SitesBLAST
Comparing Pf6N2E2_1879 Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) 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)
32% identity, 98% coverage: 3:504/511 of query aligns to 23:550/561 of P69451
- Y213 (= Y168) mutation to A: Loss of activity.
- T214 (= T169) mutation to A: 10% of wild-type activity.
- G216 (= G171) mutation to A: Decreases activity.
- T217 (= T172) mutation to A: Decreases activity.
- G219 (= G174) mutation to A: Decreases activity.
- K222 (= K177) mutation to A: Decreases activity.
- E361 (= E311) mutation to A: Loss of activity.
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)
31% identity, 95% coverage: 26:509/511 of query aligns to 55:542/546 of Q84P21
- K530 (= K497) mutation to N: Lossed enzymatic activity.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 99% coverage: 7:511/511 of query aligns to 6:484/484 of 5gtdA
- active site: T151 (= T169), S171 (≠ T188), H195 (= H213), T288 (= T310), E289 (= E311)
- binding adenosine-5'-monophosphate: G263 (= G284), G264 (≠ Q285), Y285 (≠ W307), G286 (= G308), M287 (= M309), T288 (= T310), D366 (= D391), V378 (≠ I403)
- binding magnesium ion: F314 (≠ P335), S315 (≠ H336)
- binding 2-succinylbenzoate: H195 (= H213), S197 (≠ Y215), A237 (≠ G255), L260 (≠ V282), G262 (= G283), G263 (= G284), G286 (= G308), M287 (= M309), S292 (≠ G313), Q293 (≠ G314)
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)
31% identity, 99% coverage: 7:511/511 of query aligns to 6:484/485 of 5x8fB
- active site: T151 (= T169), S171 (≠ T188), H195 (= H213), T288 (= T310), E289 (= E311), I387 (= I412), N392 (= N417), K470 (= K497)
- binding magnesium ion: Y23 (≠ F24), E24 (= E25), H70 (≠ Y71), N178 (≠ T195), L202 (≠ M220), L214 (= L232), T296 (= T317), L297 (≠ T318), S298 (≠ H319)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ M86), L191 (= L209), P192 (= P210), H195 (= H213), I196 (≠ V214), S197 (≠ Y215), A237 (≠ G255), V238 (= V256), L260 (≠ V282), G262 (= G283), G286 (= G308), M287 (= M309), S292 (≠ G313), Q293 (≠ G314), S388 (≠ T413), G389 (≠ A414), G390 (= G415), E391 (≠ F416), K420 (≠ I445), W421 (≠ K446), K450 (≠ A477), Y451 (= Y478)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 97% coverage: 7:504/511 of query aligns to 5:474/475 of 5burA
- active site: T150 (= T169), S170 (≠ T188), H194 (= H213), T287 (= T310), E288 (= E311)
- binding adenosine-5'-triphosphate: T150 (= T169), S151 (= S170), T153 (= T172), T154 (= T173), K158 (= K177), G263 (≠ Q285), S283 (≠ L306), T287 (= T310), D365 (= D391), V377 (≠ I403), R380 (= R406)
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)
30% identity, 97% coverage: 7:504/511 of query aligns to 40:547/556 of Q9S725
- K211 (= K177) mutation to S: Drastically reduces the activity.
- M293 (≠ E254) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T281) mutation K->L,A: Affects the substrate specificity.
- E401 (= E358) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q360) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R406) mutation to Q: Drastically reduces the activity.
- K457 (≠ A414) mutation to S: Drastically reduces the activity.
- K540 (= K497) mutation to N: Abolishes the activity.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 97% coverage: 7:504/511 of query aligns to 22:526/530 of 5bsmA
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding adenosine-5'-triphosphate: S182 (≠ T169), S183 (= S170), G184 (= G171), T185 (= T172), T186 (= T173), K190 (= K177), H230 (= H213), A302 (≠ Q285), A303 (≠ M286), P304 (≠ M287), Y326 (≠ W307), G327 (= G308), M328 (= M309), T329 (= T310), D413 (= D391), I425 (= I403), R428 (= R406), K519 (= K497)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 97% coverage: 7:504/511 of query aligns to 21:525/528 of 5bsrA
- active site: S181 (≠ T169), S201 (≠ N189), H229 (= H213), T328 (= T310), E329 (= E311), K433 (≠ I412), Q438 (≠ N417), K518 (= K497)
- binding adenosine monophosphate: A301 (≠ Q285), G326 (= G308), T328 (= T310), D412 (= D391), K429 (= K408), K433 (≠ I412), Q438 (≠ N417)
- binding coenzyme a: L102 (≠ M86), P226 (= P210), H229 (= H213), Y231 (= Y215), F253 (= F236), K435 (≠ A414), G436 (= G415), F437 (= F416), F498 (≠ A477)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 97% coverage: 7:504/511 of query aligns to 22:526/529 of 5bsvA
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H213), Y232 (= Y215), S236 (≠ V218), A302 (≠ Q285), A303 (≠ M286), P304 (≠ M287), G325 (≠ L306), G327 (= G308), M328 (= M309), T329 (= T310), P333 (≠ G314), V334 (≠ L315), D413 (= D391), K430 (= K408), K434 (≠ I412), Q439 (≠ N417)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 97% coverage: 7:504/511 of query aligns to 22:526/529 of 5bsuA
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H213), Y232 (= Y215), S236 (≠ V218), M299 (≠ V282), A302 (≠ Q285), A303 (≠ M286), P304 (≠ M287), G325 (≠ L306), G327 (= G308), M328 (= M309), T329 (= T310), P333 (≠ G314), D413 (= D391), K430 (= K408), K434 (≠ I412), Q439 (≠ N417)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 97% coverage: 7:504/511 of query aligns to 22:526/529 of 5bstA
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H213), Y232 (= Y215), S236 (≠ V218), A302 (≠ Q285), A303 (≠ M286), P304 (≠ M287), G325 (≠ L306), Y326 (≠ W307), G327 (= G308), M328 (= M309), T329 (= T310), P333 (≠ G314), V334 (≠ L315), D413 (= D391), K430 (= K408), K434 (≠ I412), Q439 (≠ N417)
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)
30% identity, 97% coverage: 7:504/511 of query aligns to 29:533/542 of O24146
- S189 (≠ T169) binding
- S190 (= S170) binding
- G191 (= G171) binding
- T192 (= T172) binding
- T193 (= T173) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K177) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H213) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y215) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V218) binding ; binding ; binding
- K260 (≠ T235) binding
- A309 (≠ Q285) binding ; binding ; binding
- Q331 (≠ E305) binding
- G332 (≠ L306) binding ; binding ; binding ; binding ; binding
- T336 (= T310) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L315) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T318) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D391) binding ; binding ; binding ; binding ; binding
- R435 (= R406) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K408) binding ; binding ; binding ; binding
- K441 (≠ I412) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ A414) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G415) binding
- Q446 (≠ N417) binding
- K526 (= K497) binding ; mutation to A: Abolished activity against 4-coumarate.
