SitesBLAST
Comparing AZOBR_RS09405 AZOBR_RS09405 acyl-CoA synthetase 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: 24:542/544 of query aligns to 22:535/541 of Q5SKN9
- T184 (= T191) binding
- G302 (= G307) binding
- Q322 (≠ H327) binding
- G323 (≠ L328) binding
- T327 (= T332) binding
- E328 (= E333) binding
- D418 (= D424) binding
- K435 (= K441) binding
- K439 (≠ I445) 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)
34% identity, 92% coverage: 45:542/544 of query aligns to 39:534/539 of P0DX84
- H231 (= H235) mutation to A: Retains 74% of wild-type activity.
- W235 (= W239) mutation to A: Almost completely abolishes the activity.
- G302 (≠ T305) mutation to P: Almost completely abolishes the activity.
- G303 (= G306) 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 (= 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)
34% identity, 92% coverage: 45:542/544 of query aligns to 39:534/538 of 6ijbB
- active site: T185 (= T191), H205 (≠ N211), H231 (= H235), S329 (≠ T332), E330 (= E333), K438 (≠ I445), W443 (≠ N450), A523 (≠ K531)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W239), G303 (= G306), A325 (≠ L328), W326 (≠ Y329), G327 (= G330), M328 (= M331)
- binding adenosine monophosphate: G303 (= G306), A304 (≠ G307), A305 (= A308), H324 (= H327), W326 (≠ Y329), G327 (= G330), M328 (= M331), S329 (≠ T332), Q359 (= Q362), D417 (= D424)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
38% identity, 85% coverage: 24:487/544 of query aligns to 15:464/491 of 1v25A
- active site: T177 (= T191), H197 (≠ N211), H223 (= H235), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H235), V224 (≠ C236), G295 (= G307), S296 (≠ A308), A297 (= A309), Y317 (= Y329), G318 (= G330), L319 (≠ M331), T320 (= T332), D411 (= D424), I423 (= I436), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T191), E321 (= E333)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
38% identity, 85% coverage: 24:485/544 of query aligns to 15:463/510 of 1v26B
- active site: T177 (= T191), H197 (≠ N211), H223 (= H235), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding adenosine monophosphate: G295 (= G307), S296 (≠ A308), A297 (= A309), G316 (≠ L328), Y317 (= Y329), G318 (= G330), L319 (≠ M331), T320 (= T332), D411 (= D424), K428 (= K441), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T191), E321 (= E333)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
33% identity, 92% coverage: 45:542/544 of query aligns to 39:531/533 of 6ihkB
- active site: T185 (= T191), H202 (≠ N211), H228 (= H235), S326 (≠ T332), E327 (= E333), K435 (≠ I445), W440 (≠ N450), K520 (= K531)
- binding adenosine-5'-diphosphate: H228 (= H235), G300 (= G306), A301 (≠ G307), A302 (= A308), H321 (= H327), A322 (≠ L328), W323 (≠ Y329), G324 (= G330), M325 (= M331), S326 (≠ T332), Q356 (= Q362), D414 (= D424), R429 (= R439), K520 (= K531)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
30% identity, 94% coverage: 26:539/544 of query aligns to 15:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (≠ S192), G174 (≠ T194), T175 (= T195), T176 (≠ G196), K180 (= K199), G293 (= G307), A294 (= A308), A295 (= A309), Y315 (= Y329), M317 (= M331), S318 (≠ T332), D408 (= D424), R423 (= R439)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
30% identity, 94% coverage: 26:539/544 of query aligns to 15:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A295 (= A309), G314 (≠ L328), Y315 (= Y329), G316 (= G330), M317 (= M331), S318 (≠ T332), D408 (= D424), K429 (≠ I445)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H235), W227 (= W239), G292 (= G306), G316 (= G330), P322 (≠ G336)
- 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 (= G448)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
30% identity, 94% coverage: 26:539/544 of query aligns to 13:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G307), A293 (= A309), G312 (≠ L328), Y313 (= Y329), G314 (= G330), M315 (= M331), S316 (≠ T332), D406 (= D424), R421 (= R439)
- binding magnesium ion: M315 (= M331), S316 (≠ T332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7
30% identity, 94% coverage: 26:539/544 of query aligns to 13:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G307), A293 (= A309), Y313 (= Y329), M315 (= M331), S316 (≠ T332), D406 (= D424), R421 (= R439)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W239), G290 (= G306), G312 (≠ L328), G314 (= G330), M315 (= M331), P320 (≠ G336), I321 (≠ P337)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
30% identity, 94% coverage: 26:539/544 of query aligns to 15:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A294 (= A308), A295 (= A309), G314 (≠ L328), Y315 (= Y329), M317 (= M331), S318 (≠ T332), D408 (= D424), R423 (= R439)
- binding 4'-phosphopantetheine: R93 (= R103), P220 (= P232), H223 (= H235)
8i49A Acyl-acp synthetase structure bound to atp
30% identity, 94% coverage: 26:539/544 of query aligns to 15:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
30% identity, 94% coverage: 26:539/544 of query aligns to 15:527/530 of 8i22A
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, 95% coverage: 25:540/544 of query aligns to 7:496/503 of P9WQ37
- R9 (= R27) 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 (= R222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C236) 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 (≠ Y241) 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 (≠ K271) 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 (= 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, 95% coverage: 25:540/544 of query aligns to 10:496/502 of 3r44A
Sites not aligning to the query:
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
29% identity, 97% coverage: 16:544/544 of query aligns to 34:554/556 of Q9S725
- K211 (= K199) mutation to S: Drastically reduces the activity.
