SitesBLAST
Comparing BWI76_RS17800 BWI76_RS17800 long-chain-fatty-acid--CoA ligase 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)
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)
94% identity, 98% coverage: 12:572/572 of query aligns to 1:561/561 of P69451
- Y213 (= Y224) mutation to A: Loss of activity.
- T214 (= T225) mutation to A: 10% of wild-type activity.
- G216 (= G227) mutation to A: Decreases activity.
- T217 (= T228) mutation to A: Decreases activity.
- G219 (= G230) mutation to A: Decreases activity.
- K222 (= K233) mutation to A: Decreases activity.
- E361 (= E372) mutation to A: Loss of activity.
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)
31% identity, 91% coverage: 39:561/572 of query aligns to 42:547/556 of Q9S725
- K211 (= K233) mutation to S: Drastically reduces the activity.
- M293 (≠ T315) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ A342) mutation K->L,A: Affects the substrate specificity.
- E401 (= E417) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C419) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R464) mutation to Q: Drastically reduces the activity.
- K457 (≠ S472) mutation to S: Drastically reduces the activity.
- K540 (= K554) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 91% coverage: 44:563/572 of query aligns to 28:528/528 of 3ni2A
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F274), S236 (≠ M278), G302 (= G345), A303 (≠ M346), P304 (= P347), G325 (= G367), G327 (= G369), T329 (= T371), P333 (= P375), V334 (≠ L376), D413 (= D449), K430 (= K466), K434 (≠ L470), Q439 (≠ N475)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 91% coverage: 44:563/572 of query aligns to 28:528/528 of 3a9vA
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding adenosine monophosphate: H230 (= H272), G302 (= G345), A303 (≠ M346), P304 (= P347), Y326 (= Y368), G327 (= G369), M328 (≠ L370), T329 (= T371), D413 (= D449), K430 (= K466), K434 (≠ L470), Q439 (≠ N475)
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)
31% identity, 93% coverage: 40:570/572 of query aligns to 32:542/542 of O24146
- S189 (≠ T225) binding
- S190 (≠ G226) binding
- G191 (= G227) binding
- T192 (= T228) binding
- T193 (= T229) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K233) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H272) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F274) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ M278) binding ; binding ; binding
- K260 (≠ P296) binding
- A309 (≠ G345) binding ; binding ; binding
- Q331 (≠ E366) binding
- G332 (= G367) binding ; binding ; binding ; binding ; binding
- T336 (= T371) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L376) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ V379) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D449) binding ; binding ; binding ; binding ; binding
- R435 (= R464) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K466) binding ; binding ; binding ; binding
- K441 (≠ L470) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S472) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G473) binding
- Q446 (≠ N475) binding
- K526 (= K554) 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)
31% identity, 91% coverage: 40:561/572 of query aligns to 24:525/528 of 5bsrA
- active site: S181 (≠ T225), S201 (≠ N245), H229 (= H272), T328 (= T371), E329 (= E372), K433 (≠ L470), Q438 (≠ N475), K518 (= K554)
- binding adenosine monophosphate: A301 (≠ G345), G326 (= G369), T328 (= T371), D412 (= D449), K429 (= K466), K433 (≠ L470), Q438 (≠ N475)
- binding coenzyme a: L102 (= L118), P226 (= P269), H229 (= H272), Y231 (≠ F274), F253 (≠ R297), K435 (≠ S472), G436 (= G473), F437 (= F474), F498 (≠ G534)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 91% coverage: 40:561/572 of query aligns to 25:526/530 of 5bsmA
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding adenosine-5'-triphosphate: S182 (≠ T225), S183 (≠ G226), G184 (= G227), T185 (= T228), T186 (= T229), K190 (= K233), H230 (= H272), A302 (≠ G345), A303 (≠ M346), P304 (= P347), Y326 (= Y368), G327 (= G369), M328 (≠ L370), T329 (= T371), D413 (= D449), I425 (= I461), R428 (= R464), K519 (= K554)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 91% coverage: 40:561/572 of query aligns to 25:526/529 of 5bsvA
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H272), Y232 (≠ F274), S236 (≠ M278), A302 (≠ G345), A303 (≠ M346), P304 (= P347), G325 (= G367), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (= P375), V334 (≠ L376), D413 (= D449), K430 (= K466), K434 (≠ L470), Q439 (≠ N475)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 91% coverage: 40:561/572 of query aligns to 25:526/529 of 5bsuA
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H272), Y232 (≠ F274), S236 (≠ M278), M299 (≠ A342), A302 (≠ G345), A303 (≠ M346), P304 (= P347), G325 (= G367), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (= P375), D413 (= D449), K430 (= K466), K434 (≠ L470), Q439 (≠ N475)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 91% coverage: 40:561/572 of query aligns to 25:526/529 of 5bstA
