SitesBLAST
Comparing Ga0059261_0337 FitnessBrowser__Korea:Ga0059261_0337 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)
46% identity, 99% coverage: 1:532/539 of query aligns to 1:534/539 of P0DX84
- H231 (= H230) mutation to A: Retains 74% of wild-type activity.
- W235 (= W234) mutation to A: Almost completely abolishes the activity.
- G302 (= G300) mutation to P: Almost completely abolishes the activity.
- G303 (= G301) mutation to P: Almost completely abolishes the activity.
- W326 (= W323) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P330) mutation to A: Retains 69% of wild-type activity.
- R432 (= R430) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K432) mutation to A: Retains 36% of wild-type activity.
- D435 (= D433) mutation to A: Retains 76% of wild-type activity.
- K438 (= K436) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G438) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G439) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E440) mutation to A: Retains 27% of wild-type activity.
- W443 (= W441) mutation to A: Retains 60% of wild-type activity.
- E474 (= E472) mutation to A: Retains 33% of wild-type activity.
- K523 (= K521) 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 (= K524) 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)
46% identity, 99% coverage: 1:532/539 of query aligns to 1:534/538 of 6ijbB
- active site: T185 (= T184), H205 (= H204), H231 (= H230), S329 (≠ T326), E330 (= E327), K438 (= K436), W443 (= W441), A523 (≠ K521)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W234), G303 (= G301), A325 (= A322), W326 (= W323), G327 (= G324), M328 (= M325)
- binding adenosine monophosphate: G303 (= G301), A304 (≠ S302), A305 (= A303), H324 (= H321), W326 (= W323), G327 (= G324), M328 (= M325), S329 (≠ T326), Q359 (= Q356), D417 (= D415)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
46% identity, 99% coverage: 1:532/539 of query aligns to 1:531/533 of 6ihkB
- active site: T185 (= T184), H202 (= H204), H228 (= H230), S326 (≠ T326), E327 (= E327), K435 (= K436), W440 (= W441), K520 (= K521)
- binding adenosine-5'-diphosphate: H228 (= H230), G300 (= G301), A301 (≠ S302), A302 (= A303), H321 (= H321), A322 (= A322), W323 (= W323), G324 (= G324), M325 (= M325), S326 (≠ T326), Q356 (= Q356), D414 (= D415), R429 (= R430), K520 (= K521)
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)
43% identity, 98% coverage: 5:534/539 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T184) binding
- G302 (= G301) binding
- Q322 (≠ H321) binding
- G323 (≠ A322) binding
- T327 (= T326) binding
- E328 (= E327) binding
- D418 (= D415) binding
- K435 (= K432) binding
- K439 (= K436) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 98% coverage: 5:534/539 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T184), H197 (= H204), H223 (= H230), T320 (= T326), E321 (= E327), K432 (= K436), W437 (= W441)
- binding adenosine monophosphate: G295 (= G301), S296 (= S302), A297 (= A303), G316 (≠ A322), Y317 (≠ W323), G318 (= G324), L319 (≠ M325), T320 (= T326), D411 (= D415), K428 (= K432), K432 (= K436), W437 (= W441)
- binding magnesium ion: T177 (= T184), E321 (= E327)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 98% coverage: 5:534/539 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T184), H197 (= H204), H223 (= H230), T320 (= T326), E321 (= E327), K432 (= K436), W437 (= W441)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H230), V224 (≠ A231), G295 (= G301), S296 (= S302), A297 (= A303), Y317 (≠ W323), G318 (= G324), L319 (≠ M325), T320 (= T326), D411 (= D415), I423 (= I427), K432 (= K436), W437 (= W441)
- binding magnesium ion: T177 (= T184), E321 (= E327)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
33% identity, 92% coverage: 35:528/539 of query aligns to 31:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G300), G293 (= G301), A295 (= A303), G314 (≠ A322), Y315 (≠ W323), G316 (= G324), M317 (= M325), S318 (≠ T326), D408 (= D415), K429 (= K436)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H230), W227 (= W234), G292 (= G300), G316 (= G324), P322 (= P330)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R97), P220 (= P227), H223 (= H230), I269 (≠ V276), G432 (= G439)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
34% identity, 91% coverage: 39:528/539 of query aligns to 33:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G301), A293 (= A303), G312 (≠ A322), Y313 (≠ W323), G314 (= G324), M315 (= M325), S316 (≠ T326), D406 (= D415), R421 (= R430)
- binding magnesium ion: M315 (= M325), S316 (≠ T326), E317 (= E327)
8i51A Acyl-acp synthetase structure bound to amp-mc7
34% identity, 91% coverage: 39:528/539 of query aligns to 33:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G301), A293 (= A303), Y313 (≠ W323), M315 (= M325), S316 (≠ T326), D406 (= D415), R421 (= R430)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W234), G290 (= G300), G312 (≠ A322), G314 (= G324), M315 (= M325), P320 (= P330), I321 (= I331)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
33% identity, 92% coverage: 35:528/539 of query aligns to 31:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G300), G293 (= G301), A294 (≠ S302), A295 (= A303), G314 (≠ A322), Y315 (≠ W323), M317 (= M325), S318 (≠ T326), D408 (= D415), R423 (= R430)
