SitesBLAST
Comparing Dsui_2069 FitnessBrowser__PS:Dsui_2069 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)
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)
38% identity, 92% coverage: 42:527/529 of query aligns to 31:495/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ T227) 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 (≠ E229) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T232) 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 (≠ K263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G322) 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 (= W406) 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 (= D411) 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 (= R426) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S433) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (≠ A435) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K519) 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)
38% identity, 92% coverage: 42:527/529 of query aligns to 34:495/502 of 3r44A
Sites not aligning to the query:
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
33% identity, 96% coverage: 21:526/529 of query aligns to 48:542/559 of Q67W82
- G395 (= G378) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5ie2A Crystal structure of a plant enzyme (see paper)
32% identity, 99% coverage: 6:527/529 of query aligns to 5:503/506 of 5ie2A
- active site: T165 (= T182), S185 (≠ H202), H209 (= H226), T310 (= T324), E311 (= E325), N410 (= N432), K415 (≠ N437), K495 (= K519)
- binding adenosine-5'-triphosphate: T165 (= T182), S166 (= S183), G167 (= G184), T168 (= T185), T169 (= T186), S284 (≠ G298), A285 (= A299), S286 (= S300), Y307 (= Y321), A308 (≠ G322), M309 (≠ T323), T310 (= T324), D389 (= D411), L401 (≠ I423), R404 (= R426), K495 (= K519)
5ie3A Crystal structure of a plant enzyme (see paper)
32% identity, 99% coverage: 6:527/529 of query aligns to 5:501/504 of 5ie3A
- active site: T163 (= T182), S183 (≠ H202), H207 (= H226), T308 (= T324), E309 (= E325), N408 (= N432), K413 (≠ N437), K493 (= K519)
- binding adenosine monophosphate: S164 (= S183), S282 (≠ G298), A283 (= A299), S284 (= S300), Y305 (= Y321), A306 (≠ G322), M307 (≠ T323), T308 (= T324), D387 (= D411), L399 (≠ I423), R402 (= R426), K493 (= K519)
- binding oxalic acid: V208 (≠ T227), S282 (≠ G298), A306 (≠ G322), M307 (≠ T323), H312 (≠ P328), K493 (= K519)
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)
32% identity, 99% coverage: 6:527/529 of query aligns to 5:508/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 182:186) binding
- H214 (= H226) binding ; mutation to A: Abolished activity.
- S289 (≠ G298) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GAS 298:300) binding
- EA 310:311 (≠ QI 319:320) binding
- M314 (≠ T323) binding
- T315 (= T324) binding
- H319 (≠ P328) binding ; mutation to A: Abolished activity.
- D394 (= D411) binding
- R409 (= R426) binding ; mutation to A: Abolished activity.
- K500 (= K519) binding ; binding ; mutation to A: Abolished activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 96% coverage: 21:527/529 of query aligns to 34:527/528 of 3ni2A
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ A228), S236 (≠ T232), G302 (= G298), A303 (= A299), P304 (≠ S300), G325 (≠ I320), G327 (= G322), T329 (= T324), P333 (= P328), V334 (≠ C329), D413 (= D411), K430 (≠ D428), K434 (≠ N432), Q439 (≠ N437)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 96% coverage: 21:527/529 of query aligns to 34:527/528 of 3a9vA
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding adenosine monophosphate: H230 (= H226), G302 (= G298), A303 (= A299), P304 (≠ S300), Y326 (= Y321), G327 (= G322), M328 (≠ T323), T329 (= T324), D413 (= D411), K430 (≠ D428), K434 (≠ N432), Q439 (≠ N437)
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)
33% identity, 92% coverage: 42:528/529 of query aligns to 29:479/485 of 5x8fB
- active site: T151 (= T182), S171 (≠ H202), H195 (= H226), T288 (= T324), E289 (= E325), I387 (≠ N432), N392 (= N437), K470 (= K519)
- binding magnesium ion: H70 (≠ L83), N178 (≠ A209), L202 (≠ F234), L214 (= L246), T296 (≠ V332), L297 (= L333), S298 (≠ Y334)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R98), L191 (≠ A222), P192 (= P223), H195 (= H226), I196 (≠ T227), S197 (≠ A228), A237 (= A269), V238 (≠ A270), L260 (≠ E295), G262 (= G297), G286 (= G322), M287 (≠ T323), S292 (≠ P328), Q293 (≠ C329), S388 (= S433), G389 (= G434), G390 (≠ A435), E391 (= E436), K420 (≠ T465), W421 (= W466), K450 (≠ H499), Y451 (= Y500)
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)
30% identity, 99% coverage: 5:526/529 of query aligns to 36:547/556 of Q9S725
- K211 (= K190) mutation to S: Drastically reduces the activity.
