SitesBLAST
Comparing Ac3H11_663 FitnessBrowser__acidovorax_3H11:Ac3H11_663 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)
55% identity, 99% coverage: 6:558/559 of query aligns to 5:552/561 of P69451
- Y213 (= Y213) mutation to A: Loss of activity.
- T214 (= T214) mutation to A: 10% of wild-type activity.
- G216 (= G216) mutation to A: Decreases activity.
- T217 (= T217) mutation to A: Decreases activity.
- G219 (= G219) mutation to A: Decreases activity.
- K222 (= K222) mutation to A: Decreases activity.
- E361 (= E365) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 91% coverage: 47:557/559 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H265), T303 (≠ S364), E304 (= E365), I403 (≠ L465), N408 (= N470), A491 (≠ K549)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (≠ G215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H265), S277 (≠ G338), A278 (≠ M339), P279 (≠ A340), E298 (= E359), M302 (≠ L363), T303 (≠ S364), D382 (= D444), R397 (= R459)
- binding carbonate ion: H207 (= H265), S277 (≠ G338), R299 (≠ G360), G301 (= G362)
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)
27% identity, 97% coverage: 17:558/559 of query aligns to 25:544/559 of Q67W82
- G395 (= G410) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
28% identity, 91% coverage: 47:556/559 of query aligns to 61:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ P308) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V335) mutation K->L,A: Affects the substrate specificity.
- E401 (= E411) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A413) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R459) mutation to Q: Drastically reduces the activity.
- K457 (≠ S467) mutation to S: Drastically reduces the activity.
- K540 (= K549) mutation to N: Abolishes the activity.
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)
30% identity, 91% coverage: 50:558/559 of query aligns to 30:496/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q254) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I266) 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 (= A268) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V271) 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 (≠ T303) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G362) 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 (≠ Y439) 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 (= D444) 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 (= R459) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V466) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G468) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K549) 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.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 92% coverage: 47:558/559 of query aligns to 43:528/528 of 3ni2A
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F267), S236 (≠ V271), G302 (= G338), A303 (≠ M339), P304 (≠ A340), G325 (= G360), G327 (= G362), T329 (≠ S364), P333 (= P368), V334 (≠ S369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 92% coverage: 47:558/559 of query aligns to 43:528/528 of 3a9vA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding adenosine monophosphate: H230 (= H265), G302 (= G338), A303 (≠ M339), P304 (≠ A340), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 91% coverage: 51:558/559 of query aligns to 46:527/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H265), T328 (≠ S364), E329 (= E365), K433 (≠ L465), Q438 (≠ N470), K518 (= K549)
- binding adenosine monophosphate: A301 (vs. gap), G326 (= G362), T328 (≠ S364), D412 (= D444), K429 (= K461), K433 (≠ L465), Q438 (≠ N470)
- binding coenzyme a: L102 (= L107), P226 (= P262), H229 (= H265), Y231 (≠ F267), F253 (≠ R290), K435 (≠ S467), G436 (= G468), F437 (= F469), F498 (≠ G529)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
28% identity, 91% coverage: 51:558/559 of query aligns to 47:528/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H265), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), D413 (= D444), I425 (= I456), R428 (= R459), K519 (= K549)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 91% coverage: 51:558/559 of query aligns to 47:528/529 of 5bsvA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H265), Y232 (≠ F267), S236 (≠ V271), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G360), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), V334 (≠ S369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 91% coverage: 51:558/559 of query aligns to 47:528/529 of 5bsuA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H265), Y232 (≠ F267), S236 (≠ V271), M299 (≠ V335), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G360), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 91% coverage: 51:558/559 of query aligns to 47:528/529 of 5bstA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H265), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K549)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H265), Y232 (≠ F267), S236 (≠ V271), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G360), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), V334 (≠ S369), D413 (= D444), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