- binding 4'-phosphopantetheine: R93 (= R97), P220 (= P227), H223 (= H230)
8i49A Acyl-acp synthetase structure bound to atp
33% identity, 92% coverage: 35:528/539 of query aligns to 31:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
33% identity, 92% coverage: 35:528/539 of query aligns to 31:526/530 of 8i22A
8i3iA Acyl-acp synthetase structure bound to amp-pnp
34% identity, 92% coverage: 35:528/539 of query aligns to 31:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T184), G174 (= G186), T175 (= T187), T176 (= T188), K180 (= K192), G293 (= G301), A294 (≠ S302), A295 (= A303), Y315 (≠ W323), M317 (= M325), S318 (≠ T326), D408 (= D415), R423 (= R430)
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)
29% identity, 92% coverage: 36:533/539 of query aligns to 26:499/503 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 (≠ Q219) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A231) 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 (≠ G233) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ M236) 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 (≠ K266) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G324) 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 (= W410) 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 (= D415) 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 (= R430) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S437) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G439) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K521) 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, 92% coverage: 36:533/539 of query aligns to 29:499/502 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)
27% identity, 91% coverage: 41:533/539 of query aligns to 29:482/484 of 5gtdA
- active site: T151 (= T184), S171 (≠ A207), H195 (= H230), T288 (= T326), E289 (= E327)
- binding adenosine-5'-monophosphate: G263 (= G301), G264 (≠ S302), Y285 (≠ W323), G286 (= G324), M287 (= M325), T288 (= T326), D366 (= D415), V378 (≠ I427)
- binding magnesium ion: F314 (= F361), S315 (≠ G362)
- binding 2-succinylbenzoate: H195 (= H230), S197 (≠ V232), A237 (≠ G272), L260 (≠ T298), G262 (= G300), G263 (= G301), G286 (= G324), M287 (= M325), S292 (≠ P330), Q293 (≠ I331)
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)
27% identity, 91% coverage: 41:533/539 of query aligns to 29:482/485 of 5x8fB
- active site: T151 (= T184), S171 (≠ A207), H195 (= H230), T288 (= T326), E289 (= E327), I387 (≠ K436), N392 (≠ W441), K470 (= K521)
- binding magnesium ion: H70 (= H82), N178 (vs. gap), L202 (≠ P237), L214 (≠ M249), T296 (≠ M334), L297 (≠ G335), S298 (= S336)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R97), L191 (≠ V226), P192 (= P227), H195 (= H230), I196 (≠ A231), S197 (≠ V232), A237 (≠ G272), V238 (= V273), L260 (≠ T298), G262 (= G300), G286 (= G324), M287 (= M325), S292 (≠ P330), Q293 (≠ I331), S388 (= S437), G389 (= G438), G390 (= G439), E391 (= E440), K420 (= K469), W421 (= W470), K450 (= K501), Y451 (≠ W502)
Sites not aligning to the query:
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
26% identity, 91% coverage: 41:533/539 of query aligns to 28:479/481 of 5busA
- active site: T150 (= T184), S170 (≠ A207), H194 (= H230), T287 (= T326), E288 (= E327)
- binding adenosine monophosphate: H194 (= H230), G262 (= G301), G263 (≠ S302), S283 (≠ A322), M286 (= M325), T287 (= T326), D365 (= D415), V377 (≠ I427), R380 (= R430), K467 (= K521)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
26% identity, 91% coverage: 41:529/539 of query aligns to 28:475/475 of 5burA
- active site: T150 (= T184), S170 (≠ A207), H194 (= H230), T287 (= T326), E288 (= E327)
- binding adenosine-5'-triphosphate: T150 (= T184), S151 (= S185), T153 (= T187), T154 (= T188), K158 (= K192), G263 (≠ S302), S283 (≠ A322), T287 (= T326), D365 (= D415), V377 (≠ I427), R380 (= R430)
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)
24% identity, 90% coverage: 42:528/539 of query aligns to 66:547/556 of Q9S725
- K211 (= K192) mutation to S: Drastically reduces the activity.
- M293 (≠ A271) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ T298) mutation K->L,A: Affects the substrate specificity.
- E401 (≠ R384) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q386) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R430) mutation to Q: Drastically reduces the activity.
- K457 (≠ G438) mutation to S: Drastically reduces the activity.
- K540 (= K521) mutation to N: Abolishes the activity.
Query Sequence
>Ga0059261_0337 FitnessBrowser__Korea:Ga0059261_0337
MLGAMQDFELRVPRLIDHAEREYGDREIVSRWFDGSETRTNWAGIARDSRKLAQALERMG
IKKGDRVATMAMNHSRHLVAWHGTIGMGGVIHTINPRLFEDQLAFIGNHAEDRVLMYDRM
FQPIVDKMKPQWKTIEHYIVFDPGSEAGAGADGPDSFEAVIGAEDGNYAWVEGDEREPCM
LCYTSGTTGNPKGVLYTHRSSVIHAMAEIQPAVFDLSTQSVVLPVVPMFHAVGWGMPFAA
PMVGVKLVMSAINEGKVLCELMNREKVTHTAGVPTVWFAMFQHMDETGDVPAYLKVVTIG
GSAAPRAMIERIMKMGARVNHAWGMTETSPIGTMGSPSADWDDLSFEAKVDKMVCQGRAP
FGVELRTVDDAGNLLPRDGESSGRLQVRGPWIIKQYFKDESGPCLTADGWFDTGDVAVLH
PDGIMQITDRAKDVIKSGGEWISSVELENAAVGCPGVAEAAAIGIHHPKWDERPLLLVIR
KPGSEVTADQIQQHLAKHVAKWWLPDEIHFVEALPHTATGKLLKTAIRDQYKGFQFAAA
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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