SitesBLAST
Comparing GFF3502 FitnessBrowser__Phaeo:GFF3502 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)
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)
59% identity, 99% coverage: 1:536/539 of query aligns to 1:537/539 of P0DX84
- H231 (= H231) mutation to A: Retains 74% of wild-type activity.
- W235 (= W235) mutation to A: Almost completely abolishes the activity.
- G302 (= G302) mutation to P: Almost completely abolishes the activity.
- G303 (= G303) mutation to P: Almost completely abolishes the activity.
- W326 (= W326) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P333) mutation to A: Retains 69% of wild-type activity.
- R432 (= R432) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K434) mutation to A: Retains 36% of wild-type activity.
- D435 (= D435) mutation to A: Retains 76% of wild-type activity.
- K438 (= K438) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G440) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G441) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E442) mutation to A: Retains 27% of wild-type activity.
- W443 (= W443) mutation to A: Retains 60% of wild-type activity.
- E474 (= E474) mutation to A: Retains 33% of wild-type activity.
- K523 (= K522) 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 (= K525) 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)
59% identity, 99% coverage: 1:536/539 of query aligns to 1:537/538 of 6ijbB
- active site: T185 (= T185), H205 (= H205), H231 (= H231), S329 (≠ T329), E330 (= E330), K438 (= K438), W443 (= W443), A523 (≠ K522)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W235), G303 (= G303), A325 (= A325), W326 (= W326), G327 (= G327), M328 (= M328)
- binding adenosine monophosphate: G303 (= G303), A304 (≠ S304), A305 (= A305), H324 (= H324), W326 (= W326), G327 (= G327), M328 (= M328), S329 (≠ T329), Q359 (= Q359), D417 (= D417)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
59% identity, 99% coverage: 1:534/539 of query aligns to 1:532/533 of 6ihkB
- active site: T185 (= T185), H202 (= H205), H228 (= H231), S326 (≠ T329), E327 (= E330), K435 (= K438), W440 (= W443), K520 (= K522)
- binding adenosine-5'-diphosphate: H228 (= H231), G300 (= G303), A301 (≠ S304), A302 (= A305), H321 (= H324), A322 (= A325), W323 (= W326), G324 (= G327), M325 (= M328), S326 (≠ T329), Q356 (= Q359), D414 (= D417), R429 (= R432), K520 (= K522)
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)
43% identity, 98% coverage: 5:533/539 of query aligns to 13:535/541 of Q5SKN9
- T184 (= T185) binding
- G302 (= G303) binding
- Q322 (≠ H324) binding
- G323 (≠ A325) binding
- T327 (= T329) binding
- E328 (= E330) binding
- D418 (= D417) binding
- K435 (= K434) binding
- K439 (= K438) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 98% coverage: 5:533/539 of query aligns to 6:504/510 of 1v26B
- active site: T177 (= T185), H197 (= H205), H223 (= H231), T320 (= T329), E321 (= E330), K432 (= K438), W437 (= W443)
- binding adenosine monophosphate: G295 (= G303), S296 (= S304), A297 (= A305), G316 (≠ A325), Y317 (≠ W326), G318 (= G327), L319 (≠ M328), T320 (= T329), D411 (= D417), K428 (= K434), K432 (= K438), W437 (= W443)
- binding magnesium ion: T177 (= T185), E321 (= E330)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 98% coverage: 5:533/539 of query aligns to 6:485/491 of 1v25A
- active site: T177 (= T185), H197 (= H205), H223 (= H231), T320 (= T329), E321 (= E330), K432 (= K438), W437 (= W443)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H231), V224 (= V232), G295 (= G303), S296 (= S304), A297 (= A305), Y317 (≠ W326), G318 (= G327), L319 (≠ M328), T320 (= T329), D411 (= D417), I423 (= I429), K432 (= K438), W437 (= W443)
- binding magnesium ion: T177 (= T185), E321 (= E330)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
37% identity, 89% coverage: 49:530/539 of query aligns to 45:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T185), G174 (= G187), T175 (= T188), T176 (= T189), K180 (= K193), G293 (= G303), A294 (≠ S304), A295 (= A305), Y315 (≠ W326), M317 (= M328), S318 (≠ T329), D408 (= D417), R423 (= R432)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
37% identity, 89% coverage: 49:530/539 of query aligns to 43:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G303), A293 (= A305), G312 (≠ A325), Y313 (≠ W326), G314 (= G327), M315 (= M328), S316 (≠ T329), D406 (= D417), R421 (= R432)
- binding magnesium ion: M315 (= M328), S316 (≠ T329), E317 (= E330)
8i51A Acyl-acp synthetase structure bound to amp-mc7
37% identity, 89% coverage: 49:530/539 of query aligns to 43:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G303), A293 (= A305), Y313 (≠ W326), M315 (= M328), S316 (≠ T329), D406 (= D417), R421 (= R432)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W235), G290 (= G302), G312 (≠ A325), G314 (= G327), M315 (= M328), P320 (= P333), I321 (= I334)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
37% identity, 89% coverage: 49:530/539 of query aligns to 45:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G302), G293 (= G303), A295 (= A305), G314 (≠ A325), Y315 (≠ W326), G316 (= G327), M317 (= M328), S318 (≠ T329), D408 (= D417), K429 (= K438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H231), W227 (= W235), G292 (= G302), G316 (= G327), P322 (= P333)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R97), P220 (= P228), H223 (= H231), I269 (= I278), G432 (= G441)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
37% identity, 89% coverage: 49:530/539 of query aligns to 45:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G302), G293 (= G303), A294 (≠ S304), A295 (= A305), G314 (≠ A325), Y315 (≠ W326), M317 (= M328), S318 (≠ T329), D408 (= D417), R423 (= R432)
- binding 4'-phosphopantetheine: R93 (= R97), P220 (= P228), H223 (= H231)
8i49A Acyl-acp synthetase structure bound to atp
37% identity, 89% coverage: 49:530/539 of query aligns to 45:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
37% identity, 89% coverage: 49:530/539 of query aligns to 45:527/530 of 8i22A
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: 39:532/539 of query aligns to 29:497/503 of P9WQ37
- K172 (= K193) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R218) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V232) 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 (= A234) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T237) 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 (≠ K268) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G327) 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 (= W412) 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 (= D417) 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 (= R432) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S439) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G441) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K522) 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: 39:532/539 of query aligns to 32:497/502 of 3r44A
Sites not aligning to the query:
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)
26% identity, 93% coverage: 38:538/539 of query aligns to 62:556/556 of Q9S725
- K211 (= K193) mutation to S: Drastically reduces the activity.
