SitesBLAST
Comparing WP_011385011.1 NCBI__GCF_000009985.1:WP_011385011.1 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)
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)
38% identity, 95% coverage: 25:539/541 of query aligns to 23:535/541 of Q5SKN9
- T184 (= T191) binding
- G302 (= G306) binding
- Q322 (≠ H326) binding
- G323 (≠ V327) binding
- T327 (= T331) binding
- E328 (= E332) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (≠ I444) binding
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 86% coverage: 25:488/541 of query aligns to 16:466/491 of 1v25A
- active site: T177 (= T191), H197 (≠ N211), H223 (= H235), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H235), V224 (≠ C236), G295 (= G306), S296 (≠ A307), A297 (= A308), Y317 (= Y328), G318 (= G329), L319 (= L330), T320 (= T331), D411 (= D423), I423 (= I435), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T191), E321 (= E332)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 85% coverage: 25:484/541 of query aligns to 16:463/510 of 1v26B
- active site: T177 (= T191), H197 (≠ N211), H223 (= H235), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding adenosine monophosphate: G295 (= G306), S296 (≠ A307), A297 (= A308), G316 (≠ V327), Y317 (= Y328), G318 (= G329), L319 (= L330), T320 (= T331), D411 (= D423), K428 (= K440), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T191), E321 (= E332)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
31% identity, 92% coverage: 39:536/541 of query aligns to 28:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T191), G174 (= G193), T175 (= T194), T176 (= T195), K180 (= K199), G293 (= G306), A294 (= A307), A295 (= A308), Y315 (= Y328), M317 (≠ L330), S318 (≠ T331), D408 (= D423), R423 (= R438)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
31% identity, 92% coverage: 39:536/541 of query aligns to 28:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A305), G293 (= G306), A295 (= A308), G314 (≠ V327), Y315 (= Y328), G316 (= G329), M317 (≠ L330), S318 (≠ T331), D408 (= D423), K429 (≠ I444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H235), W227 (= W239), G292 (≠ A305), G316 (= G329), P322 (= P336)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R103), P220 (= P232), H223 (= H235), I269 (≠ V281), G432 (= G447)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
31% identity, 92% coverage: 39:536/541 of query aligns to 28:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A305), G293 (= G306), A294 (= A307), A295 (= A308), G314 (≠ V327), Y315 (= Y328), M317 (≠ L330), S318 (≠ T331), D408 (= D423), R423 (= R438)
- binding 4'-phosphopantetheine: R93 (= R103), P220 (= P232), H223 (= H235)
8i49A Acyl-acp synthetase structure bound to atp
31% identity, 92% coverage: 39:536/541 of query aligns to 28:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
31% identity, 92% coverage: 39:536/541 of query aligns to 28:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 92% coverage: 39:536/541 of query aligns to 26:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G306), A293 (= A308), G312 (≠ V327), Y313 (= Y328), G314 (= G329), M315 (≠ L330), S316 (≠ T331), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (≠ L330), S316 (≠ T331), E317 (= E332)
8i51A Acyl-acp synthetase structure bound to amp-mc7
31% identity, 92% coverage: 39:536/541 of query aligns to 26:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G306), A293 (= A308), Y313 (= Y328), M315 (≠ L330), S316 (≠ T331), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W239), G290 (≠ A305), G312 (≠ V327), G314 (= G329), M315 (≠ L330), P320 (= P336), I321 (≠ T337)
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, 92% coverage: 42:540/541 of query aligns to 35:535/539 of P0DX84
- H231 (= H235) mutation to A: Retains 74% of wild-type activity.
- W235 (= W239) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A305) mutation to P: Almost completely abolishes the activity.
