SitesBLAST
Comparing Dsui_0644 FitnessBrowser__PS:Dsui_0644 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)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
54% identity, 96% coverage: 14:548/558 of query aligns to 7:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G311), G293 (= G312), A295 (= A314), G314 (= G333), Y315 (= Y334), G316 (= G335), M317 (= M336), S318 (= S337), D408 (= D427), K429 (= K448)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H242), W227 (= W246), G292 (= G311), G316 (= G335), P322 (= P341)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R100), P220 (= P239), H223 (= H242), I269 (= I288), G432 (= G451)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
54% identity, 96% coverage: 14:548/558 of query aligns to 7:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G311), G293 (= G312), A294 (≠ S313), A295 (= A314), G314 (= G333), Y315 (= Y334), M317 (= M336), S318 (= S337), D408 (= D427), R423 (= R442)
- binding 4'-phosphopantetheine: R93 (= R100), P220 (= P239), H223 (= H242)
8i49A Acyl-acp synthetase structure bound to atp
54% identity, 96% coverage: 14:548/558 of query aligns to 7:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
54% identity, 96% coverage: 14:548/558 of query aligns to 7:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
54% identity, 96% coverage: 14:548/558 of query aligns to 5:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G312), A293 (= A314), G312 (= G333), Y313 (= Y334), G314 (= G335), M315 (= M336), S316 (= S337), D406 (= D427), R421 (= R442)
- binding magnesium ion: M315 (= M336), S316 (= S337), E317 (= E338)
8i51A Acyl-acp synthetase structure bound to amp-mc7
54% identity, 96% coverage: 14:548/558 of query aligns to 5:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G312), A293 (= A314), Y313 (= Y334), M315 (= M336), S316 (= S337), D406 (= D427), R421 (= R442)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W246), G290 (= G311), G312 (= G333), G314 (= G335), M315 (= M336), P320 (= P341), I321 (= I342)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
54% identity, 96% coverage: 14:548/558 of query aligns to 7:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T191), G174 (= G193), T175 (= T194), T176 (= T195), K180 (= K199), G293 (= G312), A294 (≠ S313), A295 (= A314), Y315 (= Y334), M317 (= M336), S318 (= S337), D408 (= D427), R423 (= R442)
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, 91% coverage: 42:549/558 of query aligns to 47:533/541 of Q5SKN9
- T184 (= T191) binding
- G302 (= G312) binding
- Q322 (≠ T332) binding
- G323 (= G333) binding
- T327 (≠ S337) binding
- E328 (= E338) binding
- D418 (= D427) binding
- K435 (= K444) binding
- K439 (= K448) 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)
37% identity, 97% coverage: 14:553/558 of query aligns to 7:536/539 of P0DX84
- H231 (= H242) mutation to A: Retains 74% of wild-type activity.
- W235 (= W246) mutation to A: Almost completely abolishes the activity.
- G302 (= G311) mutation to P: Almost completely abolishes the activity.
- G303 (= G312) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y334) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P341) mutation to A: Retains 69% of wild-type activity.
- R432 (= R442) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K444) mutation to A: Retains 36% of wild-type activity.
- D435 (= D445) mutation to A: Retains 76% of wild-type activity.
- K438 (= K448) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G450) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G451) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E452) mutation to A: Retains 27% of wild-type activity.
- W443 (= W453) mutation to A: Retains 60% of wild-type activity.
- E474 (= E484) 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.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
37% identity, 96% coverage: 16:553/558 of query aligns to 9:536/538 of 6ijbB
- active site: T185 (= T191), H205 (= H211), H231 (= H242), S329 (= S337), E330 (= E338), K438 (= K448), W443 (= W453), A523 (≠ K540)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W246), G303 (= G312), A325 (≠ G333), W326 (≠ Y334), G327 (= G335), M328 (= M336)
- binding adenosine monophosphate: G303 (= G312), A304 (≠ S313), A305 (= A314), H324 (≠ T332), W326 (≠ Y334), G327 (= G335), M328 (= M336), S329 (= S337), Q359 (≠ T367), D417 (= D427)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 80% coverage: 42:490/558 of query aligns to 40:464/491 of 1v25A
- active site: T177 (= T191), H197 (= H211), H223 (= H242), T320 (≠ S337), E321 (= E338), K432 (= K448), W437 (= W453)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H242), V224 (= V243), G295 (= G312), S296 (= S313), A297 (= A314), Y317 (= Y334), G318 (= G335), L319 (≠ M336), T320 (≠ S337), D411 (= D427), I423 (= I439), K432 (= K448), W437 (= W453)
- binding magnesium ion: T177 (= T191), E321 (= E338)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 83% coverage: 42:506/558 of query aligns to 40:475/510 of 1v26B
