SitesBLAST
Comparing 15923 FitnessBrowser__Keio:15923 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
100% identity, 100% coverage: 1:561/561 of query aligns to 1:561/561 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.
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, 94% coverage: 25:550/561 of query aligns to 38:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ T304) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ A331) 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 (= R453) mutation to Q: Drastically reduces the activity.
- K457 (≠ S461) mutation to S: Drastically reduces the activity.
- K540 (= K543) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 93% coverage: 31:552/561 of query aligns to 26:528/528 of 3ni2A
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F263), S236 (≠ I267), G302 (= G334), A303 (≠ M335), P304 (= P336), G325 (= G356), G327 (= G358), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D438), K430 (= K455), K434 (≠ L459), Q439 (≠ N464)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 93% coverage: 31:552/561 of query aligns to 26:528/528 of 3a9vA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- binding adenosine monophosphate: H230 (= H261), G302 (= G334), A303 (≠ M335), P304 (= P336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D438), K430 (= K455), K434 (≠ L459), Q439 (≠ N464)
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, 92% coverage: 37:550/561 of query aligns to 46:542/559 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.
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: 41:549/561 of query aligns to 48:536/546 of Q84P21
- K530 (= K543) mutation to N: Lossed enzymatic activity.
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, 93% coverage: 31:550/561 of query aligns to 33:533/542 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 (= H261) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F263) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ I267) binding ; binding ; binding
- K260 (≠ P285) binding
- A309 (≠ G334) binding ; binding ; binding
- Q331 (≠ E355) binding
- G332 (= G356) binding ; binding ; binding ; binding ; binding
- T336 (= T360) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L365) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ V368) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D438) binding ; binding ; binding ; binding ; binding
- R435 (= R453) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K455) binding ; binding ; binding ; binding
- K441 (≠ L459) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S461) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G462) binding
- Q446 (≠ N464) binding
- K526 (= K543) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H261), T328 (= T360), E329 (= E361), K433 (≠ L459), Q438 (≠ N464), K518 (= K543)
- binding adenosine monophosphate: A301 (≠ G334), G326 (= G358), T328 (= T360), D412 (= D438), K429 (= K455), K433 (≠ L459), Q438 (≠ N464)
- binding coenzyme a: L102 (= L107), P226 (= P258), H229 (= H261), Y231 (≠ F263), F253 (≠ R286), K435 (≠ S461), G436 (= G462), F437 (= F463), F498 (≠ G523)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:526/529 of 5bsvA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- 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 (≠ I267), A302 (≠ G334), A303 (≠ M335), P304 (= P336), G325 (= G356), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D438), K430 (= K455), K434 (≠ L459), Q439 (≠ N464)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:526/529 of 5bsuA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- 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 (≠ I267), M299 (≠ A331), A302 (≠ G334), A303 (≠ M335), P304 (= P336), G325 (= G356), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), D413 (= D438), K430 (= K455), K434 (≠ L459), Q439 (≠ N464)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:526/529 of 5bstA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- 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 (≠ I267), A302 (≠ G334), A303 (≠ M335), P304 (= P336), G325 (= G356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D438), K430 (= K455), K434 (≠ L459), Q439 (≠ N464)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L459), Q439 (≠ N464), K519 (= K543)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H261), A302 (≠ G334), A303 (≠ M335), P304 (= P336), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D438), I425 (= I450), R428 (= R453), K519 (= K543)
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, 93% coverage: 42:560/561 of query aligns to 58:580/590 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
30% identity, 93% coverage: 31:550/561 of query aligns to 25:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H261), F245 (= F263), T249 (≠ I273), G314 (= G334), A315 (≠ M335), P316 (= P336), G337 (= G356), Y338 (= Y357), G339 (= G358), L340 (= L359), T341 (= T360), S345 (≠ P364), A346 (≠ L365), D420 (= D438), I432 (= I450), K527 (= K543)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F263), R335 (≠ L354), G337 (= G356), G339 (= G358), L340 (= L359), A346 (≠ L365)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
30% identity, 93% coverage: 31:550/561 of query aligns to 26:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H261), F245 (= F263), T249 (≠ I273), G314 (= G334), A315 (≠ M335), P316 (= P336), G337 (= G356), Y338 (= Y357), G339 (= G358), L340 (= L359), T341 (= T360), A346 (≠ L365), D420 (= D438), I432 (= I450), K527 (= K543)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 46:551/561 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T214), N183 (= N234), H207 (= H261), T303 (= T360), E304 (= E361), I403 (≠ L459), N408 (= N464), A491 (≠ K543)
- binding adenosine-5'-triphosphate: T163 (= T214), S164 (≠ G215), G165 (= G216), T166 (= T217), T167 (= T218), H207 (= H261), S277 (≠ G334), A278 (≠ M335), P279 (= P336), E298 (= E355), M302 (≠ L359), T303 (= T360), D382 (= D438), R397 (= R453)
- binding carbonate ion: H207 (= H261), S277 (≠ G334), R299 (≠ G356), G301 (= G358)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
32% identity, 96% coverage: 14:551/561 of query aligns to 8:533/539 of 2d1sA
- active site: S194 (≠ T214), R214 (≠ N234), H241 (= H261), T339 (= T360), E340 (= E361), K439 (≠ L459), Q444 (≠ N464), K525 (= K543)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T214), S195 (≠ G215), H241 (= H261), F243 (= F263), T247 (≠ N268), I282 (≠ T304), G312 (= G334), A313 (≠ M335), P314 (= P336), Q334 (≠ E355), G335 (= G356), Y336 (= Y357), G337 (= G358), L338 (= L359), T339 (= T360), S343 (≠ P364), A344 (≠ L365), D418 (= D438), R433 (= R453), K525 (= K543)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
32% identity, 96% coverage: 14:551/561 of query aligns to 8:533/539 of 2d1rA
- active site: S194 (≠ T214), R214 (≠ N234), H241 (= H261), T339 (= T360), E340 (= E361), K439 (≠ L459), Q444 (≠ N464), K525 (= K543)
- binding adenosine monophosphate: S194 (≠ T214), S195 (≠ G215), H241 (= H261), G312 (= G334), A313 (≠ M335), P314 (= P336), G335 (= G356), Y336 (= Y357), G337 (= G358), L338 (= L359), T339 (= T360), D418 (= D438), K525 (= K543)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H261), F243 (= F263), T247 (≠ N268), G335 (= G356), G337 (= G358), L338 (= L359), A344 (≠ L365)
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: 49:557/561 of query aligns to 30:501/503 of P9WQ37
- K172 (= K222) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ L245) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K250) 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 (= A264) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ C269) 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 (≠ F300) 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 (= W433) 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 (= D438) 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 (= R453) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V460) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G462) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K543) 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
>15923 FitnessBrowser__Keio:15923
MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRA
FAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDS
GASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHL
PDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA
TYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPF
TAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLT
ECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQ
RPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGV
QEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSN
VGKILRRELRDEARGKVDNKA
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