SitesBLAST
Comparing H281DRAFT_05558 H281DRAFT_05558 fatty-acyl-CoA synthase 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, 94% coverage: 26:541/550 of query aligns to 23:536/541 of Q5SKN9
- T184 (= T192) binding
- G302 (= G307) binding
- Q322 (≠ H327) binding
- G323 (≠ I328) binding
- T327 (= T332) binding
- E328 (= E333) binding
- D418 (= D424) binding
- K435 (= K441) binding
- K439 (≠ I445) binding
8i3iA Acyl-acp synthetase structure bound to amp-pnp
30% identity, 97% coverage: 7:538/550 of query aligns to 3:520/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T192), G174 (= G194), T175 (= T195), T176 (= T196), K180 (= K200), G293 (= G307), A294 (= A308), A295 (≠ P309), Y315 (= Y329), M317 (≠ L331), S318 (≠ T332), D408 (= D424), R423 (= R439)
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, 90% coverage: 46:542/550 of query aligns to 39:536/539 of P0DX84
- H231 (= H236) mutation to A: Retains 74% of wild-type activity.
- W235 (= W240) mutation to A: Almost completely abolishes the activity.
- G302 (= G306) mutation to P: Almost completely abolishes the activity.
- G303 (= G307) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y329) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G336) mutation to A: Retains 69% of wild-type activity.
- R432 (= R439) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K441) mutation to A: Retains 36% of wild-type activity.
- D435 (= D442) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I445) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G447) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G448) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E449) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N450) mutation to A: Retains 60% of wild-type activity.
- E474 (= E481) mutation to A: Retains 33% of wild-type activity.
- K523 (= K529) 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 (= K532) mutation to A: Retains 48% of wild-type activity.
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 94% coverage: 26:541/550 of query aligns to 16:505/510 of 1v26B
- active site: T177 (= T192), H197 (≠ S212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding adenosine monophosphate: G295 (= G307), S296 (≠ A308), A297 (≠ P309), G316 (≠ I328), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D424), K428 (= K441), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T192), E321 (= E333)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
30% identity, 97% coverage: 7:538/550 of query aligns to 3:528/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A294 (= A308), A295 (≠ P309), G314 (≠ I328), Y315 (= Y329), M317 (≠ L331), S318 (≠ T332), D408 (= D424), R423 (= R439)
- binding 4'-phosphopantetheine: R93 (= R104), P220 (= P233), H223 (= H236)
8i49A Acyl-acp synthetase structure bound to atp
30% identity, 97% coverage: 7:538/550 of query aligns to 3:528/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
30% identity, 97% coverage: 7:538/550 of query aligns to 3:528/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
30% identity, 97% coverage: 7:538/550 of query aligns to 1:526/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G307), A293 (≠ P309), G312 (≠ I328), Y313 (= Y329), G314 (= G330), M315 (≠ L331), S316 (≠ T332), D406 (= D424), R421 (= R439)
- binding magnesium ion: M315 (≠ L331), S316 (≠ T332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7
30% identity, 97% coverage: 7:538/550 of query aligns to 1:526/528 of 8i51A
- binding adenosine monophosphate: G291 (= G307), A293 (≠ P309), Y313 (= Y329), M315 (≠ L331), S316 (≠ T332), D406 (= D424), R421 (= R439)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W240), G290 (= G306), G312 (≠ I328), G314 (= G330), M315 (≠ L331), P320 (≠ G336), I321 (≠ P337)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
30% identity, 97% coverage: 7:538/550 of query aligns to 3:528/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A295 (≠ P309), G314 (≠ I328), Y315 (= Y329), G316 (= G330), M317 (≠ L331), S318 (≠ T332), D408 (= D424), K429 (≠ I445)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H236), W227 (= W240), G292 (= G306), G316 (= G330), P322 (≠ G336)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R104), P220 (= P233), H223 (= H236), I269 (= I281), G432 (= G448)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
32% identity, 90% coverage: 46:542/550 of query aligns to 39:536/538 of 6ijbB
- active site: T185 (= T192), H205 (≠ S212), H231 (= H236), S329 (≠ T332), E330 (= E333), K438 (≠ I445), W443 (≠ N450), A523 (≠ K529)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W240), G303 (= G307), A325 (≠ I328), W326 (≠ Y329), G327 (= G330), M328 (≠ L331)
- binding adenosine monophosphate: G303 (= G307), A304 (= A308), A305 (≠ P309), H324 (= H327), W326 (≠ Y329), G327 (= G330), M328 (≠ L331), S329 (≠ T332), Q359 (= Q362), D417 (= D424)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 84% coverage: 26:487/550 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T192), H197 (≠ S212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H236), V224 (≠ C237), G295 (= G307), S296 (≠ A308), A297 (≠ P309), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D424), I423 (= I436), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T192), E321 (= E333)
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)
33% identity, 89% coverage: 46:537/550 of query aligns to 29:495/503 of P9WQ37
- K172 (= K200) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P223) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C237) 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 (≠ G239) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M242) 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 (= R272) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G330) 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 (= W419) 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 (= D424) 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 (= R439) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S446) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G448) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K529) 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.
