 (= Y326), M315 (≠ I328), S316 (≠ T329), D406 (= D421), R421 (= R436)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W239), G290 (≠ A303), G312 (≠ V325), G314 (= G327), M315 (≠ I328), P320 (≠ T334), I321 (≠ P335)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
27% identity, 94% coverage: 18:535/550 of query aligns to 15:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A303), G293 (= G304), A295 (≠ P306), G314 (≠ V325), Y315 (= Y326), G316 (= G327), M317 (≠ I328), S318 (≠ T329), D408 (= D421), K429 (≠ I442)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H235), W227 (= W239), G292 (≠ A303), G316 (= G327), P322 (≠ T334)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R103), P220 (= P232), H223 (= H235), I269 (≠ V281), G432 (= G445)
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)
27% identity, 93% coverage: 22:535/550 of query aligns to 5:478/485 of 5x8fB
- active site: T151 (= T191), S171 (≠ M211), H195 (= H235), T288 (= T329), E289 (= E330), I387 (= I442), N392 (= N447), K470 (= K527)
- binding magnesium ion: Y23 (≠ H41), E24 (≠ G42), H70 (≠ F88), N178 (= N218), L202 (≠ T242), L214 (≠ C254), T296 (≠ S337), L297 (≠ C338), S298 (≠ V339)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (= L231), P192 (= P232), H195 (= H235), I196 (≠ A236), S197 (≠ N237), A237 (= A277), V238 (≠ A278), L260 (= L301), G262 (≠ A303), G286 (= G327), M287 (≠ I328), S292 (≠ G333), Q293 (≠ T334), S388 (= S443), G389 (= G444), G390 (= G445), E391 (= E446), K420 (≠ I475), W421 (= W476), K450 (≠ R508), Y451 (≠ F509)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
27% identity, 93% coverage: 22:535/550 of query aligns to 5:478/484 of 5gtdA
- active site: T151 (= T191), S171 (≠ M211), H195 (= H235), T288 (= T329), E289 (= E330)
- binding adenosine-5'-monophosphate: G263 (= G304), G264 (≠ S305), Y285 (= Y326), G286 (= G327), M287 (≠ I328), T288 (= T329), D366 (= D421), V378 (≠ I433)
- binding magnesium ion: F314 (≠ A364), S315 (≠ G365)
- binding 2-succinylbenzoate: H195 (= H235), S197 (≠ N237), A237 (= A277), L260 (= L301), G262 (≠ A303), G263 (= G304), G286 (= G327), M287 (≠ I328), S292 (≠ G333), Q293 (≠ T334)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 93% coverage: 25:536/550 of query aligns to 10:496/502 of 3r44A
Sites not aligning to the query:
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
27% identity, 94% coverage: 22:536/550 of query aligns to 4:472/475 of 5burA
- active site: T150 (= T191), S170 (≠ M211), H194 (= H235), T287 (= T329), E288 (= E330)
- binding adenosine-5'-triphosphate: T150 (= T191), S151 (= S192), T153 (= T194), T154 (= T195), K158 (= K199), G263 (≠ S305), S283 (≠ V325), T287 (= T329), D365 (= D421), V377 (≠ I433), R380 (= R436)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
27% identity, 94% coverage: 22:536/550 of query aligns to 4:472/481 of 5busA
- active site: T150 (= T191), S170 (≠ M211), H194 (= H235), T287 (= T329), E288 (= E330)
- binding adenosine monophosphate: H194 (= H235), G262 (= G304), G263 (≠ S305), S283 (≠ V325), M286 (≠ I328), T287 (= T329), D365 (= D421), V377 (≠ I433), R380 (= R436), K467 (= K527)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 24:536/550 of query aligns to 8:504/506 of 5ie2A
- active site: T165 (= T191), S185 (≠ M213), H209 (= H235), T310 (= T329), E311 (= E330), N410 (≠ I442), K415 (≠ N447), K495 (= K527)
- binding adenosine-5'-triphosphate: T165 (= T191), S166 (= S192), G167 (= G193), T168 (= T194), T169 (= T195), S284 (= S305), A285 (≠ P306), S286 (≠ P307), Y307 (= Y326), A308 (≠ G327), M309 (≠ I328), T310 (= T329), D389 (= D421), L401 (≠ I433), R404 (= R436), K495 (= K527)
Query Sequence
>AO356_29235 FitnessBrowser__pseudo5_N2C3_1:AO356_29235
MKPGAYENGLEQSKANYLPLTPLGFLDRAALVHPDRVAVVHGDLRRTWRQTRERCYRLAS
ALSNEGMGAGDTVSILSPNTPAMLEAHFGVPLCGAVLNTVNYRLDAEGVAFILRHGECKL
LLVDREFAALAVAALERLEHPPVVIDINDHLAPLGSSIGDVDYETFIGRGSPDFQGVWPS
DEWQPIALNYTSGTTGDPKGVVASHRGTYLMSMLQMTNWPLSRAPRYLWTLPMFHANGWC
FTWAITAAAGTHVCLRKVSAEAVFDAIDTQGVDHFCAAPIVMAMIANSADRPPLETPVRV
LTAGSPPPATVLDAVVSLGFDVDHVYGITEVSGTPISCVWQDGWNALAQSDQGALRVRQG
ARAAGFEGLMVADADTLQPVPKDGHTTGELLLKGNTVMMGYLKNENATRKAFEGGWFHTG
DVAVVHPNGYIQITDRCKDVIISGGENISSVEIEEAIHCHPAVLHAAVVAQPDDIWGEVP
CAFIELKGGAERPTEADMIAFCQARLARFKCPRRVIFMELPKTATGKIQKFLLREQAGSR
DAIVRLASSG
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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