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)
28% identity, 91% coverage: 51:558/559 of query aligns to 54:535/542 of O24146
- S189 (≠ T214) binding
- S190 (≠ G215) binding
- G191 (= G216) binding
- T192 (= T217) binding
- T193 (= T218) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K222) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H265) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F267) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V271) binding ; binding ; binding
- K260 (≠ P289) binding
- A309 (vs. gap) binding ; binding ; binding
- Q331 (≠ E359) binding
- G332 (= G360) binding ; binding ; binding ; binding ; binding
- T336 (≠ S364) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ S369) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ C372) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D444) binding ; binding ; binding ; binding ; binding
- R435 (= R459) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K461) binding ; binding ; binding ; binding
- K441 (≠ L465) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S467) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G468) binding
- Q446 (≠ N470) binding
- K526 (= K549) binding ; mutation to A: Abolished activity against 4-coumarate.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 91% coverage: 50:558/559 of query aligns to 33:496/502 of 3r44A
Sites not aligning to the query:
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
28% identity, 91% coverage: 51:558/559 of query aligns to 46:524/527 of 5u95B
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)
26% identity, 93% coverage: 35:555/559 of query aligns to 41:536/546 of Q84P21
- K530 (= K549) 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)
27% identity, 93% coverage: 36:556/559 of query aligns to 49:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
26% identity, 96% coverage: 19:556/559 of query aligns to 5:509/518 of 4wv3B
- active site: S175 (≠ T214), T320 (≠ S364), E321 (= E365), K418 (≠ L465), W423 (≠ N470), K502 (= K549)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H265), T221 (≠ I266), F222 (= F267), A293 (≠ G337), S294 (≠ G338), E295 (≠ M339), A296 (= A340), G316 (= G360), I317 (≠ Y361), G318 (= G362), C319 (≠ L363), T320 (≠ S364), D397 (= D444), H409 (≠ I456), R412 (= R459), K502 (= K549)
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 95% coverage: 25:553/559 of query aligns to 5:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 214:218) binding
- H214 (= H265) binding ; mutation to A: Abolished activity.
- S289 (≠ G338) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 338:340) binding
- EA 310:311 (≠ EG 359:360) binding
- M314 (≠ L363) binding
- T315 (≠ S364) binding
- H319 (≠ P368) binding ; mutation to A: Abolished activity.
- D394 (= D444) binding
- R409 (= R459) binding ; mutation to A: Abolished activity.
- K500 (= K549) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 95% coverage: 25:553/559 of query aligns to 5:499/506 of 5ie2A
- active site: T165 (= T214), S185 (≠ E239), H209 (= H265), T310 (≠ S364), E311 (= E365), N410 (≠ L465), K415 (≠ N470), K495 (= K549)
- binding adenosine-5'-triphosphate: T165 (= T214), S166 (≠ G215), G167 (= G216), T168 (= T217), T169 (= T218), S284 (≠ G338), A285 (≠ M339), S286 (≠ A340), Y307 (= Y361), A308 (≠ G362), M309 (≠ L363), T310 (≠ S364), D389 (= D444), L401 (≠ I456), R404 (= R459), K495 (= K549)
Query Sequence
>Ac3H11_663 FitnessBrowser__acidovorax_3H11:Ac3H11_663
MTDRPWLAAYPQGVPADIDTSQYTSLVALMDEAFKKYADRVAYSFMGKEVTYGQTDSLSS
AFAAYLQSLGLVKGDRVAIMMPNVPQYPVAVAAVLRAGFVVVNVNPLYTPRELEHQLKDS
GAKAIVIIENFAATLEQCIAHTPVKHVVLCAMGDQLGLLKGALVNYVVRNVKKMVPAYNL
PGAVRFNQAVAQGTRSTLKKPDIKPDDIALLQYTGGTTGVSKGAVLLHRNILANVLQSEA
WNSPVMSKVPAGEQPTAVCALPLYHIFAFTVNMMLSMRTGGKTILIPNPRDLPAVLKELS
KHTFHSFPAVNTLFNGLANHPDFNTVNWKNLKVSVGGGMAVQGAVAKLWLEKTGCPICEG
YGLSETSPSTSCNPVTATEYTGTIGVPIPGTYMKLIDDEGREITTLGEPGEIAIKGPQVM
AGYWQRPDETAKVMTDDGYFKSGDIGIMDARGFFKIVDRKKDMVLVSGFNVYPNEVEEVV
ASCPGVLECAVVGVPDEKTGEAVKLVIVKKDPALTEAQVKEFCRRELTGYKQPKVIEFRT
ELPKTPVGKILRRELRDKK
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