SitesBLAST
Comparing WP_028315795.1 NCBI__GCF_000429905.1:WP_028315795.1 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)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 5:524/527 of 8jylA
- binding magnesium ion: S316 (= S332), E317 (= E333)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W241), G290 (= G306), G291 (= G307), A292 (= A308), A293 (= A309), G312 (≠ A328), Y313 (= Y329), G314 (= G330), M315 (= M331), S316 (= S332), I321 (≠ L337), D406 (= D422), R421 (= R437), K427 (= K443), W432 (= W448)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 7:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A294 (= A308), A295 (= A309), G314 (≠ A328), Y315 (= Y329), M317 (= M331), S318 (= S332), D408 (= D422), R423 (= R437)
- binding 4'-phosphopantetheine: R93 (= R98), P220 (= P234), H223 (= H237)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 5:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G307), A293 (= A309), G312 (≠ A328), Y313 (= Y329), G314 (= G330), M315 (= M331), S316 (= S332), D406 (= D422), R421 (= R437)
- binding magnesium ion: M315 (= M331), S316 (= S332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 5:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G307), A293 (= A309), Y313 (= Y329), M315 (= M331), S316 (= S332), D406 (= D422), R421 (= R437)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W241), G290 (= G306), G312 (≠ A328), G314 (= G330), M315 (= M331), P320 (= P336), I321 (≠ L337)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 7:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
53% identity, 97% coverage: 14:540/544 of query aligns to 7:526/530 of 8i22A
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 7:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G306), G293 (= G307), A295 (= A309), G314 (≠ A328), Y315 (= Y329), G316 (= G330), M317 (= M331), S318 (= S332), D408 (= D422), K429 (= K443)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H237), W227 (= W241), G292 (= G306), G316 (= G330), P322 (= P336)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R98), P220 (= P234), H223 (= H237), I269 (= I283), G432 (= G446)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
53% identity, 97% coverage: 14:540/544 of query aligns to 7:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T186), G174 (= G188), T175 (= T189), T176 (= T190), K180 (= K194), G293 (= G307), A294 (= A308), A295 (= A309), Y315 (= Y329), M317 (= M331), S318 (= S332), D408 (= D422), R423 (= R437)
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)
40% identity, 92% coverage: 42:542/544 of query aligns to 49:533/541 of Q5SKN9
- T184 (= T186) binding Mg(2+)
- G302 (= G307) binding tetradecanoyl-AMP
- Q322 (≠ S327) binding tetradecanoyl-AMP
- G323 (≠ A328) binding tetradecanoyl-AMP
- T327 (≠ S332) binding tetradecanoyl-AMP
- E328 (= E333) binding Mg(2+)
- D418 (= D422) binding tetradecanoyl-AMP
- K435 (= K439) binding tetradecanoyl-AMP
- K439 (= K443) binding tetradecanoyl-AMP
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)
41% identity, 97% coverage: 16:540/544 of query aligns to 9:530/539 of P0DX84
- H231 (= H237) mutation to A: Retains 74% of wild-type activity.
- W235 (= W241) mutation to A: Almost completely abolishes the activity.
- G302 (= G306) mutation to P: Almost completely abolishes the activity.
- G303 (= G307) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y329) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P336) mutation to A: Retains 69% of wild-type activity.
- R432 (= R437) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K439) mutation to A: Retains 36% of wild-type activity.
- D435 (= D440) mutation to A: Retains 76% of wild-type activity.
- K438 (= K443) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G445) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G446) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E447) mutation to A: Retains 27% of wild-type activity.
- W443 (= W448) mutation to A: Retains 60% of wild-type activity.
- E474 (= E479) mutation to A: Retains 33% of wild-type activity.
- K523 (= K533) 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 (= K536) 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)
40% identity, 97% coverage: 16:540/544 of query aligns to 9:530/538 of 6ijbB
- active site: T185 (= T186), H205 (= H206), H231 (= H237), S329 (= S332), E330 (= E333), K438 (= K443), W443 (= W448), A523 (≠ K533)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W241), G303 (= G307), A325 (= A328), W326 (≠ Y329), G327 (= G330), M328 (= M331)
- binding adenosine monophosphate: G303 (= G307), A304 (= A308), A305 (= A309), H324 (≠ S327), W326 (≠ Y329), G327 (= G330), M328 (= M331), S329 (= S332), Q359 (≠ T362), D417 (= D422)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
40% identity, 97% coverage: 16:540/544 of query aligns to 9:527/533 of 6ihkB
- active site: T185 (= T186), H202 (= H206), H228 (= H237), S326 (= S332), E327 (= E333), K435 (= K443), W440 (= W448), K520 (= K533)
- binding adenosine-5'-diphosphate: H228 (= H237), G300 (= G307), A301 (= A308), A302 (= A309), H321 (≠ S327), A322 (= A328), W323 (≠ Y329), G324 (= G330), M325 (= M331), S326 (= S332), Q356 (≠ T362), D414 (= D422), R429 (= R437), K520 (= K533)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 90% coverage: 42:529/544 of query aligns to 42:496/510 of 1v26B
