SitesBLAST
Comparing Ac3H11_4250 FitnessBrowser__acidovorax_3H11:Ac3H11_4250 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)
47% identity, 99% coverage: 6:546/546 of query aligns to 5:553/561 of P69451
- Y213 (= Y202) mutation to A: Loss of activity.
- T214 (= T203) mutation to A: 10% of wild-type activity.
- G216 (= G205) mutation to A: Decreases activity.
- T217 (= T206) mutation to A: Decreases activity.
- G219 (= G208) mutation to A: Decreases activity.
- K222 (= K211) mutation to A: Decreases activity.
- E361 (= E350) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 92% coverage: 43:544/546 of query aligns to 23:499/506 of 4gxqA
- active site: T163 (= T203), N183 (= N223), H207 (= H250), T303 (≠ S349), E304 (= E350), I403 (= I449), N408 (= N454), A491 (≠ K536)
- binding adenosine-5'-triphosphate: T163 (= T203), S164 (≠ G204), G165 (= G205), T166 (= T206), T167 (= T207), H207 (= H250), S277 (≠ G323), A278 (= A324), P279 (≠ A325), E298 (= E344), M302 (≠ L348), T303 (≠ S349), D382 (= D428), R397 (= R443)
- binding carbonate ion: H207 (= H250), S277 (≠ G323), R299 (≠ G345), G301 (= G347)
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, 94% coverage: 33:543/546 of query aligns to 46:547/556 of Q9S725
- K211 (= K211) mutation to S: Drastically reduces the activity.
- M293 (= M293) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ G320) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R443) mutation to Q: Drastically reduces the activity.
- K457 (≠ S451) mutation to S: Drastically reduces the activity.
- K540 (= K536) mutation to N: Abolishes the activity.
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, 95% coverage: 23:543/546 of query aligns to 29:542/559 of Q67W82
- G395 (= G394) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 96% coverage: 19:544/546 of query aligns to 10:527/528 of 3ni2A
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F252), S236 (≠ V256), G302 (= G323), A303 (= A324), P304 (vs. gap), G325 (= G345), G327 (= G347), T329 (≠ S349), P333 (= P353), V334 (= V354), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 96% coverage: 19:544/546 of query aligns to 10:527/528 of 3a9vA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding adenosine monophosphate: H230 (= H250), G302 (= G323), A303 (= A324), P304 (vs. gap), Y326 (= Y346), G327 (= G347), M328 (≠ L348), T329 (≠ S349), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
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, 95% coverage: 26:543/546 of query aligns to 27:533/542 of O24146
- S189 (≠ T203) binding
- S190 (≠ G204) binding
- G191 (= G205) binding
- T192 (= T206) binding
- T193 (= T207) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K211) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H250) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F252) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V256) binding ; binding ; binding
- K260 (≠ P274) binding
- A309 (vs. gap) binding ; binding ; binding
- Q331 (= Q340) binding
- G332 (= G345) binding ; binding ; binding ; binding ; binding
- T336 (≠ S349) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V354) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D428) binding ; binding ; binding ; binding ; binding
- R435 (= R443) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K445) binding ; binding ; binding ; binding
- K441 (≠ I449) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S451) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G452) binding
- Q446 (≠ N454) binding
- K526 (= K536) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 95% coverage: 26:543/546 of query aligns to 20:526/530 of 5bsmA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding adenosine-5'-triphosphate: S182 (≠ T203), S183 (≠ G204), G184 (= G205), T185 (= T206), T186 (= T207), K190 (= K211), H230 (= H250), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), Y326 (= Y346), G327 (= G347), M328 (≠ L348), T329 (≠ S349), D413 (= D428), I425 (= I440), R428 (= R443), K519 (= K536)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 95% coverage: 26:543/546 of query aligns to 20:526/529 of 5bsvA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H250), Y232 (≠ F252), S236 (≠ V256), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G345), G327 (= G347), M328 (≠ L348), T329 (≠ S349), P333 (= P353), V334 (= V354), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 95% coverage: 26:543/546 of query aligns to 20:526/529 of 5bsuA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H250), Y232 (≠ F252), S236 (≠ V256), M299 (≠ G320), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G345), G327 (= G347), M328 (≠ L348), T329 (≠ S349), P333 (= P353), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 95% coverage: 26:543/546 of query aligns to 20:526/529 of 5bstA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H250), T329 (≠ S349), E330 (= E350), K434 (≠ I449), Q439 (≠ N454), K519 (= K536)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H250), Y232 (≠ F252), S236 (≠ V256), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G345), Y326 (= Y346), G327 (= G347), M328 (≠ L348), T329 (≠ S349), P333 (= P353), V334 (= V354), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 95% coverage: 26:543/546 of query aligns to 19:525/528 of 5bsrA
