SitesBLAST
Comparing AZOBR_RS06255 FitnessBrowser__azobra:AZOBR_RS06255 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)
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)
36% identity, 95% coverage: 27:548/551 of query aligns to 22:539/541 of Q5SKN9
- T184 (= T196) binding
- G302 (= G311) binding
- Q322 (≠ H331) binding
- G323 (≠ V332) binding
- T327 (= T336) binding
- E328 (= E337) binding
- D418 (= D428) binding
- K435 (= K445) binding
- K439 (≠ I449) 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)
32% identity, 96% coverage: 20:548/551 of query aligns to 7:539/539 of P0DX84
- H231 (= H240) mutation to A: Retains 74% of wild-type activity.
- W235 (= W244) mutation to A: Almost completely abolishes the activity.
- G302 (≠ T309) mutation to P: Almost completely abolishes the activity.
- G303 (≠ A310) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y333) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G340) mutation to A: Retains 69% of wild-type activity.
- R432 (= R443) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K445) mutation to A: Retains 36% of wild-type activity.
- D435 (= D446) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I449) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G451) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G452) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E453) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N454) mutation to A: Retains 60% of wild-type activity.
- E474 (= E485) mutation to A: Retains 33% of wild-type activity.
- K523 (= K533) 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 (= K536) mutation to A: Retains 48% of wild-type activity.
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 89% coverage: 28:515/551 of query aligns to 16:487/491 of 1v25A
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H240), V224 (≠ C241), G295 (= G311), S296 (≠ A312), A297 (= A313), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), I423 (≠ L440), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 92% coverage: 28:535/551 of query aligns to 16:502/510 of 1v26B
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding adenosine monophosphate: G295 (= G311), S296 (≠ A312), A297 (= A313), G316 (≠ V332), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), K428 (= K445), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
32% identity, 91% coverage: 45:544/551 of query aligns to 35:534/538 of 6ijbB
- active site: T185 (= T196), H205 (≠ N216), H231 (= H240), S329 (≠ T336), E330 (= E337), K438 (≠ I449), W443 (≠ N454), A523 (≠ K533)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W244), G303 (≠ A310), A325 (≠ V332), W326 (≠ Y333), G327 (= G334), M328 (≠ L335)
- binding adenosine monophosphate: G303 (≠ A310), A304 (≠ G311), A305 (= A312), H324 (= H331), W326 (≠ Y333), G327 (= G334), M328 (≠ L335), S329 (≠ T336), Q359 (= Q366), D417 (= D428)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 95% coverage: 20:544/551 of query aligns to 7:531/533 of 6ihkB
- active site: T185 (= T196), H202 (≠ N216), H228 (= H240), S326 (≠ T336), E327 (= E337), K435 (≠ I449), W440 (≠ N454), K520 (= K533)
- binding adenosine-5'-diphosphate: H228 (= H240), G300 (≠ A310), A301 (≠ G311), A302 (= A312), H321 (= H331), A322 (≠ V332), W323 (≠ Y333), G324 (= G334), M325 (≠ L335), S326 (≠ T336), Q356 (= Q366), D414 (= D428), R429 (= R443), K520 (= K533)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
29% identity, 93% coverage: 27:540/551 of query aligns to 14:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T196), G174 (= G198), T175 (= T199), T176 (= T200), K180 (= K204), G293 (= G311), A294 (= A312), A295 (= A313), Y315 (= Y333), M317 (≠ L335), S318 (≠ T336), D408 (= D428), R423 (= R443)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
29% identity, 93% coverage: 27:540/551 of query aligns to 12:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G311), A293 (= A313), G312 (≠ V332), Y313 (= Y333), G314 (= G334), M315 (≠ L335), S316 (≠ T336), D406 (= D428), R421 (= R443)
- binding magnesium ion: M315 (≠ L335), S316 (≠ T336), E317 (= E337)
8i51A Acyl-acp synthetase structure bound to amp-mc7
29% identity, 93% coverage: 27:540/551 of query aligns to 12:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G311), A293 (= A313), Y313 (= Y333), M315 (≠ L335), S316 (≠ T336), D406 (= D428), R421 (= R443)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W244), G290 (≠ A310), G312 (≠ V332), G314 (= G334), M315 (≠ L335), P320 (≠ G340), I321 (≠ P341)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
29% identity, 93% coverage: 27:540/551 of query aligns to 14:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A310), G293 (= G311), A295 (= A313), G314 (≠ V332), Y315 (= Y333), G316 (= G334), M317 (≠ L335), S318 (≠ T336), D408 (= D428), K429 (≠ I449)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H240), W227 (= W244), G292 (≠ A310), G316 (= G334), P322 (≠ G340)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R106), P220 (= P237), H223 (= H240), I269 (= I286), G432 (= G452)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
