SitesBLAST
Comparing Ac3H11_4302 FitnessBrowser__acidovorax_3H11:Ac3H11_4302 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)
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)
49% identity, 99% coverage: 7:545/546 of query aligns to 3:539/539 of P0DX84
- H231 (= H238) mutation to A: Retains 74% of wild-type activity.
- W235 (= W242) mutation to A: Almost completely abolishes the activity.
- G302 (= G309) mutation to P: Almost completely abolishes the activity.
- G303 (= G310) mutation to P: Almost completely abolishes the activity.
- W326 (= W333) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ A340) mutation to A: Retains 69% of wild-type activity.
- R432 (= R438) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K440) mutation to A: Retains 36% of wild-type activity.
- D435 (= D441) mutation to A: Retains 76% of wild-type activity.
- K438 (= K444) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G446) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G447) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E448) mutation to A: Retains 27% of wild-type activity.
- W443 (= W449) mutation to A: Retains 60% of wild-type activity.
- E474 (= E480) mutation to A: Retains 33% of wild-type activity.
- K523 (= K529) 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 (= K532) 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)
50% identity, 97% coverage: 7:536/546 of query aligns to 3:530/538 of 6ijbB
- active site: T185 (= T192), H205 (≠ S212), H231 (= H238), S329 (≠ T336), E330 (= E337), K438 (= K444), W443 (= W449), A523 (≠ K529)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W242), G303 (= G310), A325 (≠ G332), W326 (= W333), G327 (= G334), M328 (= M335)
- binding adenosine monophosphate: G303 (= G310), A304 (≠ S311), A305 (= A312), H324 (= H331), W326 (= W333), G327 (= G334), M328 (= M335), S329 (≠ T336), Q359 (= Q366), D417 (= D423)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
49% identity, 97% coverage: 7:536/546 of query aligns to 3:527/533 of 6ihkB
- active site: T185 (= T192), H202 (≠ S212), H228 (= H238), S326 (≠ T336), E327 (= E337), K435 (= K444), W440 (= W449), K520 (= K529)
- binding adenosine-5'-diphosphate: H228 (= H238), G300 (= G310), A301 (≠ S311), A302 (= A312), H321 (= H331), A322 (≠ G332), W323 (= W333), G324 (= G334), M325 (= M335), S326 (≠ T336), Q356 (= Q366), D414 (= D423), R429 (= R438), K520 (= K529)
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)
46% identity, 99% coverage: 6:545/546 of query aligns to 10:540/541 of Q5SKN9
- T184 (= T192) binding
- G302 (= G310) binding
- Q322 (≠ H331) binding
- G323 (= G332) binding
- T327 (= T336) binding
- E328 (= E337) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (= K444) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
45% identity, 99% coverage: 6:545/546 of query aligns to 3:509/510 of 1v26B
- active site: T177 (= T192), H197 (≠ S212), H223 (= H238), T320 (= T336), E321 (= E337), K432 (= K444), W437 (= W449)
- binding adenosine monophosphate: G295 (= G310), S296 (= S311), A297 (= A312), G316 (= G332), Y317 (≠ W333), G318 (= G334), L319 (≠ M335), T320 (= T336), D411 (= D423), K428 (= K440), K432 (= K444), W437 (= W449)
- binding magnesium ion: T177 (= T192), E321 (= E337)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
44% identity, 99% coverage: 6:545/546 of query aligns to 3:490/491 of 1v25A
- active site: T177 (= T192), H197 (≠ S212), H223 (= H238), T320 (= T336), E321 (= E337), K432 (= K444), W437 (= W449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H238), V224 (≠ I239), G295 (= G310), S296 (= S311), A297 (= A312), Y317 (≠ W333), G318 (= G334), L319 (≠ M335), T320 (= T336), D411 (= D423), I423 (= I435), K432 (= K444), W437 (= W449)
- binding magnesium ion: T177 (= T192), E321 (= E337)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
35% identity, 91% coverage: 43:539/546 of query aligns to 35:521/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T192), G174 (= G194), T175 (= T195), T176 (= T196), K180 (= K200), G293 (= G310), A294 (≠ S311), A295 (= A312), Y315 (≠ W333), M317 (= M335), S318 (≠ T336), D408 (= D423), R423 (= R438)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
34% identity, 91% coverage: 43:539/546 of query aligns to 35:529/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G309), G293 (= G310), A294 (≠ S311), A295 (= A312), G314 (= G332), Y315 (≠ W333), M317 (= M335), S318 (≠ T336), D408 (= D423), R423 (= R438)
- binding 4'-phosphopantetheine: R93 (= R101), P220 (= P235), H223 (= H238)
8i49A Acyl-acp synthetase structure bound to atp
34% identity, 91% coverage: 43:539/546 of query aligns to 35:529/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
34% identity, 91% coverage: 43:539/546 of query aligns to 35:529/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
34% identity, 91% coverage: 43:539/546 of query aligns to 33:527/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G310), A293 (= A312), G312 (= G332), Y313 (≠ W333), G314 (= G334), M315 (= M335), S316 (≠ T336), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (= M335), S316 (≠ T336), E317 (= E337)
8i51A Acyl-acp synthetase structure bound to amp-mc7
34% identity, 91% coverage: 43:539/546 of query aligns to 33:527/528 of 8i51A
- binding adenosine monophosphate: G291 (= G310), A293 (= A312), Y313 (≠ W333), M315 (= M335), S316 (≠ T336), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W242), G290 (= G309), G312 (= G332), G314 (= G334), M315 (= M335), P320 (≠ A340), I321 (= I341)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
34% identity, 91% coverage: 43:539/546 of query aligns to 35:529/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G309), G293 (= G310), A295 (= A312), G314 (= G332), Y315 (≠ W333), G316 (= G334), M317 (= M335), S318 (≠ T336), D408 (= D423), K429 (= K444)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H238), W227 (= W242), G292 (= G309), G316 (= G334), P322 (≠ A340)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R101), P220 (= P235), H223 (= H238), I269 (= I285), G432 (= G447)
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)
28% identity, 91% coverage: 43:541/546 of query aligns to 29:499/503 of P9WQ37
- K172 (= K200) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S225) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I239) 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 (= A241) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L244) 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 (= R275) 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 (= W418) 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 (= D423) 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 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K529) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
28% identity, 91% coverage: 43:541/546 of query aligns to 32:499/502 of 3r44A
Sites not aligning to the query:
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, 90% coverage: 44:536/546 of query aligns to 64:547/556 of Q9S725
- K211 (= K200) mutation to S: Drastically reduces the activity.
