SitesBLAST
Comparing 3607419 Dshi_0833 AMP-dependent synthetase and ligase (RefSeq) 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)
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)
36% identity, 95% coverage: 26:539/541 of query aligns to 24:535/541 of Q5SKN9
- T184 (= T192) binding
- G302 (= G307) binding
- Q322 (= Q327) binding
- G323 (≠ V328) binding
- T327 (= T332) binding
- E328 (= E333) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (≠ I444) binding
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)
32% identity, 91% coverage: 45:539/541 of query aligns to 39:534/539 of P0DX84
- H231 (= H236) mutation to A: Retains 74% of wild-type activity.
- W235 (= W240) mutation to A: Almost completely abolishes the activity.
- G302 (≠ T305) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A306) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y329) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G336) mutation to A: Retains 69% of wild-type activity.
- R432 (= R438) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K440) mutation to A: Retains 36% of wild-type activity.
- D435 (= D441) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I444) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G446) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G447) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E448) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N449) mutation to A: Retains 60% of wild-type activity.
- E474 (= E480) mutation to A: Retains 33% of wild-type activity.
- K523 (= K528) 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 (= K531) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
32% identity, 91% coverage: 45:539/541 of query aligns to 39:534/538 of 6ijbB
- active site: T185 (= T192), H205 (≠ M212), H231 (= H236), S329 (≠ T332), E330 (= E333), K438 (≠ I444), W443 (≠ N449), A523 (≠ K528)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W240), G303 (≠ A306), A325 (≠ V328), W326 (≠ Y329), G327 (= G330), M328 (≠ L331)
- binding adenosine monophosphate: G303 (≠ A306), A304 (≠ G307), A305 (= A308), H324 (≠ Q327), W326 (≠ Y329), G327 (= G330), M328 (≠ L331), S329 (≠ T332), Q359 (= Q362), D417 (= D423)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
31% identity, 93% coverage: 34:536/541 of query aligns to 24:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T192), G174 (= G194), T175 (= T195), T176 (= T196), K180 (= K200), G293 (≠ A306), A294 (≠ G307), A295 (= A308), Y315 (= Y329), M317 (≠ L331), S318 (≠ T332), D408 (= D423), R423 (= R438)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
31% identity, 91% coverage: 45:539/541 of query aligns to 39:531/533 of 6ihkB
- active site: T185 (= T192), H202 (≠ M212), H228 (= H236), S326 (≠ T332), E327 (= E333), K435 (≠ I444), W440 (≠ N449), K520 (= K528)
- binding adenosine-5'-diphosphate: H228 (= H236), G300 (≠ A306), A301 (≠ G307), A302 (= A308), H321 (≠ Q327), A322 (≠ V328), W323 (≠ Y329), G324 (= G330), M325 (≠ L331), S326 (≠ T332), Q356 (= Q362), D414 (= D423), R429 (= R438), K520 (= K528)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
31% identity, 93% coverage: 34:536/541 of query aligns to 24:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ T305), G293 (≠ A306), A294 (≠ G307), A295 (= A308), G314 (≠ V328), Y315 (= Y329), M317 (≠ L331), S318 (≠ T332), D408 (= D423), R423 (= R438)
- binding 4'-phosphopantetheine: R93 (= R103), P220 (= P233), H223 (= H236)
8i49A Acyl-acp synthetase structure bound to atp
31% identity, 93% coverage: 34:536/541 of query aligns to 24:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
31% identity, 93% coverage: 34:536/541 of query aligns to 24:527/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp
31% identity, 93% coverage: 34:536/541 of query aligns to 24:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ T305), G293 (≠ A306), A295 (= A308), G314 (≠ V328), Y315 (= Y329), G316 (= G330), M317 (≠ L331), S318 (≠ T332), D408 (= D423), K429 (≠ I444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H236), W227 (= W240), G292 (≠ T305), G316 (= G330), P322 (≠ G336)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R103), P220 (= P233), H223 (= H236), I269 (≠ V282), G432 (= G447)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 93% coverage: 34:536/541 of query aligns to 22:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A306), A293 (= A308), G312 (≠ V328), Y313 (= Y329), G314 (= G330), M315 (≠ L331), S316 (≠ T332), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (≠ L331), S316 (≠ T332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7
31% identity, 93% coverage: 34:536/541 of query aligns to 22:525/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A306), A293 (= A308), Y313 (= Y329), M315 (≠ L331), S316 (≠ T332), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W240), G290 (≠ T305), G312 (≠ V328), G314 (= G330), M315 (≠ L331), P320 (≠ G336), I321 (≠ H337)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 93% coverage: 26:530/541 of query aligns to 17:502/510 of 1v26B
- active site: T177 (= T192), H197 (≠ M212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I444), W437 (≠ N449)