- M293 (≠ L273) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I300) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ N387) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q389) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R432) mutation to Q: Drastically reduces the activity.
- K457 (≠ G440) mutation to S: Drastically reduces the activity.
- K540 (= K522) mutation to N: Abolishes the activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
27% identity, 91% coverage: 38:529/539 of query aligns to 34:509/518 of 4wv3B
- active site: S175 (≠ T185), T320 (= T329), E321 (= E330), K418 (= K438), W423 (= W443), K502 (= K522)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H231), T221 (vs. gap), F222 (≠ V232), A293 (≠ G302), S294 (≠ G303), E295 (≠ S304), A296 (= A305), G316 (≠ A325), I317 (≠ W326), G318 (= G327), C319 (≠ M328), T320 (= T329), D397 (= D417), H409 (≠ I429), R412 (= R432), K502 (= K522)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 97% coverage: 8:531/539 of query aligns to 16:528/528 of 3ni2A
- active site: S182 (≠ T185), S202 (= S202), H230 (= H231), T329 (= T329), E330 (= E330), K434 (= K438), Q439 (≠ W443), K519 (= K522)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ N233), S236 (≠ T237), G302 (= G303), A303 (≠ S304), P304 (≠ A305), G325 (≠ A325), G327 (= G327), T329 (= T329), P333 (= P333), V334 (≠ I334), D413 (= D417), K430 (= K434), K434 (= K438), Q439 (≠ W443)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 97% coverage: 8:531/539 of query aligns to 16:528/528 of 3a9vA
- active site: S182 (≠ T185), S202 (= S202), H230 (= H231), T329 (= T329), E330 (= E330), K434 (= K438), Q439 (≠ W443), K519 (= K522)
- binding adenosine monophosphate: H230 (= H231), G302 (= G303), A303 (≠ S304), P304 (≠ A305), Y326 (≠ W326), G327 (= G327), M328 (= M328), T329 (= T329), D413 (= D417), K430 (= K434), K434 (= K438), Q439 (≠ W443)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
27% identity, 98% coverage: 11:537/539 of query aligns to 26:534/539 of P40871
- G191 (≠ S186) binding
- HN 234:235 (≠ HV 231:232) binding
- S240 (≠ T237) binding
- G307 (= G303) binding
- V329 (≠ A325) binding
- D413 (= D417) binding
- R428 (= R432) binding
- K519 (= K522) binding ; binding
Query Sequence
>GFF3502 FitnessBrowser__Phaeo:GFF3502
MLGKMMHKQLTIGSLIEHAGRFHSSTTVTSVETSGETEHVTWGDIDANARKLAAALGRLG
IAQGARCGTIAWNNRRHLEIYFGVSGGGYVCHTINPRLKPEQLIYIINHAEDQVLFIDTT
FVPAVAQLRAQFTTVQHIVVMGPKDADIAAQIEGVLFYDDVLDAEAAGYDWPDLDENLPS
SLCYTSGTTGNPKGVEYTHRTSVLHTIGGNQPDGLALRARDTVLAVVPMFHVNAWGTPYM
TAAVGAKLVLPGPHLDGVSLARLIDAEKVTVALGVPTIWMGLLQGLEETGCTAESLERTI
VGGSALPTVMIPTFRDKYGVDLVHAWGMTETSPIGTLNQLLQKHNELDAEAQAKLREGQG
RPMYGIDLRIVDDSGAVLPHDGETQGNLQICGHWVIDSYFRAGETALTDDGWFDTGDVAT
IDDDGYMIIRDRSKDIIKSGGEWISTVELEDIAMSHPNIAQAAAIAAKHPKWDERPVVIA
VKRSGDVTEADLLAHYQGKVASWQIPDRVIFVESLPLGGTGKVQKNTLRERYEEILLDS
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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