29% identity, 93% coverage: 27:540/551 of query aligns to 14:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A310), G293 (= G311), A294 (= A312), A295 (= A313), G314 (≠ V332), Y315 (= Y333), M317 (≠ L335), S318 (≠ T336), D408 (= D428), R423 (= R443)
- binding 4'-phosphopantetheine: R93 (= R106), P220 (= P237), H223 (= H240)
8i49A Acyl-acp synthetase structure bound to atp
29% identity, 93% coverage: 27:540/551 of query aligns to 14:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
29% identity, 93% coverage: 27:540/551 of query aligns to 14:526/530 of 8i22A
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, 94% coverage: 28:545/551 of query aligns to 7:499/503 of P9WQ37
- R9 (= R30) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (≠ Q38) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K204) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C241) 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 (≠ G243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ P247) 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 (≠ G276) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G334) 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 (= W423) 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 (= D428) 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 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K533) 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)
32% identity, 94% coverage: 28:545/551 of query aligns to 10:499/502 of 3r44A
Sites not aligning to the query:
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 93% coverage: 27:541/551 of query aligns to 6:478/484 of 5gtdA
- active site: T151 (= T196), S171 (≠ N216), H195 (= H240), T288 (= T336), E289 (= E337)
- binding adenosine-5'-monophosphate: G263 (≠ A312), G264 (≠ A313), Y285 (= Y333), G286 (= G334), M287 (≠ L335), T288 (= T336), D366 (= D428), V378 (≠ L440)
- binding magnesium ion: F314 (≠ A371), S315 (≠ T372)
- binding 2-succinylbenzoate: H195 (= H240), S197 (≠ N242), A237 (≠ G282), L260 (≠ T309), G262 (= G311), G263 (≠ A312), G286 (= G334), M287 (≠ L335), S292 (≠ G340), Q293 (≠ P341)
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)
28% identity, 93% coverage: 27:541/551 of query aligns to 6:478/485 of 5x8fB
- active site: T151 (= T196), S171 (≠ N216), H195 (= H240), T288 (= T336), E289 (= E337), I387 (= I449), N392 (= N454), K470 (= K533)
- binding magnesium ion: Y23 (≠ H44), E24 (≠ G45), H70 (≠ F91), N178 (≠ T223), L202 (≠ P247), L214 (≠ C259), T296 (≠ I344), L297 (≠ C345), S298 (≠ A346)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R106), L191 (= L236), P192 (= P237), H195 (= H240), I196 (≠ C241), S197 (≠ N242), A237 (≠ G282), V238 (≠ A283), L260 (≠ T309), G262 (= G311), G286 (= G334), M287 (≠ L335), S292 (≠ G340), Q293 (≠ P341), S388 (= S450), G389 (= G451), G390 (= G452), E391 (= E453), K420 (= K482), W421 (= W483), K450 (≠ H514), Y451 (≠ F515)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
28% identity, 93% coverage: 29:541/551 of query aligns to 7:475/475 of 5burA
- active site: T150 (= T196), S170 (≠ N216), H194 (= H240), T287 (= T336), E288 (= E337)
- binding adenosine-5'-triphosphate: T150 (= T196), S151 (= S197), T153 (= T199), T154 (= T200), K158 (= K204), G263 (≠ A313), S283 (≠ V332), T287 (= T336), D365 (= D428), V377 (≠ L440), R380 (= R443)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
28% identity, 93% coverage: 29:541/551 of query aligns to 7:475/481 of 5busA
- active site: T150 (= T196), S170 (≠ N216), H194 (= H240), T287 (= T336), E288 (= E337)
- binding adenosine monophosphate: H194 (= H240), G262 (≠ A312), G263 (≠ A313), S283 (≠ V332), M286 (≠ L335), T287 (= T336), D365 (= D428), V377 (≠ L440), R380 (= R443), K467 (= K533)
5ie3A Crystal structure of a plant enzyme (see paper)
31% identity, 93% coverage: 28:539/551 of query aligns to 9:499/504 of 5ie3A
- active site: T163 (= T196), S183 (≠ N216), H207 (= H240), T308 (= T336), E309 (= E337), N408 (≠ I449), K413 (≠ N454), K493 (= K533)
- binding adenosine monophosphate: S164 (= S197), S282 (≠ T309), A283 (= A310), S284 (≠ G311), Y305 (= Y333), A306 (≠ G334), M307 (≠ L335), T308 (= T336), D387 (= D428), L399 (= L440), R402 (= R443), K493 (= K533)
- binding oxalic acid: V208 (≠ C241), S282 (≠ T309), A306 (≠ G334), M307 (≠ L335), H312 (= H348), K493 (= K533)
Query Sequence
>AZOBR_RS06255 FitnessBrowser__azobra:AZOBR_RS06255
VTDARHNPYETDLDQNAANTVPLSPLSFLRRTAAVYPQRIAVIHGPVRRTWAETYERCVR
LASALAKRGIGLGDTVAVMAPNTPESFEAHFGVPMTGAVLNALNIRLDAEALAFILEHGE
AKVLLTDREFSGVISKAVHMLEPKRRPIVIDIDDPQAKGGELIGEQTYEQFLETGDPAYE
WPMPADEWQAIALNYTSGTTGNPKGVVYHHRGAYLNAMGNVLTWAMPHHPVYLWTLPMFH
CNGWCFPWTVTAMAGTNVCVRTITAKGIYDALADLGVTHMCGAPIIMGLIVNAPEDQKRE
IPRGVKMMTAGAAPPAAVIEKIERMGFDVTHVYGLTEVYGPVTICAWHEHWNDLPLEERA
ALKARQGVNYATLEGLMVADPNTLQPTRKDGVTMGEIFMRGNTVMKGYLKNPRATQEAFS
GGWFHTGDLGVWHADGYIELKDRSKDIIISGGENISTIEVESVLYKHPDIVEAAVVARPD
EKWGETPCAFVTVKEGKQLTEAEVIAYCREHLAHFKCPRTVVFTALPKTSTGKIQKYVLR
DQARALNGAKV
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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