- active site: S181 (≠ T203), S201 (≠ N223), H229 (= H250), T328 (≠ S349), E329 (= E350), K433 (≠ I449), Q438 (≠ N454), K518 (= K536)
- binding adenosine monophosphate: A301 (vs. gap), G326 (= G347), T328 (≠ S349), D412 (= D428), K429 (= K445), K433 (≠ I449), Q438 (≠ N454)
- binding coenzyme a: L102 (= L107), P226 (= P247), H229 (= H250), Y231 (≠ F252), F253 (≠ R275), K435 (≠ S451), G436 (= G452), F437 (= F453), F498 (≠ A516)
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)
28% identity, 92% coverage: 42:546/546 of query aligns to 58:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 95% coverage: 26:543/546 of query aligns to 19:522/527 of 5u95B
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)
31% identity, 91% coverage: 50:544/546 of query aligns to 49:532/541 of Q5SKN9
- T184 (= T203) binding
- G302 (= G323) binding
- Q322 (≠ E344) binding
- G323 (= G345) binding
- T327 (≠ S349) binding
- E328 (= E350) binding
- D418 (= D428) binding
- K435 (= K445) binding
- K439 (≠ I449) binding
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, 91% coverage: 49:544/546 of query aligns to 30:495/503 of P9WQ37
- K172 (= K211) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ A234) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R236) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I251) 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 (= A253) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V256) 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 (= R288) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G347) 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 (≠ Y423) 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 (= D428) 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 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K536) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 91% coverage: 49:544/546 of query aligns to 33:495/502 of 3r44A
Sites not aligning to the query:
4rm2A Crystal structure of a benzoate coenzyme a ligase with 2-fluoro benzoic acid (see paper)
30% identity, 96% coverage: 19:544/546 of query aligns to 5:515/516 of 4rm2A
- active site: S176 (≠ T203), T196 (≠ N223), T324 (≠ S349), E325 (= E350), K422 (≠ I449), Y427 (≠ N454), K507 (= K536)
- binding 2-fluorobenzoic acid: A216 (= A245), A222 (≠ I251), Y223 (≠ F252), P246 (≠ R275), T247 (≠ D276), V251 (≠ L280), F267 (= F292), G269 (= G294), A270 (≠ V295), G273 (≠ L298), M277 (≠ L302), A297 (≠ G322), G298 (= G323), I321 (≠ Y346), G322 (= G347), S323 (≠ L348), H328 (≠ P353), K422 (≠ I449)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
30% identity, 96% coverage: 19:544/546 of query aligns to 6:516/518 of 4rm3A
- active site: S177 (≠ T203), T197 (≠ N223), T325 (≠ S349), E326 (= E350), K423 (≠ I449), Y428 (≠ N454), K508 (= K536)
- binding 2-furoic acid: A223 (≠ I251), Y224 (≠ F252), A298 (≠ G322), G323 (= G347), H329 (≠ P353), I330 (≠ V354), K423 (≠ I449)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
30% identity, 96% coverage: 19:544/546 of query aligns to 5:515/518 of 4rmnA
- active site: S176 (≠ T203), T196 (≠ N223), T324 (≠ S349), E325 (= E350), K422 (≠ I449), Y427 (≠ N454), K507 (= K536)
- binding thiophene-2-carboxylic acid: A217 (≠ I246), F221 (≠ H250), Y223 (≠ F252), G269 (= G294), A270 (≠ V295), A297 (≠ G322), G298 (= G323), G322 (= G347), S323 (≠ L348), H328 (≠ P353), I329 (≠ V354), K422 (≠ I449), G425 (= G452)
Query Sequence
>Ac3H11_4250 FitnessBrowser__acidovorax_3H11:Ac3H11_4250
MSPQPWLASYGAIPAHIDPDSHPSVVHLLCAAMQRYAHRPAFTCLGQTLTYAHVDQQSRA
FAAYLQNVLRVRKGDRIAVMCPNLVAFPIAMLGIARAGCVQVNVNPLYTPRELEHQLLDA
GVRVMVVYAGSTATLAAIQDRVELHSIITVAPGDGTAADLPGPPVDAHLHTTTSFARALA
EGATLPFAPPVLEGGDLLFLQYTGGTTGLSKGAMLTHRNLVANVEQFKAFVPDALRPAQE
VIVTAIPLYHIFALMVNLISYFAVGARNWLVPNPRDLDALIHVLNAARPSVFMGVNTLYA
GLAAHPGTQGVDFSNLRLAGGGGAAILSSVSARWQAITGQFIREGYGLSETSPVVAFNPA
SVTAFSGSTGLPLPSTDVLLLDDQGHPVPLGQPGEVCVKGPQVMGGYWQQPEANAVAFTP
DGYFRTGDIGQLDERGFLKIVDRKKDMVIVSGFNVFPNEIEAVATACPGVLECACIGVSD
DKTGEALRLYVVRAAGTAPPVDADQIAAHCRAALTAYKVPRQIVFLEALPKSSVGKILRR
ELRDMA
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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