SitesBLAST
Comparing CCNA_01889 FitnessBrowser__Caulo:CCNA_01889 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)
50% identity, 99% coverage: 1:540/544 of query aligns to 1:537/539 of P0DX84
- H231 (= H230) mutation to A: Retains 74% of wild-type activity.
- W235 (= W234) mutation to A: Almost completely abolishes the activity.
- G302 (= G305) mutation to P: Almost completely abolishes the activity.
- G303 (= G306) mutation to P: Almost completely abolishes the activity.
- W326 (= W329) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P336) mutation to A: Retains 69% of wild-type activity.
- R432 (= R435) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K437) mutation to A: Retains 36% of wild-type activity.
- D435 (= D438) mutation to A: Retains 76% of wild-type activity.
- K438 (= K441) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G443) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G444) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E445) mutation to A: Retains 27% of wild-type activity.
- W443 (= W446) mutation to A: Retains 60% of wild-type activity.
- E474 (= E477) mutation to A: Retains 33% of wild-type activity.
- K523 (= K526) 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 (= K529) 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, 99% coverage: 1:540/544 of query aligns to 1:537/538 of 6ijbB
- active site: T185 (= T184), H205 (= H204), H231 (= H230), S329 (≠ T332), E330 (= E333), K438 (= K441), W443 (= W446), A523 (≠ K526)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W234), G303 (= G306), A325 (= A328), W326 (= W329), G327 (= G330), M328 (= M331)
- binding adenosine monophosphate: G303 (= G306), A304 (≠ S307), A305 (= A308), H324 (= H327), W326 (= W329), G327 (= G330), M328 (= M331), S329 (≠ T332), Q359 (= Q362), D417 (= D420)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
50% identity, 99% coverage: 1:538/544 of query aligns to 1:532/533 of 6ihkB
- active site: T185 (= T184), H202 (= H204), H228 (= H230), S326 (≠ T332), E327 (= E333), K435 (= K441), W440 (= W446), K520 (= K526)
- binding adenosine-5'-diphosphate: H228 (= H230), G300 (= G306), A301 (≠ S307), A302 (= A308), H321 (= H327), A322 (= A328), W323 (= W329), G324 (= G330), M325 (= M331), S326 (≠ T332), Q356 (= Q362), D414 (= D420), R429 (= R435), K520 (= K526)
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)
45% identity, 98% coverage: 5:539/544 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T184) binding Mg(2+)
- G302 (= G306) binding tetradecanoyl-AMP
- Q322 (≠ H327) binding tetradecanoyl-AMP
- G323 (≠ A328) binding tetradecanoyl-AMP
- T327 (= T332) binding tetradecanoyl-AMP
- E328 (= E333) binding Mg(2+)
- D418 (= D420) binding tetradecanoyl-AMP
- K435 (= K437) binding tetradecanoyl-AMP
- K439 (= K441) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
43% identity, 98% coverage: 5:539/544 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T184), H197 (= H204), H223 (= H230), T320 (= T332), E321 (= E333), K432 (= K441), W437 (= W446)
- binding adenosine monophosphate: G295 (= G306), S296 (= S307), A297 (= A308), G316 (≠ A328), Y317 (≠ W329), G318 (= G330), L319 (≠ M331), T320 (= T332), D411 (= D420), K428 (= K437), K432 (= K441), W437 (= W446)
- binding magnesium ion: T177 (= T184), E321 (= E333)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 98% coverage: 5:539/544 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T184), H197 (= H204), H223 (= H230), T320 (= T332), E321 (= E333), K432 (= K441), W437 (= W446)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H230), V224 (= V231), G295 (= G306), S296 (= S307), A297 (= A308), Y317 (≠ W329), G318 (= G330), L319 (≠ M331), T320 (= T332), D411 (= D420), I423 (≠ L432), K432 (= K441), W437 (= W446)
- binding magnesium ion: T177 (= T184), E321 (= E333)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
35% identity, 97% coverage: 10:536/544 of query aligns to 10:521/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T184), G174 (= G186), T175 (= T187), T176 (= T188), K180 (= K192), G293 (= G306), A294 (≠ S307), A295 (= A308), Y315 (≠ W329), M317 (= M331), S318 (≠ T332), D408 (= D420), R423 (= R435)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 8:527/527 of 8jylA
- binding magnesium ion: S316 (≠ T332), E317 (= E333)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W234), G290 (= G305), G291 (= G306), A292 (≠ S307), A293 (= A308), G312 (≠ A328), Y313 (≠ W329), G314 (= G330), M315 (= M331), S316 (≠ T332), I321 (≠ L337), D406 (= D420), R421 (= R435), K427 (= K441), W432 (= W446)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 8:527/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G306), A293 (= A308), G312 (≠ A328), Y313 (≠ W329), G314 (= G330), M315 (= M331), S316 (≠ T332), D406 (= D420), R421 (= R435)
- binding magnesium ion: M315 (= M331), S316 (≠ T332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 8:527/528 of 8i51A
