SitesBLAST
Comparing BWI76_RS23695 FitnessBrowser__Koxy:BWI76_RS23695 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)
30% identity, 97% coverage: 8:509/518 of query aligns to 1:501/503 of P9WQ37
- R9 (≠ S16) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (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.
- K172 (= K170) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T193) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A195) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I207) 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 (≠ G209) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ A212) 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 (≠ N243) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G307) 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 (= W384) 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 (= D389) 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 (= R404) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R411) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G413) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K495) 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)
29% identity, 97% coverage: 8:509/518 of query aligns to 4:501/502 of 3r44A
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 95% coverage: 15:507/518 of query aligns to 8:483/484 of 5gtdA
- active site: T151 (= T162), S171 (≠ A182), H195 (= H206), T288 (= T309), E289 (= E310)
- binding adenosine-5'-monophosphate: G263 (≠ A282), G264 (= G283), Y285 (= Y306), G286 (= G307), M287 (≠ L308), T288 (= T309), D366 (= D389), V378 (≠ I401)
- binding magnesium ion: F314 (≠ P336), S315 (≠ G337)
- binding 2-succinylbenzoate: H195 (= H206), S197 (≠ T208), A237 (≠ G249), L260 (≠ A279), G262 (= G281), G263 (≠ A282), G286 (= G307), M287 (≠ L308), S292 (= S313), Q293 (≠ P314)
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)
29% identity, 95% coverage: 15:507/518 of query aligns to 8:483/485 of 5x8fB
- active site: T151 (= T162), S171 (≠ A182), H195 (= H206), T288 (= T309), E289 (= E310), I387 (≠ N410), N392 (≠ K415), K470 (= K495)
- binding magnesium ion: Y23 (≠ F30), E24 (= E31), H70 (≠ F78), N178 (≠ K189), L202 (= L213), L214 (= L226), T296 (≠ I317), L297 (≠ F318), S298 (≠ P319)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (= K93), L191 (≠ V202), P192 (= P203), H195 (= H206), I196 (= I207), S197 (≠ T208), A237 (≠ G249), V238 (≠ S250), L260 (≠ A279), G262 (= G281), G286 (= G307), M287 (≠ L308), S292 (= S313), Q293 (≠ P314), S388 (≠ R411), G389 (= G412), G390 (= G413), E391 (= E414), K420 (≠ V443), W421 (≠ Y444), K450 (≠ R475), Y451 (≠ F476)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 94% coverage: 15:502/518 of query aligns to 7:474/475 of 5burA
- active site: T150 (= T162), S170 (≠ A182), H194 (= H206), T287 (= T309), E288 (= E310)
- binding adenosine-5'-triphosphate: T150 (= T162), S151 (= S163), T153 (= T165), T154 (= T166), K158 (= K170), G263 (= G283), S283 (≠ I305), T287 (= T309), D365 (= D389), V377 (≠ I401), R380 (= R404)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 95% coverage: 15:507/518 of query aligns to 7:480/481 of 5busA
- active site: T150 (= T162), S170 (≠ A182), H194 (= H206), T287 (= T309), E288 (= E310)
- binding adenosine monophosphate: H194 (= H206), G262 (≠ A282), G263 (= G283), S283 (≠ I305), M286 (≠ L308), T287 (= T309), D365 (= D389), V377 (≠ I401), R380 (= R404), K467 (= K495)
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)
28% identity, 95% coverage: 7:499/518 of query aligns to 2:504/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 162:166) binding
- H214 (= H206) binding ; mutation to A: Abolished activity.
- S289 (≠ A282) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGH 282:284) binding
- E-A 310:311 (≠ QPI 303:305) binding
- M314 (≠ L308) binding
- T315 (= T309) binding
- H319 (≠ S313) binding ; mutation to A: Abolished activity.
- D394 (= D389) binding
- R409 (= R404) binding ; mutation to A: Abolished activity.
- K500 (= K495) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 95% coverage: 7:499/518 of query aligns to 2:497/504 of 5ie3A
- active site: T163 (= T162), S183 (≠ A182), H207 (= H206), T308 (= T309), E309 (= E310), N408 (= N410), K413 (= K415), K493 (= K495)
- binding adenosine monophosphate: S164 (= S163), S282 (≠ A282), A283 (≠ G283), S284 (≠ H284), Y305 (= Y306), A306 (≠ G307), M307 (≠ L308), T308 (= T309), D387 (= D389), L399 (≠ I401), R402 (= R404), K493 (= K495)
- binding oxalic acid: V208 (≠ I207), S282 (≠ A282), A306 (≠ G307), M307 (≠ L308), H312 (≠ S313), K493 (= K495)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 95% coverage: 7:499/518 of query aligns to 2:499/506 of 5ie2A
- active site: T165 (= T162), S185 (≠ A182), H209 (= H206), T310 (= T309), E311 (= E310), N410 (= N410), K415 (= K415), K495 (= K495)
- binding adenosine-5'-triphosphate: T165 (= T162), S166 (= S163), G167 (= G164), T168 (= T165), T169 (= T166), S284 (≠ A282), A285 (≠ G283), S286 (≠ H284), Y307 (= Y306), A308 (≠ G307), M309 (≠ L308), T310 (= T309), D389 (= D389), L401 (≠ I401), R404 (= R404), K495 (= K495)
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
32% identity, 65% coverage: 155:490/518 of query aligns to 162:494/504 of 6qjzA
- active site: T169 (= T162), S189 (≠ A182), H213 (= H206), T314 (= T309), E315 (= E310), N414 (= N410), K419 (= K415)
- binding adenosine monophosphate: H213 (= H206), S288 (≠ A282), A289 (≠ G283), S290 (≠ H284), A312 (≠ G307), M313 (≠ L308), T314 (= T309), D393 (= D389), L405 (≠ I401), K410 (= K406), K419 (= K415)
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 69% coverage: 146:501/518 of query aligns to 181:536/546 of Q84P21
- K530 (= K495) mutation to N: Lossed enzymatic activity.