- M293 (≠ C276) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T305) mutation K->L,A: Affects the substrate specificity.
- E401 (= E392) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A394) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R439) mutation to Q: Drastically reduces the activity.
- K457 (≠ G447) mutation to S: Drastically reduces the activity.
- K540 (= K531) mutation to N: Abolishes the activity.
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
29% identity, 97% coverage: 16:544/544 of query aligns to 23:540/542 of O24146
- S189 (≠ T191) binding
- S190 (= S192) binding
- G191 (= G193) binding
- T192 (= T194) binding
- T193 (= T195) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K199) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H235) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ N237) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ Y241) binding ; binding ; binding
- K260 (≠ A257) binding
- A309 (= A308) binding ; binding ; binding
- Q331 (≠ H327) binding
- G332 (≠ L328) binding ; binding ; binding ; binding ; binding
- T336 (= T332) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ S338) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ C341) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D424) binding ; binding ; binding ; binding ; binding
- R435 (= R439) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K441) binding ; binding ; binding ; binding
- K441 (≠ I445) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G447) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G448) binding
- Q446 (≠ N450) binding
- K526 (= K531) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 97% coverage: 16:540/544 of query aligns to 15:527/528 of 5bsrA
- active site: S181 (≠ T191), S201 (≠ N211), H229 (= H235), T328 (= T332), E329 (= E333), K433 (≠ I445), Q438 (≠ N450), K518 (= K531)
- binding adenosine monophosphate: A301 (= A308), G326 (= G330), T328 (= T332), D412 (= D424), K429 (= K441), K433 (≠ I445), Q438 (≠ N450)
- binding coenzyme a: L102 (≠ R103), P226 (= P232), H229 (= H235), Y231 (≠ N237), F253 (≠ V258), K435 (≠ G447), G436 (= G448), F437 (≠ E449), F498 (≠ H512)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 97% coverage: 16:540/544 of query aligns to 16:528/529 of 5bsvA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H235), T329 (= T332), E330 (= E333), K434 (≠ I445), Q439 (≠ N450), K519 (= K531)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H235), Y232 (≠ N237), S236 (≠ Y241), A302 (= A308), A303 (= A309), P304 (= P310), G325 (≠ L328), G327 (= G330), M328 (= M331), T329 (= T332), P333 (= P337), V334 (≠ S338), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 97% coverage: 16:540/544 of query aligns to 16:528/529 of 5bsuA
- active site: S182 (≠ T191), S202 (≠ N211), H230 (= H235), T329 (= T332), E330 (= E333), K434 (≠ I445), Q439 (≠ N450), K519 (= K531)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H235), Y232 (≠ N237), S236 (≠ Y241), M299 (≠ T305), A302 (= A308), A303 (= A309), P304 (= P310), G325 (≠ L328), G327 (= G330), M328 (= M331), T329 (= T332), P333 (= P337), D413 (= D424), K430 (= K441), K434 (≠ I445), Q439 (≠ N450)
Query Sequence
>AZOBR_RS09405 AZOBR_RS09405 acyl-CoA synthetase
VDATTPSAELSRRTANHVPLTPLDFLRRSAMVYPDKTAVVYGPLRRSWLEVEHRARALAS
AVSRAGVRPGEVVSVLAFNTPAMLEAHFGVPGAGAVLNAINTRLDPPAVAFILEHAESRL
FLVDRGLSAVARAALERMTAPPRVVWIDDPAAQDADPVGDLEYEDFLKTGDPEAPWRRPE
DEWESIALNYTSGTTGNPKGVLYHHRGAHLNALGNVITFGLRPDSVYLWTLPMFHCNGWT
YPWAVTAVGATHVCLRAVDPAAIFRLIAEEKVTHLCGAPVVLTMLIHAPDAVKRAFDHGP
VQVATGGAAPPSAVIAGMERMGFRLTHLYGMTECYGPSTGCAWQEAWAELPLEERAVKMA
RQGVPNVTMSEQTVLDPDTGREVPADGETLGELALRGNTVMKGYLKNPAATDEALRDGWL
HTGDLAVLHPDRYVEIKDRAKDIIISGGENIASLEVEEVLYKHPHVMEAAVVARPDAKWG
ETPCAFVTLKPGSEGRVSEAEVIGWCRDHLAHFKTPRTVVFGALPKTSTGKIQKFVLREQ
ARGL
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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