- M293 (≠ A280) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ R305) mutation K->L,A: Affects the substrate specificity.
- E401 (= E394) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ M396) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R438) mutation to Q: Drastically reduces the activity.
- K457 (≠ G446) mutation to S: Drastically reduces the activity.
- K540 (= K529) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 90% coverage: 44:537/546 of query aligns to 46:527/528 of 3ni2A
- active site: S182 (≠ T192), S202 (= S212), H230 (= H238), T329 (= T336), E330 (= E337), K434 (= K444), Q439 (≠ W449), K519 (= K529)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ N240), S236 (≠ C243), G302 (= G310), A303 (≠ S311), P304 (≠ A312), G325 (= G332), G327 (= G334), T329 (= T336), P333 (≠ A340), V334 (≠ I341), D413 (= D423), K430 (= K440), K434 (= K444), Q439 (≠ W449)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 90% coverage: 44:537/546 of query aligns to 46:527/528 of 3a9vA
- active site: S182 (≠ T192), S202 (= S212), H230 (= H238), T329 (= T336), E330 (= E337), K434 (= K444), Q439 (≠ W449), K519 (= K529)
- binding adenosine monophosphate: H230 (= H238), G302 (= G310), A303 (≠ S311), P304 (≠ A312), Y326 (≠ W333), G327 (= G334), M328 (= M335), T329 (= T336), D413 (= D423), K430 (= K440), K434 (= K444), Q439 (≠ W449)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
27% identity, 90% coverage: 46:538/546 of query aligns to 38:511/518 of 4wv3B
- active site: S175 (≠ T192), T320 (= T336), E321 (= E337), K418 (= K444), W423 (= W449), K502 (= K529)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H238), T221 (≠ I239), F222 (vs. gap), A293 (≠ G309), S294 (≠ G310), E295 (≠ S311), A296 (= A312), G316 (= G332), I317 (≠ W333), G318 (= G334), C319 (≠ M335), T320 (= T336), D397 (= D423), H409 (≠ I435), R412 (= R438), K502 (= K529)
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, 91% coverage: 46:542/546 of query aligns to 51:557/561 of P69451
- Y213 (= Y191) mutation to A: Loss of activity.
- T214 (= T192) mutation to A: 10% of wild-type activity.
- G216 (= G194) mutation to A: Decreases activity.
- T217 (= T195) mutation to A: Decreases activity.
- G219 (= G197) mutation to A: Decreases activity.
- K222 (= K200) mutation to A: Decreases activity.
- E361 (= E337) mutation to A: Loss of activity.
Query Sequence
>Ac3H11_4302 FitnessBrowser__acidovorax_3H11:Ac3H11_4302
MQQHQPGSMMDRPLLVSAILEHGENQYGDRQIVSRDTDGRLHRYRFADMAQRARQLASAL
QALGLRPGSVVGSLAWNNHRHLEAYYAVSGSGMVMHTCNPRLHPEQLAYIVNHADDEVVL
FDTTFAPLVRAIAASCPRVRHWVALCDADTLGTMDMQGVSGVEAYETLVASQNDRFTWPL
CDEKAGAALCYTSGTTGNPKGVLYSHRALVLSALSACMPGVLSISARETILPVVPMFHIN
AWCLPYAALIGGAKLVLPGPRLDAASLYELMETERVTVSAGVPTIWMGLIQHVEQHGLRF
TTMRRTGVGGSAMPKALIAKFNDLYDVEVRHGWGMTETTAIATMSVLGAGDAELPPEDRH
ALVAKQGKSVFGIELKLVDENGASLPRDGVAQGELMVRGQWIVDRYHKAERSALVDGWFP
TGDIATINPQGVVQIRDRTKDVIKSGGEWISSIDLENAAVAHPAVAMAAVIGVKHPKWDE
RPLLFIVRKPGQSLDKAQILDFLAQRVAKWWLPDDVLFVDSLPLGGTGKVQKNELRQSHG
AVFGGE
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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