- M293 (≠ F268) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ E295) mutation K->L,A: Affects the substrate specificity.
- E401 (= E379) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L381) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R426) mutation to Q: Drastically reduces the activity.
- K457 (≠ G434) mutation to S: Drastically reduces the activity.
- K540 (= K519) mutation to N: Abolishes the activity.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
33% identity, 92% coverage: 42:528/529 of query aligns to 29:479/484 of 5gtdA
- active site: T151 (= T182), S171 (≠ H202), H195 (= H226), T288 (= T324), E289 (= E325)
- binding adenosine-5'-monophosphate: G263 (= G298), G264 (≠ A299), Y285 (= Y321), G286 (= G322), M287 (≠ T323), T288 (= T324), D366 (= D411), V378 (≠ I423)
- binding magnesium ion: F314 (≠ L350), S315 (≠ N351)
- binding 2-succinylbenzoate: H195 (= H226), S197 (≠ A228), A237 (= A269), L260 (≠ E295), G262 (= G297), G263 (= G298), G286 (= G322), M287 (≠ T323), S292 (≠ P328), Q293 (≠ C329)
5zrnA Inhibitor bound crystal structure of n-terminal domain of facl13 from mycobacterium tuberculosis
37% identity, 73% coverage: 42:427/529 of query aligns to 31:398/398 of 5zrnA
- active site: T164 (= T182), A184 (= A204), H208 (= H226), T304 (= T324), E305 (= E325)
- binding 5'-O-{[(1R)-1-hydroxydodecyl]sulfamoyl}adenosine: W188 (≠ Q208), H208 (= H226), G279 (= G298), G300 (≠ I320), Y301 (= Y321), A302 (≠ G322), L303 (≠ T323), T304 (= T324), G308 (≠ P328), D382 (= D411)
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)
31% identity, 96% coverage: 18:526/529 of query aligns to 38:533/542 of O24146
- S189 (≠ T182) binding
- S190 (= S183) binding
- G191 (= G184) binding
- T192 (= T185) binding
- T193 (= T186) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K190) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H226) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ A228) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T232) binding ; binding ; binding
- K260 (≠ R249) binding
- A309 (≠ G298) binding ; binding ; binding
- Q331 (= Q319) binding
- G332 (≠ I320) binding ; binding ; binding ; binding ; binding
- T336 (= T324) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ C329) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M330) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D411) binding ; binding ; binding ; binding ; binding
- R435 (= R426) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (≠ D428) binding ; binding ; binding ; binding
- K441 (≠ N432) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G434) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (≠ A435) binding
- Q446 (≠ N437) binding
- K526 (= K519) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 96% coverage: 18:526/529 of query aligns to 31:526/530 of 5bsmA
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding adenosine-5'-triphosphate: S182 (≠ T182), S183 (= S183), G184 (= G184), T185 (= T185), T186 (= T186), K190 (= K190), H230 (= H226), A302 (≠ G298), A303 (= A299), P304 (≠ S300), Y326 (= Y321), G327 (= G322), M328 (≠ T323), T329 (= T324), D413 (= D411), I425 (= I423), R428 (= R426), K519 (= K519)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 96% coverage: 18:526/529 of query aligns to 30:525/528 of 5bsrA
- active site: S181 (≠ T182), S201 (≠ H202), H229 (= H226), T328 (= T324), E329 (= E325), K433 (≠ N432), Q438 (≠ N437), K518 (= K519)