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 90% coverage: 46:542/550 of query aligns to 39:533/533 of 6ihkB
- active site: T185 (= T192), H202 (≠ S212), H228 (= H236), S326 (≠ T332), E327 (= E333), K435 (≠ I445), W440 (≠ N450), K520 (= K529)
- binding adenosine-5'-diphosphate: H228 (= H236), G300 (= G307), A301 (= A308), A302 (≠ P309), H321 (= H327), A322 (≠ I328), W323 (≠ Y329), G324 (= G330), M325 (≠ L331), S326 (≠ T332), Q356 (= Q362), D414 (= D424), R429 (= R439), K520 (= K529)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 89% coverage: 46:537/550 of query aligns to 32:495/502 of 3r44A
Sites not aligning to the query:
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)
28% identity, 94% coverage: 23:537/550 of query aligns to 5:478/485 of 5x8fB
- active site: T151 (= T192), S171 (= S212), H195 (= H236), T288 (= T332), E289 (= E333), I387 (= I445), N392 (= N450), K470 (= K529)
- binding magnesium ion: Y23 (= Y42), E24 (≠ G43), H70 (≠ F89), N178 (≠ S219), L202 (≠ P243), L214 (≠ C255), T296 (≠ I340), L297 (≠ C341), S298 (≠ E342)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R104), L191 (= L232), P192 (= P233), H195 (= H236), I196 (≠ C237), S197 (≠ N238), A237 (≠ G278), V238 (= V282), L260 (= L304), G262 (= G306), G286 (= G330), M287 (≠ L331), S292 (≠ G336), Q293 (≠ P337), S388 (= S446), G389 (= G447), G390 (= G448), E391 (= E449), K420 (= K478), W421 (= W479), K450 (≠ H510), Y451 (≠ F511)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 94% coverage: 23:537/550 of query aligns to 5:478/484 of 5gtdA
- active site: T151 (= T192), S171 (= S212), H195 (= H236), T288 (= T332), E289 (= E333)
- binding adenosine-5'-monophosphate: G263 (= G307), G264 (≠ A308), Y285 (= Y329), G286 (= G330), M287 (≠ L331), T288 (= T332), D366 (= D424), V378 (≠ I436)
- binding magnesium ion: F314 (≠ M375), S315 (≠ N376)
- binding 2-succinylbenzoate: H195 (= H236), S197 (≠ N238), A237 (≠ G278), L260 (= L304), G262 (= G306), G263 (= G307), G286 (= G330), M287 (≠ L331), S292 (≠ G336), Q293 (≠ P337)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
28% identity, 94% coverage: 23:537/550 of query aligns to 4:475/475 of 5burA
- active site: T150 (= T192), S170 (= S212), H194 (= H236), T287 (= T332), E288 (= E333)
- binding adenosine-5'-triphosphate: T150 (= T192), S151 (= S193), T153 (= T195), T154 (= T196), K158 (= K200), G263 (≠ A308), S283 (≠ I328), T287 (= T332), D365 (= D424), V377 (≠ I436), R380 (= R439)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
28% identity, 94% coverage: 23:537/550 of query aligns to 4:475/481 of 5busA
- active site: T150 (= T192), S170 (= S212), H194 (= H236), T287 (= T332), E288 (= E333)
- binding adenosine monophosphate: H194 (= H236), G262 (= G307), G263 (≠ A308), S283 (≠ I328), M286 (≠ L331), T287 (= T332), D365 (= D424), V377 (≠ I436), R380 (= R439), K467 (= K529)
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
27% identity, 94% coverage: 23:537/550 of query aligns to 4:466/473 of 5buqB
Query Sequence
>H281DRAFT_05558 H281DRAFT_05558 fatty-acyl-CoA synthase
MQTSRWNDPGLRPRAANFDALTPVTFLQRAEKVFPDRTAVVYGSHRETWREHAATCRRFA
SALARAGIEYGDVVALLMTNTPPMLAAHFAVPMAGAVLNTINTRLDAENVSYILGHSEAR
LIIVDAEFLELARTAVARLQHPPRLVCFADEQAAFAASSDVEDYVSFLASGDENASFCKV
EEEWTPIAVNYTSGTTGRPKGVVYSHRGAYLSAVSSIISWGVPKAASYLWTLPLFHCNGW
CMPWVLALQGGKSVCLRRVDGDKIVQLINDERVTHYCGAPIVHALIRDRAQQQDLVFNPA
VSALIGGAPPPASLIAAMDAIGVQLTHIYGLTETYGPAAICEQQPAWAELGEAERADRKA
RQGVNYALQAGMTVMNCNSSDEVSADGAMMGEIVFRGNMTMMGYLKDSESTDRAFDGGWF
RSGDLAVLEPDGYVRIKDRSKDIIISGGENISSVEVEDVLYRHETVAAAAVVAMPDEKWG
EVPVAIVELREGSHASEDALIAHCREQLAHFKCPKRVIFHPIPKTATGKIQKNVLREIIR
NSKVSPTTTG
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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