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
31% identity, 97% coverage: 7:504/511 of query aligns to 5:474/481 of 5busA
- active site: T150 (= T169), S170 (≠ T188), H194 (= H213), T287 (= T310), E288 (= E311)
- binding adenosine monophosphate: H194 (= H213), G262 (= G284), G263 (≠ Q285), S283 (≠ L306), M286 (= M309), T287 (= T310), D365 (= D391), V377 (≠ I403), R380 (= R406), K467 (= K497)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 95% coverage: 26:509/511 of query aligns to 26:503/506 of 4gxqA
- active site: T163 (= T169), N183 (= N189), H207 (= H213), T303 (= T310), E304 (= E311), I403 (= I412), N408 (= N417), A491 (≠ K497)
- binding adenosine-5'-triphosphate: T163 (= T169), S164 (= S170), G165 (= G171), T166 (= T172), T167 (= T173), H207 (= H213), S277 (≠ G284), A278 (≠ Q285), P279 (≠ M286), E298 (= E305), M302 (= M309), T303 (= T310), D382 (= D391), R397 (= R406)
- binding carbonate ion: H207 (= H213), S277 (≠ G284), R299 (≠ L306), G301 (= G308)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 97% coverage: 7:504/511 of query aligns to 21:522/527 of 5u95B
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 98% coverage: 7:505/511 of query aligns to 22:527/528 of 3ni2A
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y215), S236 (≠ V218), G302 (= G284), A303 (≠ Q285), P304 (≠ M286), G325 (≠ L306), G327 (= G308), T329 (= T310), P333 (≠ G314), V334 (≠ L315), D413 (= D391), K430 (= K408), K434 (≠ I412), Q439 (≠ N417)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 98% coverage: 7:505/511 of query aligns to 22:527/528 of 3a9vA
- active site: S182 (≠ T169), S202 (≠ N189), H230 (= H213), T329 (= T310), E330 (= E311), K434 (≠ I412), Q439 (≠ N417), K519 (= K497)
- binding adenosine monophosphate: H230 (= H213), G302 (= G284), A303 (≠ Q285), P304 (≠ M286), Y326 (≠ W307), G327 (= G308), M328 (= M309), T329 (= T310), D413 (= D391), K430 (= K408), K434 (≠ I412), Q439 (≠ N417)
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, 94% coverage: 30:511/511 of query aligns to 31:501/503 of P9WQ37
- K172 (= K177) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T200) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ S202) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V214) 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 (≠ G216) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V219) 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 (≠ G249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G308) 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 (= W386) 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 (= D391) 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 (= R406) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T413) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G415) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K497) 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.
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, 99% coverage: 4:511/511 of query aligns to 38:577/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
29% identity, 94% coverage: 26:504/511 of query aligns to 57:542/559 of Q67W82
- G395 (= G357) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Query Sequence
>Pf6N2E2_1879 Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3)
MEHSIGNWVGRSAARFGNKPAIIFEGKYWSFLDIDVQSSRLAASLESMGVKREDVVSIYS
PNSPEWIITYYAILKIGAIVNPLNTMLTAREAAFAIKNCGAVAVFSTSDKLLALQEHIGP
TEVISLISFDGITVAGMRHFNLLVDANVAVREYPVTGIQKDDISTIGYTSGTTGQPKGAV
LSHRCILTNVSMTATMHLRTASDIAVSALPLSHVYGNVVMNSAIAYGMTLVLHKTFDAEA
ILSSIQIYGATLLEGVPTMYIYLLNCPNLGAYDVSSLTRCTVGGQMMPYTAMENVERALG
CRLLELWGMTELGGLGTTHSLYGERRLGSIGVALPHLEARIAQLELDGDALPLGEIGELQ
IRGPVVMKHYLGRPDATAETKTDEGWLRTGDLARMDSEGFIYIVDRLKDMFITAGFNIYP
AELERVIAEHPSVAMVAVGSVLDEIKGELAKAYIVPKTGYEIDIQQIERHCRDRLAAYKV
PRLFQIVEDLPKTSSGKVMRRMLRQIFESKL
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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