SitesBLAST
Comparing WP_050464745.1 NCBI__GCF_001189915.1:WP_050464745.1 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: 23:539/545 of query aligns to 22:536/541 of Q5SKN9
- T184 (= T190) binding Mg(2+)
- G302 (= G305) binding tetradecanoyl-AMP
- Q322 (≠ H325) binding tetradecanoyl-AMP
- G323 (≠ S326) binding tetradecanoyl-AMP
- T327 (= T330) binding tetradecanoyl-AMP
- E328 (= E331) binding Mg(2+)
- D418 (= D422) binding tetradecanoyl-AMP
- K435 (= K439) binding tetradecanoyl-AMP
- K439 (≠ I443) binding tetradecanoyl-AMP
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)
33% identity, 91% coverage: 44:538/545 of query aligns to 39:534/539 of P0DX84
- H231 (= H234) mutation to A: Retains 74% of wild-type activity.
- W235 (= W238) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A304) mutation to P: Almost completely abolishes the activity.
- G303 (= G305) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y327) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G334) mutation to A: Retains 69% of wild-type activity.
- R432 (= R437) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K439) mutation to A: Retains 36% of wild-type activity.
- D435 (= D440) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I443) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G445) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G446) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E447) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N448) mutation to A: Retains 60% of wild-type activity.
- E474 (= E479) mutation to A: Retains 33% of wild-type activity.
- K523 (= K527) 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 (= K530) 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)
33% identity, 91% coverage: 44:538/545 of query aligns to 39:534/538 of 6ijbB
- active site: T185 (= T190), H205 (≠ N210), H231 (= H234), S329 (≠ T330), E330 (= E331), K438 (≠ I443), W443 (≠ N448), A523 (≠ K527)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W238), G303 (= G305), A325 (≠ S326), W326 (≠ Y327), G327 (= G328), M328 (≠ L329)
- binding adenosine monophosphate: G303 (= G305), A304 (= A306), A305 (≠ P307), H324 (= H325), W326 (≠ Y327), G327 (= G328), M328 (≠ L329), S329 (≠ T330), Q359 (= Q360), D417 (= D422)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 95% coverage: 19:535/545 of query aligns to 15:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G305), A293 (≠ P307), G312 (≠ S326), Y313 (= Y327), G314 (= G328), M315 (≠ L329), S316 (≠ T330), D406 (= D422), R421 (= R437)
- binding magnesium ion: M315 (≠ L329), S316 (≠ T330), E317 (= E331)
8i51A Acyl-acp synthetase structure bound to amp-mc7
31% identity, 95% coverage: 19:535/545 of query aligns to 15:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G305), A293 (≠ P307), Y313 (= Y327), M315 (≠ L329), S316 (≠ T330), D406 (= D422), R421 (= R437)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W238), G290 (≠ A304), G312 (≠ S326), G314 (= G328), M315 (≠ L329), P320 (≠ G334), I321 (≠ P335)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 93% coverage: 23:529/545 of query aligns to 15:502/510 of 1v26B
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T330), E321 (= E331), K432 (≠ I443), W437 (≠ N448)
- binding adenosine monophosphate: G295 (= G305), S296 (≠ A306), A297 (≠ P307), G316 (≠ S326), Y317 (= Y327), G318 (= G328), L319 (= L329), T320 (= T330), D411 (= D422), K428 (= K439), K432 (≠ I443), W437 (≠ N448)
- binding magnesium ion: T177 (= T190), E321 (= E331)
8jylA Acyl-acp synthetase structure bound to c10-ams
31% identity, 95% coverage: 19:535/545 of query aligns to 15:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T330), E317 (= E331)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W238), G290 (≠ A304), G291 (= G305), A292 (= A306), A293 (≠ P307), G312 (≠ S326), Y313 (= Y327), G314 (= G328), M315 (≠ L329), S316 (≠ T330), I321 (≠ P335), D406 (= D422), R421 (= R437), K427 (≠ I443), W432 (≠ N448)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
31% identity, 95% coverage: 19:535/545 of query aligns to 17:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ A304), G293 (= G305), A295 (≠ P307), G314 (≠ S326), Y315 (= Y327), G316 (= G328), M317 (≠ L329), S318 (≠ T330), D408 (= D422), K429 (≠ I443)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H234), W227 (= W238), G292 (≠ A304), G316 (= G328), P322 (≠ G334)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R102), P220 (= P231), H223 (= H234), I269 (≠ V280), G432 (= G446)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
31% identity, 95% coverage: 19:535/545 of query aligns to 17:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ A304), G293 (= G305), A294 (= A306), A295 (≠ P307), G314 (≠ S326), Y315 (= Y327), M317 (≠ L329), S318 (≠ T330), D408 (= D422), R423 (= R437)
- binding 4'-phosphopantetheine: R93 (= R102), P220 (= P231), H223 (= H234)
8i49A Acyl-acp synthetase structure bound to atp
31% identity, 95% coverage: 19:535/545 of query aligns to 17:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
31% identity, 95% coverage: 19:535/545 of query aligns to 17:527/530 of 8i22A
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
