SitesBLAST
Comparing 3607285 FitnessBrowser__Dino:3607285 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)
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)
32% identity, 99% coverage: 2:503/505 of query aligns to 3:498/503 of P9WQ37
- R9 (≠ Q8) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D16) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K164) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T188) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q190) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ G202) 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 (≠ G204) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ N207) 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 (= R238) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ R291) 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 (= W381) 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 (= D386) 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 (= R401) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S408) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G410) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K492) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 96% coverage: 15:499/505 of query aligns to 16:498/506 of 4gxqA
- active site: T163 (= T156), N183 (≠ M176), H207 (= H201), T303 (≠ G299), E304 (= E300), I403 (= I407), N408 (= N412), A491 (≠ K492)
- binding adenosine-5'-triphosphate: T163 (= T156), S164 (= S157), G165 (= G158), T166 (= T159), T167 (= T160), H207 (= H201), S277 (≠ G273), A278 (≠ G274), P279 (= P275), E298 (≠ Q294), M302 (≠ Q298), T303 (≠ G299), D382 (= D386), R397 (= R401)
- binding carbonate ion: H207 (= H201), S277 (≠ G273), R299 (≠ V295), G301 (= G297)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 99% coverage: 2:503/505 of query aligns to 6:498/502 of 3r44A
Sites not aligning to the query:
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, 98% coverage: 6:499/505 of query aligns to 7:477/485 of 5x8fB
- active site: T151 (= T156), S171 (≠ M176), H195 (= H201), T288 (≠ G299), E289 (= E300), I387 (= I407), N392 (= N412), K470 (= K492)
- binding magnesium ion: Y23 (≠ T22), E24 (≠ G23), H70 (≠ Y70), N178 (≠ D183), L202 (vs. gap), L214 (≠ V219), T296 (≠ A307), L297 (= L308), S298 (= S309)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (= K85), L191 (≠ A197), P192 (= P198), H195 (= H201), I196 (≠ G202), S197 (≠ A203), A237 (= A244), V238 (≠ A245), L260 (≠ V270), G262 (≠ A272), G286 (= G297), M287 (≠ Q298), S292 (≠ M303), Q293 (≠ S304), S388 (= S408), G389 (= G409), G390 (= G410), E391 (≠ S411), K420 (≠ E440), W421 (= W441), K450 (≠ R472), Y451 (≠ F473)
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)
29% identity, 98% coverage: 7:499/505 of query aligns to 29:550/561 of P69451
- Y213 (= Y155) mutation to A: Loss of activity.
- T214 (= T156) mutation to A: 10% of wild-type activity.
- G216 (= G158) mutation to A: Decreases activity.
- T217 (= T159) mutation to A: Decreases activity.
- G219 (= G161) mutation to A: Decreases activity.
- K222 (= K164) mutation to A: Decreases activity.
- E361 (≠ R310) mutation to A: Loss of activity.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
30% identity, 93% coverage: 30:499/505 of query aligns to 67:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 98% coverage: 6:499/505 of query aligns to 7:477/484 of 5gtdA
- active site: T151 (= T156), S171 (≠ M176), H195 (= H201), T288 (≠ G299), E289 (= E300)
- binding adenosine-5'-monophosphate: G263 (= G273), G264 (= G274), Y285 (= Y296), G286 (= G297), M287 (≠ Q298), T288 (≠ G299), D366 (= D386), V378 (≠ M398)
- binding magnesium ion: F314 (≠ T333), S315 (≠ I334)
- binding 2-succinylbenzoate: H195 (= H201), S197 (≠ A203), A237 (= A244), L260 (≠ V270), G262 (≠ A272), G263 (= G273), G286 (= G297), M287 (≠ Q298), S292 (≠ M303), Q293 (≠ S304)
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)
31% identity, 99% coverage: 1:501/505 of query aligns to 18:533/541 of Q5SKN9
- T184 (= T156) binding
- G302 (= G274) binding
- Q322 (= Q294) binding
- G323 (≠ V295) binding
- T327 (≠ G299) binding
- E328 (= E300) binding
- D418 (= D386) binding
- K435 (= K403) binding
- K439 (≠ I407) binding
3cw9A 4-chlorobenzoyl-coa ligase/synthetase in the thioester-forming conformation, bound to 4-chlorophenacyl-coa (see paper)
31% identity, 97% coverage: 7:498/505 of query aligns to 8:498/503 of 3cw9A
- active site: T161 (= T156), R181 (≠ M176), H207 (= H201), T307 (≠ G299), E308 (= E300), I406 (= I407), N411 (= N412), K492 (= K492)