- binding adenosine monophosphate: G291 (= G306), A293 (= A308), Y313 (≠ W329), M315 (= M331), S316 (≠ T332), D406 (= D420), R421 (= R435)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W234), G290 (= G305), G312 (≠ A328), G314 (= G330), M315 (= M331), P320 (= P336), I321 (≠ L337)
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 10:529/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G305), G293 (= G306), A295 (= A308), G314 (≠ A328), Y315 (≠ W329), G316 (= G330), M317 (= M331), S318 (≠ T332), D408 (= D420), K429 (= K441)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H230), W227 (= W234), G292 (= G305), G316 (= G330), P322 (= P336)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R96), P220 (= P227), H223 (= H230), I269 (≠ V277), G432 (= G444)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 10:529/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G305), G293 (= G306), A294 (≠ S307), A295 (= A308), G314 (≠ A328), Y315 (≠ W329), M317 (= M331), S318 (≠ T332), D408 (= D420), R423 (= R435)
- binding 4'-phosphopantetheine: R93 (= R96), P220 (= P227), H223 (= H230)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
34% identity, 97% coverage: 10:536/544 of query aligns to 10:529/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
34% identity, 97% coverage: 10:536/544 of query aligns to 10:529/530 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)
30% identity, 93% coverage: 32:536/544 of query aligns to 23:497/503 of P9WQ37
- K172 (= K192) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S217) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R219) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V231) 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 (= A233) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ I236) 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 (= R267) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G330) 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 (= W415) 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 (= D420) 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 (= R435) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S442) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G444) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K526) 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)
29% identity, 93% coverage: 32:536/544 of query aligns to 26:497/502 of 3r44A
Sites not aligning to the query:
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
30% identity, 92% coverage: 35:533/544 of query aligns to 26:484/486 of 8wevA
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)
28% identity, 92% coverage: 33:533/544 of query aligns to 59:547/556 of Q9S725
- K211 (= K192) mutation to S: Drastically reduces the activity.
- M293 (≠ L272) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V304) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ D390) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q392) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R435) mutation to Q: Drastically reduces the activity.
- K457 (≠ G443) mutation to S: Drastically reduces the activity.
- K540 (= K526) mutation to N: Abolishes the activity.
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
29% identity, 91% coverage: 38:532/544 of query aligns to 53:530/535 of 5wm6A
- active site: S193 (≠ T184), N213 (≠ H204), H237 (= H230), A336 (≠ T332), E337 (= E333), N437 (≠ K441), K442 (≠ W446), K524 (= K526)
- binding magnesium ion: S301 (≠ A295), L303 (= L297), G326 (= G322)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ N232), G310 (= G306), S311 (= S307), K312 (≠ A308), V332 (≠ A328), F333 (≠ W329), G334 (= G330), M335 (= M331), A336 (≠ T332), D416 (= D420), K433 (= K437), K442 (≠ W446)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
29% identity, 91% coverage: 38:532/544 of query aligns to 53:530/536 of 5wm2A
- active site: S193 (≠ T184), N213 (≠ H204), H237 (= H230), A336 (≠ T332), E337 (= E333), N437 (≠ K441), K442 (≠ W446), K524 (= K526)
- binding adenosine monophosphate: G310 (= G306), S311 (= S307), K312 (≠ A308), V332 (≠ A328), F333 (≠ W329), G334 (= G330), M335 (= M331), A336 (≠ T332), E337 (= E333), D416 (= D420), V428 (≠ L432), K433 (= K437), K442 (≠ W446)
Query Sequence
>CCNA_01889 FitnessBrowser__Caulo:CCNA_01889
MLGLMQDTPLTLSSLLDHAARFHGEVEIVSREPGGVTRTNYARVAVRARKLAAALRRRGL
REGDRVASLALNSARHLELYYGATGAGGILNTVNPRLFPEQIAFILRHAENRIVFFDPAF
GPLLETLVDQAPQVEAYVCLSSAGDMPSLRLPNLIAYEDLLAPEADDAPWTVVSENAGAI
LCYTSGTTGDPKGVLYSHRSLALHAFVATGADGMAISRRDSILLVTPLFHVNAWGIPFSA
AMCGAKLVLPGAAVDGENLFNLMRAERCTFSLGVPTVWLGFLDYVATHREELDLAGLALE
RILVGGSAAPRSMIERFDYMLGVYVIHAWGMTETSPLATIGTPLPEHAFLDRQARYDIQA
LQGRAIYGVELRIVDADGVVAPHDGMAVGDLQVRGPWVVRRYFKADAPATTEDGWFPTGD
VAKIHPNGYLQLTDRSKDIIKSGGEWISSVDLENVAIAHPDIREAAVIGVPHPKWQERPL
LIIVPAPETTPDKDDILKFLASRVARWQVPDDVVIVESLPHTATGKLLKAKLRETYRDYL
AEPA
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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