SitesBLAST
Comparing CCNA_00192 FitnessBrowser__Caulo:CCNA_00192 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)
48% identity, 99% coverage: 4:539/539 of query aligns to 3:539/539 of P0DX84
- H231 (= H231) mutation to A: Retains 74% of wild-type activity.
- W235 (= W235) mutation to A: Almost completely abolishes the activity.
- G302 (= G302) mutation to P: Almost completely abolishes the activity.
- G303 (= G303) mutation to P: Almost completely abolishes the activity.
- W326 (= W326) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P333) mutation to A: Retains 69% of wild-type activity.
- R432 (= R433) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K435) mutation to A: Retains 36% of wild-type activity.
- D435 (= D436) mutation to A: Retains 76% of wild-type activity.
- K438 (= K439) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G441) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G442) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E443) mutation to A: Retains 27% of wild-type activity.
- W443 (= W444) mutation to A: Retains 60% of wild-type activity.
- E474 (= E475) mutation to A: Retains 33% of wild-type activity.
- K523 (= K523) 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 (= K526) 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)
47% identity, 99% coverage: 4:537/539 of query aligns to 3:537/538 of 6ijbB
- active site: T185 (= T185), H205 (= H205), H231 (= H231), S329 (≠ T329), E330 (= E330), K438 (= K439), W443 (= W444), A523 (≠ K523)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W235), G303 (= G303), A325 (≠ I325), W326 (= W326), G327 (= G327), M328 (= M328)
- binding adenosine monophosphate: G303 (= G303), A304 (≠ S304), A305 (= A305), H324 (≠ Q324), W326 (= W326), G327 (= G327), M328 (= M328), S329 (≠ T329), Q359 (= Q360), D417 (= D418)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
47% identity, 99% coverage: 4:535/539 of query aligns to 3:532/533 of 6ihkB
- active site: T185 (= T185), H202 (= H205), H228 (= H231), S326 (≠ T329), E327 (= E330), K435 (= K439), W440 (= W444), K520 (= K523)
- binding adenosine-5'-diphosphate: H228 (= H231), G300 (= G303), A301 (≠ S304), A302 (= A305), H321 (≠ Q324), A322 (≠ I325), W323 (= W326), G324 (= G327), M325 (= M328), S326 (≠ T329), Q356 (= Q360), D414 (= D418), R429 (= R433), K520 (= K523)
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, 100% coverage: 2:539/539 of query aligns to 9:540/541 of Q5SKN9
- T184 (= T185) binding
- G302 (= G303) binding
- Q322 (= Q324) binding
- G323 (≠ I325) binding
- T327 (= T329) binding
- E328 (= E330) binding
- D418 (= D418) binding
- K435 (= K435) binding
- K439 (= K439) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 100% coverage: 2:539/539 of query aligns to 2:509/510 of 1v26B
- active site: T177 (= T185), H197 (= H205), H223 (= H231), T320 (= T329), E321 (= E330), K432 (= K439), W437 (= W444)
- binding adenosine monophosphate: G295 (= G303), S296 (= S304), A297 (= A305), G316 (≠ I325), Y317 (≠ W326), G318 (= G327), L319 (≠ M328), T320 (= T329), D411 (= D418), K428 (= K435), K432 (= K439), W437 (= W444)
- binding magnesium ion: T177 (= T185), E321 (= E330)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
43% identity, 89% coverage: 2:481/539 of query aligns to 2:464/491 of 1v25A
- active site: T177 (= T185), H197 (= H205), H223 (= H231), T320 (= T329), E321 (= E330), K432 (= K439), W437 (= W444)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H231), V224 (≠ A232), G295 (= G303), S296 (= S304), A297 (= A305), Y317 (≠ W326), G318 (= G327), L319 (≠ M328), T320 (= T329), D411 (= D418), I423 (= I430), K432 (= K439), W437 (= W444)
- binding magnesium ion: T177 (= T185), E321 (= E330)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
38% identity, 91% coverage: 40:531/539 of query aligns to 35:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G302), G293 (= G303), A294 (≠ S304), A295 (= A305), G314 (≠ I325), Y315 (≠ W326), M317 (= M328), S318 (≠ T329), D408 (= D418), R423 (= R433)
- binding 4'-phosphopantetheine: R93 (= R98), P220 (≠ S228), H223 (= H231)
8i49A Acyl-acp synthetase structure bound to atp
38% identity, 91% coverage: 40:531/539 of query aligns to 35:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
38% identity, 91% coverage: 40:531/539 of query aligns to 35:527/530 of 8i22A
8i3iA Acyl-acp synthetase structure bound to amp-pnp
38% identity, 91% coverage: 40:531/539 of query aligns to 35:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T185), G174 (= G187), T175 (= T188), T176 (= T189), K180 (= K193), G293 (= G303), A294 (≠ S304), A295 (= A305), Y315 (≠ W326), M317 (= M328), S318 (≠ T329), D408 (= D418), R423 (= R433)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
38% identity, 91% coverage: 40:531/539 of query aligns to 35:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G302), G293 (= G303), A295 (= A305), G314 (≠ I325), Y315 (≠ W326), G316 (= G327), M317 (= M328), S318 (≠ T329), D408 (= D418), K429 (= K439)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H231), W227 (= W235), G292 (= G302), G316 (= G327), P322 (= P333)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R98), P220 (≠ S228), H223 (= H231), I269 (= I278), G432 (= G442)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