- binding 4-Chlorophenacyl-coenzyme A: R87 (≠ K85), M203 (≠ A197), P204 (= P198), H207 (= H201), V208 (≠ G202), V209 (≠ A203), A280 (= A272), G305 (= G297), T306 (≠ Q298), M310 (= M303), N311 (≠ S304), S407 (= S408), G408 (= G409), G409 (= G410), E410 (≠ S411), W440 (= W441), F473 (= F473), R475 (= R475), K477 (= K477)
- binding adenosine monophosphate: T161 (= T156), G281 (= G273), A282 (≠ G274), T283 (≠ P275), I303 (≠ V295), Y304 (= Y296), G305 (= G297), T306 (≠ Q298), T307 (≠ G299), D385 (= D386), R400 (= R401), I406 (= I407), N411 (= N412)
3dlpX 4-chlorobenzoyl-coa ligase/synthetase, mutant d402p, bound to 4cb (see paper)
31% identity, 97% coverage: 7:498/505 of query aligns to 8:498/504 of 3dlpX
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
28% identity, 98% coverage: 6:499/505 of query aligns to 6:474/481 of 5busA
- active site: T150 (= T156), S170 (≠ M176), H194 (= H201), T287 (≠ G299), E288 (= E300)
- binding adenosine monophosphate: H194 (= H201), G262 (= G273), G263 (= G274), S283 (≠ V295), M286 (≠ Q298), T287 (≠ G299), D365 (= D386), V377 (≠ M398), R380 (= R401), K467 (= K492)
3cw8X 4-chlorobenzoyl-coa ligase/synthetase, bound to 4cba-adenylate (see paper)
31% identity, 97% coverage: 7:498/505 of query aligns to 8:497/501 of 3cw8X
- binding 5'-O-[(S)-{[(4-chlorophenyl)carbonyl]oxy}(hydroxy)phosphoryl]adenosine: H207 (= H201), V208 (≠ G202), V209 (≠ A203), G281 (= G273), A282 (≠ G274), T283 (≠ P275), I303 (≠ V295), Y304 (= Y296), G305 (= G297), T306 (≠ Q298), T307 (≠ G299), M310 (= M303), N311 (≠ S304), M324 (≠ S317), D385 (= D386)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
28% identity, 98% coverage: 6:499/505 of query aligns to 6:474/475 of 5burA
- active site: T150 (= T156), S170 (≠ M176), H194 (= H201), T287 (≠ G299), E288 (= E300)
- binding adenosine-5'-triphosphate: T150 (= T156), S151 (= S157), T153 (= T159), T154 (= T160), K158 (= K164), G263 (= G274), S283 (≠ V295), T287 (≠ G299), D365 (= D386), V377 (≠ M398), R380 (= R401)
1t5dX 4-chlorobenzoyl-coa ligase/synthetase bound to 4-chlorobenzoate (see paper)
30% identity, 97% coverage: 7:498/505 of query aligns to 8:496/502 of 1t5dX
2qvyX 4-chlorobenzoyl-coa ligase/synthetase, i303g mutation, bound to 3,4- dichlorobenzoate (see paper)
30% identity, 97% coverage: 7:498/505 of query aligns to 8:494/499 of 2qvyX
2qvxX 4-chlorobenzoyl-coa ligase/synthetase, i303g mutation, bound to 3- chlorobenzoate (see paper)
30% identity, 97% coverage: 7:498/505 of query aligns to 8:496/500 of 2qvxX
8pppA Amide bond synthetase from streptomyces hindustanus k492h mutant in complex with amp-cpp (see paper)
33% identity, 92% coverage: 35:501/505 of query aligns to 34:497/500 of 8pppA
5buqB Unliganded form of o-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, solved at 1.98 angstroms (see paper)
27% identity, 98% coverage: 6:499/505 of query aligns to 6:465/473 of 5buqB
5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 97% coverage: 7:495/505 of query aligns to 10:496/504 of 5ie3A
- active site: T163 (= T156), S183 (≠ T177), H207 (= H201), T308 (≠ G299), E309 (= E300), N408 (≠ I407), K413 (≠ N412), K493 (= K492)
- binding adenosine monophosphate: S164 (= S157), S282 (≠ V270), A283 (≠ Y271), S284 (≠ A272), Y305 (= Y296), A306 (≠ G297), M307 (≠ Q298), T308 (≠ G299), D387 (= D386), L399 (≠ M398), R402 (= R401), K493 (= K492)
- binding oxalic acid: V208 (≠ G202), S282 (≠ V270), A306 (≠ G297), M307 (≠ Q298), H312 (≠ A307), K493 (= K492)
5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 97% coverage: 7:495/505 of query aligns to 10:498/506 of 5ie2A
- active site: T165 (= T156), S185 (≠ T177), H209 (= H201), T310 (≠ G299), E311 (= E300), N410 (≠ I407), K415 (≠ N412), K495 (= K492)
- binding adenosine-5'-triphosphate: T165 (= T156), S166 (= S157), G167 (= G158), T168 (= T159), T169 (= T160), S284 (≠ V270), A285 (≠ Y271), S286 (≠ A272), Y307 (= Y296), A308 (≠ G297), M309 (≠ Q298), T310 (≠ G299), D389 (= D386), L401 (≠ M398), R404 (= R401), K495 (= K492)
Query Sequence
>3607285 FitnessBrowser__Dino:3607285
MNFALWLQRTAARCPDAPALYTGTRLETDYAGFADQAARIGAALSARGLGKGDRIGVFMK
NSTDYLRVLYGIWWCGAAAIPINSKLHPREAAWILSDAEAALCLVTPDLAEGLAEAAPDC
ACVVTGSAAFGEMLAAPPMAAPVARASGDLAWLFYTSGTTGKPKGVMMSFATLTAMTLSY
FVDVDEVTAQDAILYSAPMSHGAGVYNFMHVLRGARHVVPESGGFDPAEIFDLAREMRQV
SLFAAPTMVRRMIDVAKARGDTGDGIKTIVYAGGPMYLADIIEAVEVLGDRFVQVYGQGE
YPMSITALSRADVSDRSHPDWQARLASVGVAQTISDVAILDAEGRPVPPGETGEIAVRGA
GLMLGYWNRPEATAETIRDGWLWTGDMGRMDADGYVTMVDRSKDMIISGGSNVYPREVEE
VLLTHPQVAEVSVVGRPHAEWGEEVVAFVVPAPGAEMDPGVLDAHCLSQIARFKRPKAYI
ALPELPKNNYGKVLKIELRARLTKG
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