SitesBLAST
Comparing AO356_05105 FitnessBrowser__pseudo5_N2C3_1:AO356_05105 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)
53% identity, 99% coverage: 6:562/562 of query aligns to 5:553/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E369) mutation to A: Loss of activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 92% coverage: 42:559/562 of query aligns to 22:484/486 of 8wevA
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: 29:559/562 of query aligns to 42:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ L312) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N339) mutation K->L,A: Affects the substrate specificity.
- E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R462) mutation to Q: Drastically reduces the activity.
- K457 (≠ S470) mutation to S: Drastically reduces the activity.
- K540 (= K552) mutation to N: Abolishes the activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 93% coverage: 36:559/562 of query aligns to 29:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H269), T328 (= T368), E329 (= E369), K433 (≠ I468), Q438 (≠ N473), K518 (= K552)
- binding adenosine monophosphate: A301 (≠ G342), G326 (= G366), T328 (= T368), D412 (= D447), K429 (= K464), K433 (≠ I468), Q438 (≠ N473)
- binding coenzyme a: L102 (= L108), P226 (= P266), H229 (= H269), Y231 (= Y271), F253 (≠ R294), K435 (≠ S470), G436 (= G471), F437 (= F472), F498 (≠ G532)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 93% coverage: 36:559/562 of query aligns to 30:526/530 of 5bsmA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding adenosine-5'-triphosphate: S182 (≠ T215), S183 (≠ G216), G184 (= G217), T185 (= T218), T186 (= T219), K190 (= K223), H230 (= H269), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), I425 (= I459), R428 (= R462), K519 (= K552)
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: 36:559/562 of query aligns to 37:533/542 of O24146
- S189 (≠ T215) binding ATP
- S190 (≠ G216) binding ATP
- G191 (= G217) binding ATP
- T192 (= T218) binding ATP
- T193 (= T219) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K223) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H269) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y271) 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 (≠ A275) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P293) binding CoA
- A309 (≠ G342) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E363) binding ATP
- G332 (= G364) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T368) 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 (= V373) 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 (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D447) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R462) 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 (= K464) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I468) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S470) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G471) binding CoA
- Q446 (≠ N473) binding AMP
- K526 (= K552) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 93% coverage: 36:559/562 of query aligns to 30:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 93% coverage: 36:559/562 of query aligns to 30:526/529 of 5bsuA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), M299 (≠ N339), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 93% coverage: 36:559/562 of query aligns to 30:526/529 of 5bstA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 91% coverage: 47:560/562 of query aligns to 43:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y271), S236 (≠ A275), G302 (= G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), G327 (= G366), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 91% coverage: 47:560/562 of query aligns to 43:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding adenosine monophosphate: H230 (= H269), G302 (= G342), A303 (≠ T343), P304 (≠ A344), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
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)
30% identity, 91% coverage: 49:562/562 of query aligns to 47:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 91% coverage: 47:560/562 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T215), N183 (= N235), H207 (= H269), T303 (= T368), E304 (= E369), I403 (= I468), N408 (= N473), A491 (≠ K552)
- binding adenosine-5'-triphosphate: T163 (= T215), S164 (≠ G216), G165 (= G217), T166 (= T218), T167 (= T219), H207 (= H269), S277 (≠ G342), A278 (≠ T343), P279 (≠ A344), E298 (= E363), M302 (≠ L367), T303 (= T368), D382 (= D447), R397 (= R462)
- binding carbonate ion: H207 (= H269), S277 (≠ G342), R299 (≠ G364), G301 (= G366)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 93% coverage: 36:559/562 of query aligns to 29:522/527 of 5u95B
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)
29% identity, 94% coverage: 29:556/562 of query aligns to 9:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 215:219) binding ATP
- H214 (= H269) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G342) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GTA 342:344) binding ATP
- EA 310:311 (≠ EG 363:364) binding ATP
- M314 (≠ L367) binding oxalate
- T315 (= T368) binding ATP
- H319 (≠ P372) binding oxalate; mutation to A: Abolished activity.
- D394 (= D447) binding ATP
- R409 (= R462) binding ATP; mutation to A: Abolished activity.
- K500 (= K552) binding ATP; binding oxalate; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 94% coverage: 29:556/562 of query aligns to 9:499/506 of 5ie2A
- active site: T165 (= T215), S185 (≠ N235), H209 (= H269), T310 (= T368), E311 (= E369), N410 (≠ I468), K415 (≠ N473), K495 (= K552)
- binding adenosine-5'-triphosphate: T165 (= T215), S166 (≠ G216), G167 (= G217), T168 (= T218), T169 (= T219), S284 (≠ G342), A285 (≠ T343), S286 (≠ A344), Y307 (= Y365), A308 (≠ G366), M309 (≠ L367), T310 (= T368), D389 (= D447), L401 (≠ I459), R404 (= R462), K495 (= K552)
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 94% coverage: 29:556/562 of query aligns to 9:497/504 of 5ie3A
- active site: T163 (= T215), S183 (≠ N235), H207 (= H269), T308 (= T368), E309 (= E369), N408 (≠ I468), K413 (≠ N473), K493 (= K552)
- binding adenosine monophosphate: S164 (≠ G216), S282 (≠ G342), A283 (≠ T343), S284 (≠ A344), Y305 (= Y365), A306 (≠ G366), M307 (≠ L367), T308 (= T368), D387 (= D447), L399 (≠ I459), R402 (= R462), K493 (= K552)
- binding oxalic acid: V208 (≠ I270), S282 (≠ G342), A306 (≠ G366), M307 (≠ L367), H312 (≠ P372), K493 (= K552)
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, 99% coverage: 5:562/562 of query aligns to 17:540/546 of Q84P21
- K530 (= K552) mutation to N: Lossed enzymatic 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)
29% identity, 93% coverage: 36:559/562 of query aligns to 44:542/559 of Q67W82
- G395 (= G413) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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: 48:560/562 of query aligns to 28:495/503 of P9WQ37
- K172 (= K223) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ L246) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E248) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I270) 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 (= A272) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A275) 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 (= R307) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G366) 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 (= W442) 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 (= D447) 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 (= R462) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V469) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G471) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K552) 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.
Query Sequence
>AO356_05105 FitnessBrowser__pseudo5_N2C3_1:AO356_05105
MQPDFWNDKRPAGVPLDVDLGTYKSVIEVFERSCKKFADRPAFSNMGVTLTYAELERYSA
AFAGYLQTHTDLAPGDRIAVQMPNILQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKD
SGARALVYLNMFGQKVQEVLPDTDLQYLIEAKMGDLMPTAKGWLVNTMVSKVKKMVPAYS
LPQAISFKSALRLGRGQGIKPLNVSLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMQQAR
ACLGQLGEDGQPLLREGQEVMIAPLPLYHIYAFTANCMCMMVTGNHNVLITNPRDIGGFI
KELKNWRFSLLLGLNTLFVALMDHPDFKTLDFSHLKVTNSGGTALIKATAERWQQLTGCG
ITEGYGLTETSPVASANPYGGKSRLGTVGMPVPGTLMKVINDDGLEQPLGERGELCIKGP
QIMKGYWNKPEATAEVLDSEGWFKSGDIAVIDPDGFVRIVDRKKDMIIVSGFNVYPNEIE
DVVMAHPKVANCAVIGVPDERSGEAVKLFVVAREAGVSLEELKAYCKENFTGYKIPKHIV
LRDSLPMTPVGKILRRELRDIA
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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