SitesBLAST
Comparing BPHYT_RS19375 FitnessBrowser__BFirm:BPHYT_RS19375 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)
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)
43% identity, 97% coverage: 18:576/576 of query aligns to 23:585/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
31% identity, 96% coverage: 22:576/576 of query aligns to 8:561/561 of P69451
- Y213 (≠ F223) mutation to A: Loss of activity.
- T214 (= T224) mutation to A: 10% of wild-type activity.
- G216 (= G226) mutation to A: Decreases activity.
- T217 (= T227) mutation to A: Decreases activity.
- G219 (= G229) mutation to A: Decreases activity.
- K222 (= K232) mutation to A: Decreases activity.
- E361 (= E369) mutation to A: Loss of activity.
6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
30% identity, 90% coverage: 33:548/576 of query aligns to 5:493/504 of 6qjzA
- active site: T169 (= T224), S189 (≠ N244), H213 (= H268), T314 (= T368), E315 (= E369), N414 (≠ I469), K419 (≠ N474)
- binding adenosine monophosphate: H213 (= H268), S288 (≠ P345), A289 (≠ I346), S290 (≠ E347), A312 (≠ G366), M313 (= M367), T314 (= T368), D393 (= D448), L405 (≠ I460), K410 (= K465), K419 (≠ N474)
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, 92% coverage: 33:563/576 of query aligns to 3:496/503 of P9WQ37
- R9 (= R39) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ D47) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K232) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S255) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ Q257) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C269) 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 (≠ G271) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L274) 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 (≠ Q306) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G366) 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 (= W443) 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 (= D448) 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 (= R463) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ R470) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G472) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K554) 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, 92% coverage: 33:563/576 of query aligns to 6:496/502 of 3r44A
Sites not aligning to the query:
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 88% coverage: 59:562/576 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T224), N183 (= N244), H207 (= H268), T303 (= T368), E304 (= E369), I403 (= I469), N408 (= N474), A491 (≠ K554)
- binding adenosine-5'-triphosphate: T163 (= T224), S164 (= S225), G165 (= G226), T166 (= T227), T167 (= T228), H207 (= H268), S277 (≠ G341), A278 (≠ S342), P279 (= P343), E298 (≠ I363), M302 (= M367), T303 (= T368), D382 (= D448), R397 (= R463)
- binding carbonate ion: H207 (= H268), S277 (≠ G341), R299 (≠ A364), G301 (= G366)
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)
29% identity, 93% coverage: 33:567/576 of query aligns to 5:513/514 of Q9SMT7
- TSGTT 170:174 (= TSGTT 224:228) binding
- H214 (= H268) binding ; mutation to A: Abolished activity.
- S289 (≠ A340) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ AGS 340:342) binding
- EA 310:311 (≠ IA 363:364) binding
- M314 (= M367) binding
- T315 (= T368) binding
- H319 (≠ P372) binding ; mutation to A: Abolished activity.
- D394 (= D448) binding
- R409 (= R463) binding ; mutation to A: Abolished activity.
- K500 (= K554) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 33:565/576 of query aligns to 5:504/504 of 5ie3A
- active site: T163 (= T224), S183 (≠ N244), H207 (= H268), T308 (= T368), E309 (= E369), N408 (≠ I469), K413 (≠ N474), K493 (= K554)
- binding adenosine monophosphate: S164 (= S225), S282 (≠ A340), A283 (≠ G341), S284 (= S342), Y305 (= Y365), A306 (≠ G366), M307 (= M367), T308 (= T368), D387 (= D448), L399 (≠ I460), R402 (= R463), K493 (= K554)
- binding oxalic acid: V208 (≠ C269), S282 (≠ A340), A306 (≠ G366), M307 (= M367), H312 (≠ P372), K493 (= K554)
5ie2A Crystal structure of a plant enzyme (see paper)
29% identity, 93% coverage: 33:565/576 of query aligns to 5:506/506 of 5ie2A
- active site: T165 (= T224), S185 (≠ N244), H209 (= H268), T310 (= T368), E311 (= E369), N410 (≠ I469), K415 (≠ N474), K495 (= K554)
- binding adenosine-5'-triphosphate: T165 (= T224), S166 (= S225), G167 (= G226), T168 (= T227), T169 (= T228), S284 (≠ A340), A285 (≠ G341), S286 (= S342), Y307 (= Y365), A308 (≠ G366), M309 (= M367), T310 (= T368), D389 (= D448), L401 (≠ I460), R404 (= R463), K495 (= K554)
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, 93% coverage: 31:563/576 of query aligns to 17:533/541 of Q5SKN9
- T184 (= T224) binding
- G302 (= G341) binding
- Q322 (≠ I363) binding
- G323 (≠ A364) binding
- T327 (= T368) binding
- E328 (= E369) binding
- D418 (= D448) binding
- K435 (= K465) binding
- K439 (≠ I469) binding
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
31% identity, 93% coverage: 33:568/576 of query aligns to 23:536/537 of 6e97B
- active site: S190 (≠ T224), S210 (≠ N244), H234 (= H268), A336 (≠ T368), E337 (= E369), N437 (≠ I469), K442 (≠ N474), K522 (= K554)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H268), N235 (≠ C269), F236 (= F270), S240 (≠ L274), G310 (= G341), A311 (≠ S342), K312 (≠ P343), V332 (≠ A364), F333 (≠ Y365), G334 (= G366), M335 (= M367), A336 (≠ T368), D416 (= D448), K433 (= K465), K442 (≠ N474)
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, 92% coverage: 37:568/576 of query aligns to 41:554/556 of Q9S725
- K211 (= K232) mutation to S: Drastically reduces the activity.
- M293 (≠ H311) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I338) mutation K->L,A: Affects the substrate specificity.
