SitesBLAST
Comparing PP_4063 PP_4063 putative Long-chain-fatty-acid-CoA ligase 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)
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)
38% identity, 98% coverage: 5:552/560 of query aligns to 24:575/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 95% coverage: 18:548/560 of query aligns to 23:551/561 of P69451
- Y213 (= Y208) mutation to A: Loss of activity.
- T214 (= T209) mutation to A: 10% of wild-type activity.
- G216 (= G211) mutation to A: Decreases activity.
- T217 (= T212) mutation to A: Decreases activity.
- G219 (= G214) mutation to A: Decreases activity.
- K222 (= K217) mutation to A: Decreases activity.
- E361 (= E354) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 43:548/560 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T209), N183 (= N229), H207 (= H253), T303 (= T353), E304 (= E354), I403 (= I455), N408 (= N460), A491 (≠ K540)
- binding adenosine-5'-triphosphate: T163 (= T209), S164 (= S210), G165 (= G211), T166 (= T212), T167 (= T213), H207 (= H253), S277 (≠ G326), A278 (= A327), P279 (≠ T328), E298 (≠ Q347), M302 (= M352), T303 (= T353), D382 (= D434), R397 (= R449)
- binding carbonate ion: H207 (= H253), S277 (≠ G326), R299 (≠ A349), G301 (= G351)
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)
29% identity, 92% coverage: 35:548/560 of query aligns to 19:495/503 of P9WQ37
- K172 (= K217) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T240) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R242) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C254) 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 (≠ G256) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M259) 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 (= R291) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G351) 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 (= W429) 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 (= D434) 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 (= R449) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R456) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G458) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K540) 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.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 92% coverage: 35:548/560 of query aligns to 22:495/502 of 3r44A
Sites not aligning to the query:
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
30% identity, 91% coverage: 47:557/560 of query aligns to 37:517/518 of 4wv3B
- active site: S175 (≠ T209), T320 (= T353), E321 (= E354), K418 (≠ I455), W423 (≠ N460), K502 (= K540)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H253), T221 (≠ C254), F222 (= F255), A293 (= A325), S294 (≠ G326), E295 (≠ A327), A296 (≠ T328), G316 (≠ A349), I317 (≠ Y350), G318 (= G351), C319 (≠ M352), T320 (= T353), D397 (= D434), H409 (≠ I446), R412 (= R449), K502 (= K540)
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)
27% identity, 93% coverage: 36:553/560 of query aligns to 48:543/546 of Q84P21
- K530 (= K540) mutation to N: Lossed enzymatic activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 91% coverage: 27:534/560 of query aligns to 12:493/504 of 6qjzA
- active site: T169 (= T209), S189 (≠ N229), H213 (= H253), T314 (= T353), E315 (= E354), N414 (≠ I455), K419 (≠ N460)
- binding adenosine monophosphate: H213 (= H253), S288 (≠ A325), A289 (≠ G326), S290 (≠ A327), A312 (≠ G351), M313 (= M352), T314 (= T353), D393 (= D434), L405 (≠ I446), K410 (= K451), K419 (≠ N460)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 92% coverage: 36:549/560 of query aligns to 39:536/539 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 (= H253), F245 (= F255), T249 (≠ A260), G314 (= G326), A315 (= A327), P316 (≠ T328), G337 (≠ A349), Y338 (= Y350), G339 (= G351), L340 (≠ M352), T341 (= T353), S345 (≠ P357), A346 (≠ V358), D420 (= D434), I432 (= I446), K527 (= K540)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F255), R335 (≠ Q347), G337 (≠ A349), G339 (= G351), L340 (≠ M352), A346 (≠ V358)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 92% coverage: 36:549/560 of query aligns to 39:536/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H253), F245 (= F255), T249 (≠ A260), G314 (= G326), A315 (= A327), P316 (≠ T328), G337 (≠ A349), Y338 (= Y350), G339 (= G351), L340 (≠ M352), T341 (= T353), A346 (≠ V358), D420 (= D434), I432 (= I446), K527 (= K540)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
30% identity, 93% coverage: 30:547/560 of query aligns to 34:529/537 of 6e97B
- active site: S190 (≠ T209), S210 (≠ N229), H234 (= H253), A336 (≠ T353), E337 (= E354), N437 (≠ I455), K442 (≠ N460), K522 (= K540)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H253), N235 (≠ C254), F236 (= F255), S240 (≠ M259), G310 (= G326), A311 (= A327), K312 (≠ T328), V332 (≠ A349), F333 (≠ Y350), G334 (= G351), M335 (= M352), A336 (≠ T353), D416 (= D434), K433 (= K451), K442 (≠ N460)
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 91% coverage: 34:543/560 of query aligns to 16:497/512 of O74976
- S283 (≠ T328) modified: Phosphoserine
- S284 (≠ C329) modified: Phosphoserine
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
29% identity, 93% coverage: 30:547/560 of query aligns to 34:528/536 of 6e8oA
- active site: S190 (≠ T209), S210 (≠ N229), H234 (= H253), A336 (≠ T353), E337 (= E354), N437 (≠ I455), K442 (≠ N460), K521 (= K540)