- G303 (= G306) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y328) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G335) 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)
31% identity, 92% coverage: 42:540/541 of query aligns to 35:535/538 of 6ijbB
- active site: T185 (= T191), H205 (≠ N211), H231 (= H235), S329 (≠ T331), E330 (= E332), K438 (≠ I444), W443 (≠ N449), A523 (≠ K528)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W239), G303 (= G306), A325 (≠ V327), W326 (≠ Y328), G327 (= G329), M328 (≠ L330)
- binding adenosine monophosphate: G303 (= G306), A304 (= A307), A305 (= A308), H324 (= H326), W326 (≠ Y328), G327 (= G329), M328 (≠ L330), S329 (≠ T331), Q359 (= Q361), D417 (= D423)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
31% identity, 92% coverage: 42:540/541 of query aligns to 35:532/533 of 6ihkB
- active site: T185 (= T191), H202 (≠ N211), H228 (= H235), S326 (≠ T331), E327 (= E332), K435 (≠ I444), W440 (≠ N449), K520 (= K528)
- binding adenosine-5'-diphosphate: H228 (= H235), G300 (= G306), A301 (= A307), A302 (= A308), H321 (= H326), A322 (≠ V327), W323 (≠ Y328), G324 (= G329), M325 (≠ L330), S326 (≠ T331), Q356 (= Q361), D414 (= D423), R429 (= R438), K520 (= K528)
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)
32% identity, 95% coverage: 25:537/541 of query aligns to 7:496/503 of P9WQ37
- R9 (≠ E27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (= R36) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K199) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ G222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ N224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C236) 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 (≠ G238) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F241) 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 (≠ K271) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G329) 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 (= W418) 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)
31% identity, 95% coverage: 25:537/541 of query aligns to 10:496/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 91% coverage: 47:541/541 of query aligns to 30:504/506 of 4gxqA
- active site: T163 (= T191), N183 (= N211), H207 (= H235), T303 (= T331), E304 (= E332), I403 (= I444), N408 (= N449), A491 (≠ K528)
- binding adenosine-5'-triphosphate: T163 (= T191), S164 (= S192), G165 (= G193), T166 (= T194), T167 (= T195), H207 (= H235), S277 (≠ A307), A278 (= A308), P279 (= P309), E298 (≠ H326), M302 (≠ L330), T303 (= T331), D382 (= D423), R397 (= R438)
- binding carbonate ion: H207 (= H235), S277 (≠ A307), R299 (≠ V327), G301 (= G329)
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)
28% identity, 98% coverage: 10:538/541 of query aligns to 35:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 95% coverage: 25:536/541 of query aligns to 9:508/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 191:195) binding
- H214 (= H235) binding ; mutation to A: Abolished activity.
- S289 (≠ A307) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AAP 307:309) binding
- EA 310:311 (≠ HV 326:327) binding
- M314 (≠ L330) binding
- T315 (= T331) binding
- H319 (vs. gap) 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.
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 95% coverage: 25:536/541 of query aligns to 9:503/506 of 5ie2A
- active site: T165 (= T191), S185 (≠ N215), H209 (= H235), T310 (= T331), E311 (= E332), N410 (≠ I444), K415 (≠ N449), K495 (= K528)
- binding adenosine-5'-triphosphate: T165 (= T191), S166 (= S192), G167 (= G193), T168 (= T194), T169 (= T195), S284 (≠ A307), A285 (= A308), S286 (≠ P309), Y307 (= Y328), A308 (≠ G329), M309 (≠ L330), T310 (= T331), D389 (= D423), L401 (≠ I435), R404 (= R438), K495 (= K528)
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
28% identity, 93% coverage: 32:536/541 of query aligns to 20:515/518 of 6m2uA
- active site: S176 (≠ T191), T196 (≠ L210), T324 (= T331), E325 (= E332), K422 (≠ I444), Y427 (≠ N449), K507 (= K528)
- binding adenosine monophosphate: G298 (= G306), E299 (≠ A307), A300 (= A308), D319 (≠ H326), G320 (≠ V327), I321 (≠ Y328), G322 (= G329), T324 (= T331), D401 (= D423), R416 (= R438), K422 (≠ I444), Y427 (≠ N449)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ N237), A297 (= A305), G322 (= G329), S323 (≠ L330), A328 (≠ G335)
Query Sequence
>WP_011385011.1 NCBI__GCF_000009985.1:WP_011385011.1
MSSNPYELGLDRNAANFVALTPLTFLERAAAVWPDRLAVIHGPVRRTWAETFVRCRKLAA
ALTARGIGLGDTVALMGANTPETFEAHFGVPLTGAVLNAINTRLDADAITFILNHAEAKI
LITDREFSPVVKKALAALGRTIPVIDIDDPQFKGGELLGEKNYEQLLDEAASEAPWTLPT
DEWQAIALNYTSGTTGNPKGVVYHHRGAHLNAVSNALSWQMGDNTVYLWTLPMFHCNGWC
FPWTMAVVAGTSVCLRHVRVDAIMGAIRDEKVTNFCGAPIVLNMINNAPAALKEGISHAV
KVMTAGAAPPAPVIAGMERMGWEVTHVYGLTECYGPTVQCVWHDKWNGLSIDEKAQIKAR
QGVRGPMLEGLMIADPISLEPAPKDGKTVGEIFMRGNNVMKGYLKNEKATEEAFAGGWFH
TGDLAVCHPDGYIEIKDRSKDIIISGGENISSIEVEDILYAHLAVLEAAVVARPDEKWGE
TPCAFIALKDGAEATEADIITFCRERMAHFKVPRTIVFGGLPKTSTGKVQKFMLRQKAKE
L
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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