- active site: T177 (= T191), H197 (= H211), H223 (= H242), T320 (≠ S337), E321 (= E338), K432 (= K448), W437 (= W453)
- binding adenosine monophosphate: G295 (= G312), S296 (= S313), A297 (= A314), G316 (= G333), Y317 (= Y334), G318 (= G335), L319 (≠ M336), T320 (≠ S337), D411 (= D427), K428 (= K444), K432 (= K448), W437 (= W453)
- binding magnesium ion: T177 (= T191), E321 (= E338)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
37% identity, 96% coverage: 16:553/558 of query aligns to 9:533/533 of 6ihkB
- active site: T185 (= T191), H202 (= H211), H228 (= H242), S326 (= S337), E327 (= E338), K435 (= K448), W440 (= W453), K520 (= K540)
- binding adenosine-5'-diphosphate: H228 (= H242), G300 (= G312), A301 (≠ S313), A302 (= A314), H321 (≠ T332), A322 (≠ G333), W323 (≠ Y334), G324 (= G335), M325 (= M336), S326 (= S337), Q356 (≠ T367), D414 (= D427), R429 (= R442), K520 (= K540)
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: 41:552/558 of query aligns to 28:499/503 of P9WQ37
- K172 (= K199) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ Q225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V243) 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 (= A245) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L248) 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 (= R278) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G335) 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 (≠ Y422) 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 (= D427) 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 (= R442) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ T449) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G451) 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)
29% identity, 92% coverage: 41:552/558 of query aligns to 31:499/502 of 3r44A
Sites not aligning to the query:
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
26% identity, 91% coverage: 44:551/558 of query aligns to 50:538/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H244), F245 (≠ W246), T249 (vs. gap), G314 (= G312), A315 (≠ S313), P316 (≠ A314), G337 (= G333), Y338 (= Y334), G339 (= G335), L340 (≠ M336), T341 (≠ S337), A346 (≠ I342), D420 (= D427), I432 (= I439), K527 (= K540)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
26% identity, 91% coverage: 44:551/558 of query aligns to 50:538/539 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 (= H244), F245 (≠ W246), T249 (vs. gap), G314 (= G312), A315 (≠ S313), P316 (≠ A314), G337 (= G333), Y338 (= Y334), G339 (= G335), L340 (≠ M336), T341 (≠ S337), S345 (≠ P341), A346 (≠ I342), D420 (= D427), I432 (= I439), K527 (= K540)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ W246), R335 (≠ F331), G337 (= G333), G339 (= G335), L340 (≠ M336), A346 (≠ I342)
Q17577 Acyl-CoA synthetase 7; EC 6.2.1.- from Caenorhabditis elegans (see paper)
25% identity, 92% coverage: 45:557/558 of query aligns to 48:539/540 of Q17577
- SS 186:187 (≠ TT 191:192) mutation to AA: Loss of catalytic activity; when associated with A-339.
- E339 (= E338) mutation to A: Severe loss of catalytic activity. Loss of catalytic activity; when associated with 186-A-A-187.
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)
27% identity, 91% coverage: 43:550/558 of query aligns to 64:550/556 of Q9S725
- K211 (= K199) mutation to S: Drastically reduces the activity.
- M293 (≠ H283) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I310) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ V397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R442) mutation to Q: Drastically reduces the activity.
- K457 (≠ G450) mutation to S: Drastically reduces the activity.
- K540 (= K540) mutation to N: Abolishes the activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
27% identity, 94% coverage: 31:555/558 of query aligns to 32:517/518 of 4wv3B
- active site: S175 (≠ T191), T320 (≠ S337), E321 (= E338), K418 (= K448), W423 (= W453), K502 (= K540)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (= F241), T221 (≠ H242), F222 (≠ V243), A293 (≠ G312), S294 (= S313), E295 (vs. gap), A296 (= A314), G316 (= G333), I317 (≠ Y334), G318 (= G335), C319 (≠ M336), T320 (≠ S337), D397 (= D427), H409 (≠ I439), R412 (= R442), K502 (= K540)
Query Sequence
>Dsui_0644 FitnessBrowser__PS:Dsui_0644
MPVQLIETTPSAYSYPLLIKHLLHTPLAHAPDQEIVYRDSVRYTYRTLQQRIGRLANALA
ALGVEPGHTVAMMDWDSHRYLECFFAVPMMGAVLQTVNVRLTAEQMLYTLNHARADVVLV
NSEFFPLLQAMAERLESVKTFVLIHGDHENPEKMQAPVSFAGEYEELLAAAATDYDFPDF
DENAKATTFYTTGTTGLPKGVYFSHRQLVMHTMGAATGLGTAPVQGRLHRDDVYMPITPM
FHVHAWGLPYVATMLGLKQVYPGRYQPEVLLRLKARERVTFSHCVPTILHMLLNHALARE
TDLSGWKVMIGGSALPQAMAVAALEKGIDVFTGYGMSETCPILSVAHLPTAKLQAPLAEQ
AALRARTGLPLPLVDLRIVDPEMRPQPHDGQAVGELVVRSPWLTQGYLKDPAAAEELWGG
GYLHTADIGNIDANGSIQITDRIKDVIKTGGEWTSSLQLEDIIGQHPAVHEVAVIGVKDE
KWGERPLALVVLKPEMEGQVTEHAIRNHAAHLAETLGVSRYGVLMQVSFVKTLARTSIGK
INKRFMRENLEAAKAAQP
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