- binding adenosine monophosphate: A301 (≠ G298), G326 (= G322), T328 (= T324), D412 (= D411), K429 (≠ D428), K433 (≠ N432), Q438 (≠ N437)
- binding coenzyme a: L102 (≠ R98), P226 (= P223), H229 (= H226), Y231 (≠ A228), F253 (= F250), K435 (≠ G434), G436 (≠ A435), F437 (≠ E436), F498 (≠ H499)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 96% coverage: 18:526/529 of query aligns to 31:526/529 of 5bsvA
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H226), Y232 (≠ A228), S236 (≠ T232), A302 (≠ G298), A303 (= A299), P304 (≠ S300), G325 (≠ I320), G327 (= G322), M328 (≠ T323), T329 (= T324), P333 (= P328), V334 (≠ C329), D413 (= D411), K430 (≠ D428), K434 (≠ N432), Q439 (≠ N437)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 96% coverage: 18:526/529 of query aligns to 31:526/529 of 5bsuA
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H226), Y232 (≠ A228), S236 (≠ T232), M299 (≠ E295), A302 (≠ G298), A303 (= A299), P304 (≠ S300), G325 (≠ I320), G327 (= G322), M328 (≠ T323), T329 (= T324), P333 (= P328), D413 (= D411), K430 (≠ D428), K434 (≠ N432), Q439 (≠ N437)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 96% coverage: 18:526/529 of query aligns to 31:526/529 of 5bstA
- active site: S182 (≠ T182), S202 (≠ H202), H230 (= H226), T329 (= T324), E330 (= E325), K434 (≠ N432), Q439 (≠ N437), K519 (= K519)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H226), Y232 (≠ A228), S236 (≠ T232), A302 (≠ G298), A303 (= A299), P304 (≠ S300), G325 (≠ I320), Y326 (= Y321), G327 (= G322), M328 (≠ T323), T329 (= T324), P333 (= P328), V334 (≠ C329), D413 (= D411), K430 (≠ D428), K434 (≠ N432), Q439 (≠ N437)
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)
33% identity, 100% coverage: 1:527/529 of query aligns to 14:532/541 of Q5SKN9
- T184 (= T182) binding
- G302 (= G298) binding
- Q322 (= Q319) binding
- G323 (≠ I320) binding
- T327 (= T324) binding
- E328 (= E325) binding
- D418 (= D411) binding
- K435 (≠ D428) binding
- K439 (≠ N432) binding
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
33% identity, 99% coverage: 6:527/529 of query aligns to 3:500/503 of 3cw9A
- active site: T161 (= T182), R181 (≠ H202), H207 (= H226), T307 (= T324), E308 (= E325), I406 (≠ N432), N411 (= N437), K492 (= K519)
- binding 4-Chlorophenacyl-coenzyme A: R87 (= R98), M203 (≠ A222), P204 (= P223), H207 (= H226), V208 (≠ T227), V209 (≠ A228), A280 (≠ G297), G305 (= G322), T306 (= T323), M310 (= M330), N311 (≠ S331), S407 (= S433), G408 (= G434), G409 (≠ A435), E410 (= E436), W440 (= W466), F473 (≠ Y500), R475 (= R502), K477 (≠ R504)
- binding adenosine monophosphate: T161 (= T182), G281 (= G298), A282 (= A299), T283 (≠ S300), I303 (= I320), Y304 (= Y321), G305 (= G322), T306 (= T323), T307 (= T324), D385 (= D411), R400 (= R426), I406 (≠ N432), N411 (= N437)
Query Sequence
>Dsui_2069 FitnessBrowser__PS:Dsui_2069
MSRGLTLGDTLSWPARYFPDKPALIAWEGGDHDTPAQRRVWTYAQLNAEVNRHAHALLAL
GVQKGDVVAAFLYNTPAFVFSLLAAARVGAVFNPINYRLAAQELAFILEDGQAKVLLFEK
EGCEVVEKAREHGVPTAHWIYADSDAAPAFATARLDQLVRHQPATLPPVIVEENDNCILM
YTSGTTGRPKGVLHTHRSKLAHNAMMHQAMTLSREDVGLAVAPLNHTAELHTSFLPRLQL
GATQVLLRRFDAGEAWRLTEVEKVTHFFAAPTMVTLLLHHPDVASRDLSSLRLVEYGGAS
MAPHLIREWDKKVGAGLVQIYGTTEMGPCMSVLYPHEQLSHAGSAGLPSLNHDLLVARVK
ADGSPSDPADLAAPDEVGEILVRGPCMMGGYLNRPEANARALAFGWYHTGDLGSLDKEGY
LWIRDRIDHMINSGAENVYPREVEDALVEHPGVLEVAVVGEPDDTWGQVVAAHVVAKPGA
TLTQEALDHFLLEGDRLAHYKRPRRYHFIEALPKTTSGKIQKHLLRQAG
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