- active site: T177 (= T186), H197 (= H206), H223 (= H237), T320 (≠ S332), E321 (= E333), K432 (= K443), W437 (= W448)
- binding adenosine monophosphate: G295 (= G307), S296 (≠ A308), A297 (= A309), G316 (≠ A328), Y317 (= Y329), G318 (= G330), L319 (≠ M331), T320 (≠ S332), D411 (= D422), K428 (= K439), K432 (= K443), W437 (= W448)
- binding magnesium ion: T177 (= T186), E321 (= E333)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 82% coverage: 42:485/544 of query aligns to 42:464/491 of 1v25A
- active site: T177 (= T186), H197 (= H206), H223 (= H237), T320 (≠ S332), E321 (= E333), K432 (= K443), W437 (= W448)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H237), V224 (= V238), G295 (= G307), S296 (≠ A308), A297 (= A309), Y317 (= Y329), G318 (= G330), L319 (≠ M331), T320 (≠ S332), D411 (= D422), I423 (= I434), K432 (= K443), W437 (= W448)
- binding magnesium ion: T177 (= T186), E321 (= E333)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 92% coverage: 42:540/544 of query aligns to 50:534/539 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 (= H239), F245 (≠ W241), T249 (≠ Y245), G314 (= G307), A315 (= A308), P316 (≠ A309), G337 (≠ A328), Y338 (= Y329), G339 (= G330), L340 (≠ M331), T341 (≠ S332), S345 (≠ P336), A346 (≠ L337), D420 (= D422), I432 (= I434), K527 (= K533)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ W241), R335 (≠ Y326), G337 (≠ A328), G339 (= G330), L340 (≠ M331), A346 (≠ L337)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 92% coverage: 42:540/544 of query aligns to 50:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H239), F245 (≠ W241), T249 (≠ Y245), G314 (= G307), A315 (= A308), P316 (≠ A309), G337 (≠ A328), Y338 (= Y329), G339 (= G330), L340 (≠ M331), T341 (≠ S332), A346 (≠ L337), D420 (= D422), I432 (= I434), K527 (= K533)
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, 92% coverage: 41:542/544 of query aligns to 64:549/556 of Q9S725
- K211 (= K194) mutation to S: Drastically reduces the activity.
- M293 (≠ H278) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I305) mutation K->L,A: Affects the substrate specificity.
- E401 (= E390) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V392) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R437) mutation to Q: Drastically reduces the activity.
- K457 (≠ G445) mutation to S: Drastically reduces the activity.
- K540 (= K533) mutation to N: Abolishes the 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: 37:542/544 of query aligns to 49:535/542 of O24146
- S189 (≠ T186) binding ATP
- S190 (≠ T187) binding ATP
- G191 (= G188) binding ATP
- T192 (= T189) binding ATP
- T193 (= T190) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K194) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H237) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ H239) 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 (≠ M243) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R259) binding CoA
- A309 (= A308) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ S327) binding ATP
- G332 (≠ A328) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S332) 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 (≠ L337) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ Q340) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D422) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R437) 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 (= K439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (= K443) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G445) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G446) binding CoA
- Q446 (≠ W448) binding AMP
- K526 (= K533) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 93% coverage: 37:542/544 of query aligns to 42:528/529 of 5bsvA
- active site: S182 (≠ T186), S202 (≠ H206), H230 (= H237), T329 (≠ S332), E330 (= E333), K434 (= K443), Q439 (≠ W448), K519 (= K533)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H237), Y232 (≠ H239), S236 (≠ M243), A302 (= A308), A303 (= A309), P304 (= P311), G325 (≠ A328), G327 (= G330), M328 (= M331), T329 (≠ S332), P333 (= P336), V334 (≠ L337), D413 (= D422), K430 (= K439), K434 (= K443), Q439 (≠ W448)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 93% coverage: 37:542/544 of query aligns to 42:528/529 of 5bsuA
- active site: S182 (≠ T186), S202 (≠ H206), H230 (= H237), T329 (≠ S332), E330 (= E333), K434 (= K443), Q439 (≠ W448), K519 (= K533)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H237), Y232 (≠ H239), S236 (≠ M243), M299 (≠ I305), A302 (= A308), A303 (= A309), P304 (= P311), G325 (≠ A328), G327 (= G330), M328 (= M331), T329 (≠ S332), P333 (= P336), D413 (= D422), K430 (= K439), K434 (= K443), Q439 (≠ W448)
Query Sequence
>WP_028315795.1 NCBI__GCF_000429905.1:WP_028315795.1
MSVRMIQKSPSAYGYPLLIKQLLATIYEPDQEIVYRDKMTYTYKDMEKRTRKLANALEGL
GITQGSTVAVMDWDSHRYLECFFAVPMMGAVLHTINIRLSPEQLVYTVNHAEDDIILVHK
DFAPLLEAVKDQLTTVKKFVLIADYEDAPATSLEFAGEYEDLVEAAGEEYEWPDFDENAM
ATMFYTTGTTGLPKGVYFSHRQLVLHTFGLMSAANSFRAQLKIDAGDVYMPLTPMFHVHA
WGMPYSMTVMGAKQIYPGRYEPELILKLYRDYKVSFSHCVPTILHMLLNSPSAKDTDFSG
WKMIIGGAALPKGMCIEGLKLGINIYSAYGMSETCPLLTQALLKPNMLDLPLEEQVVYRT
KTGLPCPGVQLRVVDPAGNPLPHDGKTAGEVVVRAPWLTQGYLNNPEKSEELWEKGWLHT
GDVGIIDELGYLQITDRIKDVIKTGGEWLSSLELESIISQHKGVSEVAVVGVKDDKWGER
PMALIVPKEGQELSKEEVQTFMGAWVENGAIPKYGIPESILFVDEIPKTSVGKIDKKEIR
AQQG
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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