- E401 (= E416) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C418) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R463) mutation to Q: Drastically reduces the activity.
- K457 (≠ G471) mutation to S: Drastically reduces the activity.
- K540 (= K554) mutation to N: Abolishes the activity.
O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 87% coverage: 72:571/576 of query aligns to 40:511/512 of O74976
- S283 (≠ G341) modified: Phosphoserine
- S284 (= S342) modified: Phosphoserine
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)
29% identity, 93% coverage: 30:562/576 of query aligns to 3:531/543 of P38137
Sites not aligning to the query:
- 541:543 C-terminal peroxisome targeting signal (PTS1)
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, 88% coverage: 61:565/576 of query aligns to 59:537/546 of Q84P21
- K530 (= K554) mutation to N: Lossed enzymatic activity.
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 93% coverage: 24:561/576 of query aligns to 3:509/518 of 4wv3B
- active site: S175 (≠ T224), T320 (= T368), E321 (= E369), K418 (≠ I469), W423 (≠ N474), K502 (= K554)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H268), T221 (≠ C269), F222 (= F270), A293 (= A340), S294 (≠ G341), E295 (≠ S342), A296 (≠ P343), G316 (≠ A364), I317 (≠ Y365), G318 (= G366), C319 (≠ M367), T320 (= T368), D397 (= D448), H409 (≠ I460), R412 (= R463), K502 (= K554)
6e8oA Crystal structure of aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with amp
31% identity, 93% coverage: 33:568/576 of query aligns to 23:535/536 of 6e8oA
- active site: S190 (≠ T224), S210 (≠ N244), H234 (= H268), A336 (≠ T368), E337 (= E369), N437 (≠ I469), K442 (≠ N474), K521 (= K554)
- binding adenosine monophosphate: H234 (= H268), G310 (= G341), A311 (≠ S342), K312 (≠ P343), V332 (≠ A364), F333 (≠ Y365), G334 (= G366), M335 (= M367), A336 (≠ T368), D416 (= D448), V428 (≠ I460), K442 (≠ N474)
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)
28% identity, 92% coverage: 38:568/576 of query aligns to 15:537/539 of P0DX84
- H231 (= H268) mutation to A: Retains 74% of wild-type activity.
- W235 (≠ M272) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A340) mutation to P: Almost completely abolishes the activity.
- G303 (= G341) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y365) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P372) mutation to A: Retains 69% of wild-type activity.
- R432 (= R463) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K465) mutation to A: Retains 36% of wild-type activity.
- D435 (= D466) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I469) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G471) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G472) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E473) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N474) mutation to A: Retains 60% of wild-type activity.
- E474 (= E505) mutation to A: Retains 33% of wild-type activity.
- K523 (= K554) 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 (= K557) 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)
28% identity, 92% coverage: 38:568/576 of query aligns to 15:537/538 of 6ijbB
- active site: T185 (= T224), H205 (vs. gap), H231 (= H268), S329 (≠ T368), E330 (= E369), K438 (≠ I469), W443 (≠ N474), A523 (≠ K554)
- binding 3-(methylsulfanyl)propanoic acid: W235 (≠ M272), G303 (= G341), A325 (= A364), W326 (≠ Y365), G327 (= G366), M328 (= M367)
- binding adenosine monophosphate: G303 (= G341), A304 (≠ S342), A305 (≠ P343), H324 (≠ I363), W326 (≠ Y365), G327 (= G366), M328 (= M367), S329 (≠ T368), Q359 (≠ V390), D417 (= D448)
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
28% identity, 93% coverage: 28:562/576 of query aligns to 13:533/539 of 2d1sA
- active site: S194 (≠ T224), R214 (vs. gap), H241 (= H268), T339 (= T368), E340 (= E369), K439 (≠ I469), Q444 (≠ N474), K525 (= K554)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T224), S195 (= S225), H241 (= H268), F243 (= F270), T247 (vs. gap), I282 (≠ H311), G312 (= G341), A313 (≠ S342), P314 (= P343), Q334 (≠ I363), G335 (≠ A364), Y336 (= Y365), G337 (= G366), L338 (≠ M367), T339 (= T368), S343 (≠ P372), A344 (≠ V373), D418 (= D448), R433 (= R463), K525 (= K554)
Query Sequence
>BPHYT_RS19375 FitnessBrowser__BFirm:BPHYT_RS19375
MATHASGEGALIEPKDGLSYVRGSTDIPLSEATVGRFLRDTAASFPDRPAVVFREQLIRW
TWKEFAEEVDILAAGLLTLGIAKGDRVGIWSPNRVEWLLTQFATARIGAVLVNINPAYRL
AELEYALNKVGCKAIIAAERFKTSMYLEMLQALAPELATQAPGELHAARLPELRYVIRMC
DTETPGMLTFSDVIERGRVCLDVAKLDAIGATLSCHEPINIQFTSGTTGNPKGATLTHSN
VVNNARYIAMAMRLSEQDGLCIPVPLYHCFGMVLAVLACVSVGAKMVFPGEGFDPAATLA
AVAEEQCTALHGVPTMFIAELDHPNFATYDFSRLRTGIMAGSPCPIETMKKVVSRMHLSE
ITIAYGMTETSPVSFQSSTTDPLDKRTTTVGRIQPHLEVKIVDPLGAIVPVGETGELCTR
GYSVMQGYWGDEAKTRESIVDGWMHTGDLATLDAEGYCNIVGRLKDMLIRGGENIYPREI
EEFLFRHPKIQSVQVFGVPDTKYGEEVCAWVVLRSGEQVTAEEIQQFCHGQIAHYKVPKY
IRFVDELPMTVTGKVQKFIMREQMISELKLREDKTA
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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