38% identity, 91% coverage: 40:531/539 of query aligns to 33:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G303), A293 (= A305), G312 (≠ I325), Y313 (≠ W326), G314 (= G327), M315 (= M328), S316 (≠ T329), D406 (= D418), R421 (= R433)
- binding magnesium ion: M315 (= M328), S316 (≠ T329), E317 (= E330)
8i51A Acyl-acp synthetase structure bound to amp-mc7
38% identity, 91% coverage: 40:531/539 of query aligns to 33:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G303), A293 (= A305), Y313 (≠ W326), M315 (= M328), S316 (≠ T329), D406 (= D418), R421 (= R433)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W235), G290 (= G302), G312 (≠ I325), G314 (= G327), M315 (= M328), P320 (= P333), I321 (= I334)
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: 40:534/539 of query aligns to 29:498/503 of P9WQ37
- K172 (= K193) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ T218) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ F220) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A232) 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 (= A234) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L237) 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 (≠ G268) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G327) 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 (≠ F413) 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 (= D418) 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 (= R433) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S440) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G442) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K523) 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: 40:534/539 of query aligns to 32:498/502 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)
27% identity, 92% coverage: 43:538/539 of query aligns to 30:485/485 of 5x8fB
- active site: T151 (= T185), S171 (≠ H205), H195 (= H231), T288 (= T329), E289 (= E330), I387 (≠ K439), N392 (≠ W444), K470 (= K523)
- binding magnesium ion: H70 (≠ P86), N178 (= N212), L202 (≠ P238), L214 (= L250), T296 (≠ V337), L297 (≠ A338), S298 (≠ T339)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R98), L191 (≠ S227), P192 (≠ S228), H195 (= H231), I196 (≠ A232), S197 (≠ T233), A237 (≠ T277), V238 (≠ I278), L260 (≠ V300), G262 (= G302), G286 (= G327), M287 (= M328), S292 (≠ P333), Q293 (≠ I334), S388 (= S440), G389 (= G441), G390 (= G442), E391 (= E443), K420 (= K472), W421 (= W473), K450 (= K504), Y451 (≠ W505)
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, 92% coverage: 43:537/539 of query aligns to 30:484/484 of 5gtdA
- active site: T151 (= T185), S171 (≠ H205), H195 (= H231), T288 (= T329), E289 (= E330)
- binding adenosine-5'-monophosphate: G263 (= G303), G264 (≠ S304), Y285 (≠ W326), G286 (= G327), M287 (= M328), T288 (= T329), D366 (= D418), V378 (≠ I430)
- binding magnesium ion: F314 (= F365), S315 (≠ G366)
- binding 2-succinylbenzoate: H195 (= H231), S197 (≠ T233), A237 (≠ T277), L260 (≠ V300), G262 (= G302), G263 (= G303), G286 (= G327), M287 (= M328), S292 (≠ P333), Q293 (≠ I334)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
27% identity, 92% coverage: 43:537/539 of query aligns to 29:481/481 of 5busA
- active site: T150 (= T185), S170 (≠ H205), H194 (= H231), T287 (= T329), E288 (= E330)
- binding adenosine monophosphate: H194 (= H231), G262 (= G303), G263 (≠ S304), S283 (≠ I325), M286 (= M328), T287 (= T329), D365 (= D418), V377 (≠ I430), R380 (= R433), K467 (= K523)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
27% identity, 91% coverage: 43:535/539 of query aligns to 29:475/475 of 5burA
- active site: T150 (= T185), S170 (≠ H205), H194 (= H231), T287 (= T329), E288 (= E330)
- binding adenosine-5'-triphosphate: T150 (= T185), S151 (= S186), T153 (= T188), T154 (= T189), K158 (= K193), G263 (≠ S304), S283 (≠ I325), T287 (= T329), D365 (= D418), V377 (≠ I430), R380 (= R433)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
30% identity, 92% coverage: 33:529/539 of query aligns to 46:530/536 of 5wm2A
- active site: S193 (≠ T185), N213 (≠ H205), H237 (≠ S228), A336 (≠ T329), E337 (= E330), N437 (≠ K439), K442 (≠ W444), K524 (= K523)
- binding adenosine monophosphate: G310 (= G303), S311 (= S304), K312 (≠ A305), V332 (≠ I325), F333 (≠ W326), G334 (= G327), M335 (= M328), A336 (≠ T329), E337 (= E330), D416 (= D418), V428 (≠ I430), K433 (= K435), K442 (≠ W444)
Query Sequence
>CCNA_00192 FitnessBrowser__Caulo:CCNA_00192
MIPGLMQTTPLMISGILTYAAQAHGAREIVSRLIDEPLHRYDYAGLAGRAAQAAHALRRL
GIKAGDRVTSLAWNTHRHLELFYAAPGIGAVLHTANPRLFDEQIVYTINHAESGVLFFER
NFQALVERIAPQLTTVKTFVMLSDAERTVPGAVGAISYETLIEGEPDVIAWPSFDENAGA
FLCYTSGTTGDPKGVLYSHRAVVLHAMAGGLNSAFGFTPFDVVMPCSSLYHATAWGLPFS
APICGAKLVLPADKMDGASLHQLIEGEGVTFTGGVPTIWTMYLDWLDKNDRRPDSLKKVV
IGGSAVPRAMAETFKRRYGVQTLQIWGMTETCPIGVVATPTPALAALGEEAMDEAIWTRQ
GRLQFGIELKVETEDGQAAPWDGETSGALLVRGPWVVKRYFRKDADAAREDGFFDTGDIA
TLDANGFMRITDRQKDVIKSGGEWISSIDLENVAVGCPGVKIAAVIGVPHPKWEERPLLV
IETHEGAEVTKAAVLDYLTPRIVKWWTPDDVVFATVPLTATGKIDKKVLRQAWKDHLIG
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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