- binding adenosine monophosphate: H234 (= H253), G310 (= G326), A311 (= A327), K312 (≠ T328), V332 (≠ A349), F333 (≠ Y350), G334 (= G351), M335 (= M352), A336 (≠ T353), D416 (= D434), V428 (≠ I446), K442 (≠ N460)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
28% identity, 92% coverage: 36:549/560 of query aligns to 37:534/539 of 2d1sA
- active site: S194 (≠ T209), R214 (≠ N229), H241 (= H253), T339 (= T353), E340 (= E354), K439 (≠ I455), Q444 (≠ N460), K525 (= K540)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T209), S195 (= S210), H241 (= H253), F243 (= F255), T247 (≠ A260), I282 (≠ Y296), G312 (= G326), A313 (= A327), P314 (≠ T328), Q334 (≠ I348), G335 (≠ A349), Y336 (= Y350), G337 (= G351), L338 (≠ M352), T339 (= T353), S343 (≠ P357), A344 (≠ V358), D418 (= D434), R433 (= R449), K525 (= K540)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
28% identity, 92% coverage: 36:549/560 of query aligns to 37:534/539 of 2d1rA
- active site: S194 (≠ T209), R214 (≠ N229), H241 (= H253), T339 (= T353), E340 (= E354), K439 (≠ I455), Q444 (≠ N460), K525 (= K540)
- binding adenosine monophosphate: S194 (≠ T209), S195 (= S210), H241 (= H253), G312 (= G326), A313 (= A327), P314 (≠ T328), G335 (≠ A349), Y336 (= Y350), G337 (= G351), L338 (≠ M352), T339 (= T353), D418 (= D434), K525 (= K540)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (= H253), F243 (= F255), T247 (≠ A260), G335 (≠ A349), G337 (= G351), L338 (≠ M352), A344 (≠ V358)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
30% identity, 88% coverage: 56:548/560 of query aligns to 52:532/541 of Q5SKN9
- T184 (= T209) binding
- G302 (= G326) binding
- Q322 (≠ I348) binding
- G323 (≠ A349) binding
- T327 (= T353) binding
- E328 (= E354) binding
- D418 (= D434) binding
- K435 (= K451) binding
- K439 (≠ I455) binding
5ie3A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 17:543/560 of query aligns to 3:496/504 of 5ie3A
- active site: T163 (= T209), S183 (≠ N229), H207 (= H253), T308 (= T353), E309 (= E354), N408 (≠ I455), K413 (≠ N460), K493 (= K540)
- binding adenosine monophosphate: S164 (= S210), S282 (≠ A325), A283 (≠ G326), S284 (≠ A327), Y305 (= Y350), A306 (≠ G351), M307 (= M352), T308 (= T353), D387 (= D434), L399 (≠ I446), R402 (= R449), K493 (= K540)
- binding oxalic acid: V208 (≠ C254), S282 (≠ A325), A306 (≠ G351), M307 (= M352), H312 (≠ P357), K493 (= K540)
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)
27% identity, 94% coverage: 17:543/560 of query aligns to 3:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 209:213) binding
- H214 (= H253) binding ; mutation to A: Abolished activity.
- S289 (≠ A325) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGA 325:327) binding
- EA 310:311 (≠ IA 348:349) binding
- M314 (= M352) binding
- T315 (= T353) binding
- H319 (≠ P357) binding ; mutation to A: Abolished activity.
- D394 (= D434) binding
- R409 (= R449) binding ; mutation to A: Abolished activity.
- K500 (= K540) binding ; binding ; mutation to A: Abolished activity.
5ie2A Crystal structure of a plant enzyme (see paper)
27% identity, 94% coverage: 17:543/560 of query aligns to 3:498/506 of 5ie2A
- active site: T165 (= T209), S185 (≠ N229), H209 (= H253), T310 (= T353), E311 (= E354), N410 (≠ I455), K415 (≠ N460), K495 (= K540)
- binding adenosine-5'-triphosphate: T165 (= T209), S166 (= S210), G167 (= G211), T168 (= T212), T169 (= T213), S284 (≠ A325), A285 (≠ G326), S286 (≠ A327), Y307 (= Y350), A308 (≠ G351), M309 (= M352), T310 (= T353), D389 (= D434), L401 (≠ I446), R404 (= R449), K495 (= K540)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
28% identity, 90% coverage: 45:548/560 of query aligns to 39:531/539 of P0DX84
- H231 (= H253) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ M257) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A325) mutation to P: Almost completely abolishes the activity.
- G303 (= G326) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y350) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P357) mutation to A: Retains 69% of wild-type activity.
- R432 (= R449) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K451) mutation to A: Retains 36% of wild-type activity.
- D435 (= D452) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I455) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G457) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G458) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E459) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N460) mutation to A: Retains 60% of wild-type activity.
- E474 (= E491) mutation to A: Retains 33% of wild-type activity.
- K523 (= K540) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K543) mutation to A: Retains 48% of wild-type activity.
Query Sequence
>PP_4063 PP_4063 putative Long-chain-fatty-acid-CoA ligase
MSQPSYTRGRQDRPLLTQTIGQAFDATVARCCDSEALVSRHQGLRYSWRQLAEQVEIYAR
ALIALGVNTGDRVGIWSPNCAQWCILQLASAKVGAILVNINPAYRVGELEYVLRQSGCRW
LVCAEAFKTSDYHTMVQELVPELASAAPGELASECLPELRGVISLAANPPAGFLPWHAFA
ERAGQTSVEACTARQQSLQFDQPVNIQYTSGTTGAPKGATLSHYNILNNGFMVGESLGLT
ARDRMVIPVPLYHCFGMVMANLGCITHGSTMIYPNDAFDAELTLRAVAEERATILYGVPT
MFIAMLDHPSRAHMDLSTLRSGIMAGATCPIEVMRRVIDQMHMAEVQIAYGMTETSPVSL
QTGPDDDLELRVTTVGRTQPQLENKLVDADGCIVPRGEIGELCTRGYSVMLGYWDNPQAT
ADAIDPAGWMHSGDLAVMDEQGYVRIVGRNKDMIIRGGENIYPRELEEFFYTHPAVADAQ
VIGIPCSRYGEEIVAWIKLHPGHSATVEELQGWCKARIAHFKVPRYIRFVDEYPMTVTGK
VQKFRMREISVAEIAAASAG
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