- active site: S182 (≠ T225), S202 (≠ N245), H230 (= H272), T329 (= T371), E330 (= E372), K434 (≠ L470), Q439 (≠ N475), K519 (= K554)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H272), Y232 (≠ F274), S236 (≠ M278), A302 (≠ G345), A303 (≠ M346), P304 (= P347), G325 (= G367), Y326 (= Y368), G327 (= G369), M328 (≠ L370), T329 (= T371), P333 (= P375), V334 (≠ L376), D413 (= D449), K430 (= K466), K434 (≠ L470), Q439 (≠ N475)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 92% coverage: 40:566/572 of query aligns to 24:527/527 of 5u95B
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
30% identity, 91% coverage: 48:568/572 of query aligns to 46:549/559 of Q67W82
- G395 (= G416) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 89% coverage: 52:560/572 of query aligns to 48:536/546 of Q84P21
- K530 (= K554) mutation to N: Lossed enzymatic activity.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
29% identity, 94% coverage: 35:571/572 of query aligns to 38:580/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 92% coverage: 38:561/572 of query aligns to 22:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H272), F245 (= F274), T249 (≠ I284), G314 (= G345), A315 (≠ M346), P316 (= P347), G337 (= G367), Y338 (= Y368), G339 (= G369), L340 (= L370), T341 (= T371), S345 (≠ P375), A346 (≠ L376), D420 (= D449), I432 (= I461), K527 (= K554)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F274), R335 (≠ L365), G337 (= G367), G339 (= G369), L340 (= L370), A346 (≠ L376)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 92% coverage: 38:561/572 of query aligns to 22:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H272), F245 (= F274), T249 (≠ I284), G314 (= G345), A315 (≠ M346), P316 (= P347), G337 (= G367), Y338 (= Y368), G339 (= G369), L340 (= L370), T341 (= T371), A346 (≠ L376), D420 (= D449), I432 (= I461), K527 (= K554)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 88% coverage: 57:562/572 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T225), N183 (= N245), H207 (= H272), T303 (= T371), E304 (= E372), I403 (≠ L470), N408 (= N475), A491 (≠ K554)
- binding adenosine-5'-triphosphate: T163 (= T225), S164 (≠ G226), G165 (= G227), T166 (= T228), T167 (= T229), H207 (= H272), S277 (≠ G345), A278 (≠ M346), P279 (= P347), E298 (= E366), M302 (≠ L370), T303 (= T371), D382 (= D449), R397 (= R464)
- binding carbonate ion: H207 (= H272), S277 (≠ G345), R299 (≠ G367), G301 (= G369)
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, 89% coverage: 60:568/572 of query aligns to 30:501/503 of P9WQ37
- K172 (= K233) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R259) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K261) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I273) 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 (= A275) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M278) 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 (≠ P310) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G369) 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 (= W444) 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 (= D449) 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 (= R464) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V471) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G473) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K554) 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.
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
29% identity, 94% coverage: 25:562/572 of query aligns to 10:536/544 of 6q2mA
- active site: S197 (≠ T225), R217 (≠ N245), H244 (= H272), T342 (= T371), E343 (= E372), K442 (≠ L470), Q447 (≠ N475), K528 (= K554)
- binding (2S,5S)-hexane-2,5-diol: D18 (≠ Y33), G19 (≠ Q34), D186 (≠ P216), R187 (≠ Q217), R260 (≠ Q289), Y279 (= Y309)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (≠ G226), H244 (= H272), F246 (= F274), T250 (≠ N279), G315 (= G345), A316 (≠ M346), P317 (= P347), G338 (= G367), Y339 (= Y368), G340 (= G369), L341 (= L370), T342 (= T371), S346 (≠ P375), A347 (≠ L376), D421 (= D449), K528 (= K554)
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 92% coverage: 35:558/572 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T225), S183 (≠ N245), H207 (= H272), T308 (= T371), E309 (= E372), N408 (≠ L470), K413 (≠ N475), K493 (= K554)
- binding adenosine monophosphate: S164 (≠ G226), S282 (≠ G345), A283 (≠ M346), S284 (≠ P347), Y305 (= Y368), A306 (≠ G369), M307 (≠ L370), T308 (= T371), D387 (= D449), L399 (≠ I461), R402 (= R464), K493 (= K554)
- binding oxalic acid: V208 (≠ I273), S282 (≠ G345), A306 (≠ G369), M307 (≠ L370), H312 (≠ P375), K493 (= K554)
Query Sequence
>BWI76_RS17800 BWI76_RS17800 long-chain-fatty-acid--CoA ligase
MTTNNYFRGDAVKKVWLNRYPADVPAEINPDRYQSLVELFEHAVRRYADQPAFINMGEVM
TYRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYT
PRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSPAKGTVVNFVVK
YIKRLVPKYHLPDAISFRSALQHGYRMQYIKPEIVPQDLAFLQYTGGTTGVAKGAMLTHR
NMLANLEQVNGTYGPLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIP
GLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLT
GQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGEPGELCV
KGPQVMLGYWQRPDATAEIIKDGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE
IEDVVMQHAGVQEVAAVGVPSGSSGEAVKIFVVKKDPTLTEEMLITFCRRQLTGYKVPKH
VEFRDELPKSNVGKILRRELRDEARAKVDNKA
Or try a new SitesBLAST search
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