- binding adenosine monophosphate: G295 (= G307), S296 (≠ A308), A297 (≠ P309), G316 (≠ V328), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D423), K428 (= K440), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T192), E321 (= E333)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 85% coverage: 26:486/541 of query aligns to 17:464/491 of 1v25A
- active site: T177 (= T192), H197 (≠ M212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I444), W437 (≠ N449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H236), V224 (≠ C237), G295 (= G307), S296 (≠ A308), A297 (≠ P309), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D423), I423 (= I435), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T192), E321 (= E333)
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, 95% coverage: 26:540/541 of query aligns to 8:499/503 of P9WQ37
- R9 (≠ A27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D35) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K200) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ V223) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Y225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C237) 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 (≠ G239) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ H242) 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 (≠ G272) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G330) 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 (≠ Y418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K528) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 95% coverage: 26:540/541 of query aligns to 11:499/502 of 3r44A
Sites not aligning to the query:
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)
29% identity, 95% coverage: 26:539/541 of query aligns to 8:481/485 of 5x8fB
- active site: T151 (= T192), S171 (≠ M212), H195 (= H236), T288 (= T332), E289 (= E333), I387 (= I444), N392 (= N449), K470 (= K528)
- binding magnesium ion: Y23 (= Y41), E24 (≠ G42), H70 (≠ P91), N178 (≠ S219), L202 (≠ S243), L214 (≠ C255), T296 (≠ E340), L297 (≠ C341), S298 (≠ V342)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (≠ V232), P192 (= P233), H195 (= H236), I196 (≠ C237), S197 (≠ N238), A237 (≠ G278), V238 (≠ A279), L260 (≠ F304), G262 (≠ A306), G286 (= G330), M287 (≠ L331), S292 (≠ G336), Q293 (≠ H337), S388 (= S445), G389 (= G446), G390 (= G447), E391 (= E448), K420 (≠ T477), W421 (= W478), K450 (≠ G509), Y451 (≠ F510)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 95% coverage: 26:539/541 of query aligns to 8:481/484 of 5gtdA
- active site: T151 (= T192), S171 (≠ M212), H195 (= H236), T288 (= T332), E289 (= E333)
- binding adenosine-5'-monophosphate: G263 (= G307), G264 (≠ A308), Y285 (= Y329), G286 (= G330), M287 (≠ L331), T288 (= T332), D366 (= D423), V378 (≠ I435)
- binding magnesium ion: F314 (vs. gap), S315 (vs. gap)
- binding 2-succinylbenzoate: H195 (= H236), S197 (≠ N238), A237 (≠ G278), L260 (≠ F304), G262 (≠ A306), G263 (= G307), G286 (= G330), M287 (≠ L331), S292 (≠ G336), Q293 (≠ H337)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 94% coverage: 26:531/541 of query aligns to 10:498/506 of 5ie2A
- active site: T165 (= T192), S185 (≠ M212), H209 (= H236), T310 (= T332), E311 (= E333), N410 (≠ I444), K415 (≠ N449), K495 (= K528)
- binding adenosine-5'-triphosphate: T165 (= T192), S166 (= S193), G167 (= G194), T168 (= T195), T169 (= T196), S284 (≠ G307), A285 (= A308), S286 (≠ P309), Y307 (= Y329), A308 (≠ G330), M309 (≠ L331), T310 (= T332), D389 (= D423), L401 (≠ I435), R404 (= R438), K495 (= K528)
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)
28% identity, 94% coverage: 26:531/541 of query aligns to 10:503/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 192:196) binding
- H214 (= H236) binding ; mutation to A: Abolished activity.
- S289 (≠ G307) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAP 307:309) binding
- EA 310:311 (≠ QV 327:328) binding
- M314 (≠ L331) binding
- T315 (= T332) binding
- H319 (≠ G336) binding ; mutation to A: Abolished activity.
- D394 (= D423) binding
- R409 (= R438) binding ; mutation to A: Abolished activity.
- K500 (= K528) binding ; binding ; mutation to A: Abolished 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)
27% identity, 91% coverage: 44:534/541 of query aligns to 56:536/546 of Q84P21
- K530 (= K528) mutation to N: Lossed enzymatic activity.
Query Sequence
>3607419 Dshi_0833 AMP-dependent synthetase and ligase (RefSeq)
MGWLANETGLDKCAANYVPLTPLSHLARAALVYPDREAVVYGARRFTYAEYHARVSRLAS
ALAGAGIAPGDVVATLLPNIPAMVEAHFGVPACGAVLNTINIRLDVDTVAYILSHGGAKA
VLVDSQFLPLAAEACERLDGPAPLLIEVADDAAGVHALGGYTEYEDFLAGGDPDFPWIMP
RDEWESLALNYTSGTTGRPKGVVYHHRGAYLMTMGTVISWRMVLYPRWLAIVPLFHCNGW
NHSWMMPMLGGTVVCCRDVSAQAIYTAIAENGVTHFGGAPIVLNMIVNAPDAARRPFSHT
VEVFTAGAPPAAATLAAIEELGFNVTQVYGLTETYGHVTECVWNPDWDTLPQAERAAIKA
RQGVALPQMEHITVMDPEMRQVPMDGATTGEVMMRGNSVMKGYYRNPDATAEAFAGGYFH
SGDIALQHPDGYIQIADRAKDIIISGGENISSVEVEGALMHHPAVLLCAVVAKPDPTWGE
VPCAFVELKDGKTAEEAEIIAFARERLAGFKTPKKVVFTELPKTSTGKIQKFELRNRAKA
L
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