31% identity, 95% coverage: 19:535/545 of query aligns to 17:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T190), G174 (= G192), T175 (= T193), T176 (= T194), K180 (= K198), G293 (= G305), A294 (= A306), A295 (≠ P307), Y315 (= Y327), M317 (≠ L329), S318 (≠ T330), D408 (= D422), R423 (= R437)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 85% coverage: 23:485/545 of query aligns to 15:464/491 of 1v25A
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T330), E321 (= E331), K432 (≠ I443), W437 (≠ N448)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H234), V224 (≠ C235), G295 (= G305), S296 (≠ A306), A297 (≠ P307), Y317 (= Y327), G318 (= G328), L319 (= L329), T320 (= T330), D411 (= D422), I423 (= I434), K432 (≠ I443), W437 (≠ N448)
- binding magnesium ion: T177 (= T190), E321 (= E331)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 91% coverage: 44:538/545 of query aligns to 39:531/533 of 6ihkB
- active site: T185 (= T190), H202 (≠ N210), H228 (= H234), S326 (≠ T330), E327 (= E331), K435 (≠ I443), W440 (≠ N448), K520 (= K527)
- binding adenosine-5'-diphosphate: H228 (= H234), G300 (= G305), A301 (= A306), A302 (≠ P307), H321 (= H325), A322 (≠ S326), W323 (≠ Y327), G324 (= G328), M325 (≠ L329), S326 (≠ T330), Q356 (= Q360), D414 (= D422), R429 (= R437), K520 (= K527)
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: 22:536/545 of query aligns to 4:496/503 of P9WQ37
- R9 (= R27) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- R17 (= R35) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- K172 (= K198) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P221) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ H223) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C235) 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 (≠ G237) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F240) 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 (≠ G270) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G328) 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 (= W417) 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 (= D422) 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 (= R437) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S444) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G446) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K527) 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)
31% identity, 94% coverage: 22:536/545 of query aligns to 7:496/502 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, 94% coverage: 23:534/545 of query aligns to 6:477/485 of 5x8fB
- active site: T151 (= T190), S171 (≠ N210), H195 (= H234), T288 (= T330), E289 (= E331), I387 (= I443), N392 (= N448), K470 (= K527)
- binding magnesium ion: Y23 (≠ H40), E24 (≠ G41), H70 (≠ F87), N178 (≠ E217), L202 (≠ P241), L214 (≠ C253), T296 (≠ V338), L297 (≠ C339), S298 (≠ A340)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R102), L191 (= L230), P192 (= P231), H195 (= H234), I196 (≠ C235), S197 (≠ N236), A237 (= A276), V238 (= V280), L260 (≠ M302), G262 (≠ A304), G286 (= G328), M287 (≠ L329), S292 (≠ G334), Q293 (≠ P335), S388 (= S444), G389 (= G445), G390 (= G446), E391 (= E447), K420 (= K476), W421 (= W477), K450 (≠ G508), Y451 (≠ F509)
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, 94% coverage: 23:537/545 of query aligns to 40:550/556 of Q9S725
- K211 (= K198) mutation to S: Drastically reduces the activity.
- M293 (≠ C275) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V303) mutation K->L,A: Affects the substrate specificity.
- E401 (= E390) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ M392) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R437) mutation to Q: Drastically reduces the activity.
- K457 (≠ G445) mutation to S: Drastically reduces the activity.
- K540 (= K527) 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)
28% identity, 94% coverage: 23:534/545 of query aligns to 6:477/484 of 5gtdA
- active site: T151 (= T190), S171 (≠ N210), H195 (= H234), T288 (= T330), E289 (= E331)
- binding adenosine-5'-monophosphate: G263 (= G305), G264 (≠ A306), Y285 (= Y327), G286 (= G328), M287 (≠ L329), T288 (= T330), D366 (= D422), V378 (≠ I434)
- binding magnesium ion: F314 (≠ V362), S315 (≠ R363)
- binding 2-succinylbenzoate: H195 (= H234), S197 (≠ N236), A237 (= A276), L260 (≠ M302), G262 (≠ A304), G263 (= G305), G286 (= G328), M287 (≠ L329), S292 (≠ A340), Q293 (≠ E341)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
28% identity, 94% coverage: 23:534/545 of query aligns to 5:474/475 of 5burA
- active site: T150 (= T190), S170 (≠ N210), H194 (= H234), T287 (= T330), E288 (= E331)
- binding adenosine-5'-triphosphate: T150 (= T190), S151 (= S191), T153 (= T193), T154 (= T194), K158 (= K198), G263 (≠ A306), S283 (= S326), T287 (= T330), D365 (= D422), V377 (≠ I434), R380 (= R437)
Query Sequence
>WP_050464745.1 NCBI__GCF_001189915.1:WP_050464745.1
MPLDFNTGLGKNSANFAALSPIDYIARSAAVYGNRLAIVHGSLRQNWRDTYARARRLASA
LQRLGVGKGDTVAVMLPNTPAMVEAHFGVPMSGAVLNALNIRLDLASLAFMLRHGEARVL
LADSEFADLARQLVQQVPGLYVVAVNDLLGPDNVAPFGQTDYETLLAGGNPEFEWQLPDD
EWDAIALNYTSGTTGDPKGVVYHHRGAALNAISNILEWDMPRHAVYLWTLPMFHCNGWCF
PWTVAARAGVNVCLRKFEPKLVFDLIREHGVTHYCAAPIVHAALANAPEEWRAGIQHAVR
GMVAGAPPPAAVLARIEAMGFDLVHSYGLTEVYGPAAVCAEQEEWRALSQDERAGKKSRQ
GVRYHLQSAIAVLNPETMQAVAADGEEIGEIMFRGNICMKGYLKNETATHDAFAGGWFHT
GDLAVMYPDGYVKIKDRSKDIIISGGENISSVEVEDALYRHPAVLAAAVIAQPDPKWGET
PCAFVELKEGHDVSAEDLIAFCKNILAGFKAPKAIYFGPLPKTSTGKIQKFELRKRMRSD
SAIDV
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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