SitesBLAST
Comparing WP_041642354.1 NCBI__GCF_000061505.1:WP_041642354.1 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)
60% identity, 99% coverage: 1:553/561 of query aligns to 1:552/561 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 (= E361) mutation to A: Loss of 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)
31% identity, 91% coverage: 49:556/561 of query aligns to 30:499/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Q245) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R247) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I262) 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 (≠ S264) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A267) 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 (= R299) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G358) 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 (≠ F434) 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 (= D439) 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 (= R454) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V461) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G463) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K544) 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.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 46:552/561 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H261), T303 (= T360), E304 (= E361), I403 (≠ L460), N408 (= N465), A491 (≠ K544)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (≠ G215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H261), S277 (≠ G334), A278 (≠ M335), P279 (≠ A336), E298 (= E355), M302 (≠ L359), T303 (= T360), D382 (= D439), R397 (= R454)
- binding carbonate ion: H207 (= H261), S277 (≠ G334), R299 (≠ A356), G301 (= G358)
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)
29% identity, 91% coverage: 39:550/561 of query aligns to 46:536/546 of Q84P21
- K530 (= K544) mutation to N: Lossed enzymatic activity.
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)
30% identity, 94% coverage: 24:548/561 of query aligns to 5:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 214:218) binding ATP
- H214 (= H261) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G334) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 334:336) binding ATP
- EA 310:311 (= EA 355:356) binding ATP
- M314 (≠ L359) binding oxalate
- T315 (= T360) binding ATP
- H319 (≠ P364) binding oxalate; mutation to A: Abolished activity.
- D394 (= D439) binding ATP
- R409 (= R454) binding ATP; mutation to A: Abolished activity.
- K500 (= K544) binding ATP; binding oxalate; mutation to A: Abolished 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: 24:551/561 of query aligns to 38:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 91% coverage: 49:556/561 of query aligns to 33:499/502 of 3r44A
Sites not aligning to the query:
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 94% coverage: 24:548/561 of query aligns to 5:497/504 of 5ie3A
- active site: T163 (= T214), S183 (≠ N234), H207 (= H261), T308 (= T360), E309 (= E361), N408 (≠ L460), K413 (≠ N465), K493 (= K544)
- binding adenosine monophosphate: S164 (≠ G215), S282 (≠ G334), A283 (≠ M335), S284 (≠ A336), Y305 (= Y357), A306 (≠ G358), M307 (≠ L359), T308 (= T360), D387 (= D439), L399 (≠ I451), R402 (= R454), K493 (= K544)
- binding oxalic acid: V208 (≠ I262), S282 (≠ G334), A306 (≠ G358), M307 (≠ L359), H312 (≠ P364), K493 (= K544)
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 94% coverage: 24:548/561 of query aligns to 5:499/506 of 5ie2A
- active site: T165 (= T214), S185 (≠ N234), H209 (= H261), T310 (= T360), E311 (= E361), N410 (≠ L460), K415 (≠ N465), K495 (= K544)
- binding adenosine-5'-triphosphate: T165 (= T214), S166 (≠ G215), G167 (= G216), T168 (= T217), T169 (= T218), S284 (≠ G334), A285 (≠ M335), S286 (≠ A336), Y307 (= Y357), A308 (≠ G358), M309 (≠ L359), T310 (= T360), D389 (= D439), L401 (≠ I451), R404 (= R454), K495 (= K544)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 93% coverage: 31:553/561 of query aligns to 26:528/528 of 3ni2A
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F263), S236 (≠ A267), G302 (= G334), A303 (≠ M335), P304 (≠ A336), G325 (≠ A356), G327 (= G358), T329 (= T360), P333 (= P364), V334 (≠ A365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 93% coverage: 31:553/561 of query aligns to 26:528/528 of 3a9vA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine monophosphate: H230 (= H261), G302 (= G334), A303 (≠ M335), P304 (≠ A336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
30% identity, 94% coverage: 24:552/561 of query aligns to 26:527/539 of P40871
- G191 (= G215) binding ATP
- HN 234:235 (≠ HI 261:262) binding substrate
- S240 (≠ A267) binding substrate
- G307 (= G334) binding ATP
- V329 (≠ A356) binding ATP
- D413 (= D439) binding ATP
- R428 (= R454) binding ATP
- K519 (= K544) binding ATP; binding substrate
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)
27% identity, 94% coverage: 27:551/561 of query aligns to 40:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ T304) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L331) mutation K->L,A: Affects the substrate specificity.
- E401 (= E406) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C408) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R454) mutation to Q: Drastically reduces the activity.
- K457 (≠ S462) mutation to S: Drastically reduces the activity.
- K540 (= K544) mutation to N: Abolishes the activity.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 93% coverage: 31:551/561 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ A267), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), G325 (≠ A356), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ A365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 93% coverage: 31:551/561 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ A267), M299 (≠ L331), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), G325 (≠ A356), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 93% coverage: 31:551/561 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ A267), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), G325 (≠ A356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ A365), D413 (= D439), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 93% coverage: 31:551/561 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H261), T328 (= T360), E329 (= E361), K433 (≠ L460), Q438 (≠ N465), K518 (= K544)
- binding adenosine monophosphate: A301 (≠ G334), G326 (= G358), T328 (= T360), D412 (= D439), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L107), P226 (= P258), H229 (= H261), Y231 (≠ F263), F253 (≠ R286), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ A524)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
28% identity, 93% coverage: 31:551/561 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H261), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D439), I425 (= I451), R428 (= R454), K519 (= K544)
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, 93% coverage: 31:551/561 of query aligns to 33:533/542 of O24146
- S189 (≠ T214) binding ATP
- S190 (≠ G215) binding ATP
- G191 (= G216) binding ATP
- T192 (= T217) binding ATP
- T193 (= T218) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K222) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H261) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F263) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A267) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P285) binding CoA
- A309 (≠ G334) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E355) binding ATP
- G332 (≠ A356) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T360) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ A365) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ I368) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R454) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L460) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding CoA
- Q446 (≠ N465) binding AMP
- K526 (= K544) binding ATP; mutation to A: Abolished activity against 4-coumarate.
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, 92% coverage: 38:551/561 of query aligns to 47:542/559 of Q67W82
- G395 (= G405) 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
>WP_041642354.1 NCBI__GCF_000061505.1:WP_041642354.1
MDKIWLKSYPAGVPAEVDVGEFASIGDLFEQGVRRYGSRPAYICMGRSLAYDELDVLVSR
FAAYLQGELKLAHGARVALMMPNVLQYPVAMFAALRAGYTVVNVNPLYTARELEHQLRDA
AAEAVILLENFAHTLEMVVQHLPIRHVVVTSVGDLLGFPKGAVVDFVLRRVRKLVPPWKL
PGAVRFREALAAGAKHTFRPADVGHDDIAYLQYTGGTTGTAKGAILTHGNIIANLQQAHA
WIRPQVREGAEVIITALPLYHIFSLTANCLTFFKIGATNVLITNPRDIRGFVKELGKHRF
TAITGVNTLFNALLNNPDFARLDFSALHITLGGGMAVQQAVAEKWRAVTGVPLIEAYGLT
ETSPAVAINPLDLKAFNHSIGLPVPSTEVSIRDDDGVEQPPGQRGELCVRGPQVTRGYWN
RPEDSARAFTPDGFLRTGDIAVMDEAGYLRIVDRKKDMILVSGFNVYPNEVEDVVASHPG
VLEVAAVGVPDARSGEAVKVFVVRKDASLTEADLIAYCRENLTAYKVPHRVVFRESLPKT
NVGKILRRALRDEDEAAARQP
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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