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
26% identity, 96% coverage: 8:502/518 of query aligns to 22:550/561 of P69451
- Y213 (≠ F161) mutation to A: Loss of activity.
- T214 (= T162) mutation to A: 10% of wild-type activity.
- G216 (= G164) mutation to A: Decreases activity.
- T217 (= T165) mutation to A: Decreases activity.
- G219 (= G167) mutation to A: Decreases activity.
- K222 (= K170) mutation to A: Decreases activity.
- E361 (= E310) mutation to A: Loss of activity.
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)
24% identity, 92% coverage: 35:511/518 of query aligns to 64:556/556 of Q9S725
- K211 (= K170) mutation to S: Drastically reduces the activity.
- M293 (≠ H248) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ A279) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ H357) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W359) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R404) mutation to Q: Drastically reduces the activity.
- K457 (≠ G412) mutation to S: Drastically reduces the activity.
- K540 (= K495) mutation to N: Abolishes the activity.
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
28% identity, 95% coverage: 15:507/518 of query aligns to 7:471/473 of 5buqB
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 67% coverage: 154:502/518 of query aligns to 155:498/506 of 4gxqA
- active site: T163 (= T162), N183 (≠ A182), H207 (= H206), T303 (= T309), E304 (= E310), I403 (≠ N410), N408 (≠ K415), A491 (≠ K495)
- binding adenosine-5'-triphosphate: T163 (= T162), S164 (= S163), G165 (= G164), T166 (= T165), T167 (= T166), H207 (= H206), S277 (≠ A282), A278 (≠ G283), P279 (≠ H284), E298 (≠ Q303), M302 (≠ L308), T303 (= T309), D382 (= D389), R397 (= R404)
- binding carbonate ion: H207 (= H206), S277 (≠ A282), R299 (≠ P304), G301 (= G307)
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)
26% identity, 92% coverage: 35:511/518 of query aligns to 60:551/559 of Q67W82
- G395 (= G356) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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)
27% identity, 97% coverage: 3:502/518 of query aligns to 11:531/541 of Q5SKN9
- T184 (= T162) binding
- G302 (≠ A282) binding
- Q322 (≠ P304) binding
- G323 (≠ I305) binding
- T327 (= T309) binding
- E328 (= E310) binding
- D418 (= D389) binding
- K435 (= K406) binding
- K439 (≠ N410) binding
P38137 Oxalate--CoA ligase; Acyl-activating enzyme 3; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 70% coverage: 146:508/518 of query aligns to 181:536/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
26% identity, 96% coverage: 9:505/518 of query aligns to 22:537/539 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 (= H206), F245 (≠ T208), T249 (≠ A212), G314 (≠ A282), A315 (≠ G283), P316 (≠ H284), G337 (≠ I305), Y338 (= Y306), G339 (= G307), L340 (= L308), T341 (= T309), S345 (= S313), A346 (≠ P314), D420 (= D389), I432 (= I401), K527 (= K495)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ T208), R335 (≠ Q303), G337 (≠ I305), G339 (= G307), L340 (= L308), A346 (≠ P314)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
26% identity, 96% coverage: 9:505/518 of query aligns to 22:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H206), F245 (≠ T208), T249 (≠ A212), G314 (≠ A282), A315 (≠ G283), P316 (≠ H284), G337 (≠ I305), Y338 (= Y306), G339 (= G307), L340 (= L308), T341 (= T309), A346 (≠ P314), D420 (= D389), I432 (= I401), K527 (= K495)
Query Sequence
>BWI76_RS23695 FitnessBrowser__Koxy:BWI76_RS23695
MSSTSADFQNLYQALSRSAARSPDALALAFEDRRYLYRDFHLRVQRAMAQLDRIWSLRKG
DRILLAWGNHPAFCEVLFAALGLGIEVVPFSTKLKQAESEELVGHIAPRAVLFDATVQDW
LKQTPDALCVSLSEWQALSLPDPLTRLPTPVNRDDTAVMMFTSGTTGEPKGAIITHHNLL
CAIDAYAQKLNLTAADSTILAVPIYHITGLSALLALFISLGASLWLQHRFNAPQVINTLR
EQNITFLHGSPTIFILLCQAAREQSASHPGDFPALRTIACGAGHLSDGLIAELKTLFPHT
AIQPIYGLTETTSPATIFPGDVWGSDKCGSSGQAIPGLAIAIRNDRQQPLPAGQIGHIWL
KGDVVIREYWQHSERRPSCDAQGWFCTGDLGYLDDEGWLYIKDRSKDMINRGGEKIYSLE
LENILSTYRGVREVAVIPTPSPVYGEEPVAFIVPDGQHHLTSEEILGWLKVKIARFKLPA
RIIFTRVLPRTHNGKVSKQQLKARLAESIITLSTEDKK
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