SitesBLAST
Comparing GFF2396 FitnessBrowser__psRCH2:GFF2396 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)
47% identity, 98% coverage: 4:534/544 of query aligns to 3:537/539 of P0DX84
- H231 (= H228) mutation to A: Retains 74% of wild-type activity.
- W235 (= W232) mutation to A: Almost completely abolishes the activity.
- G302 (= G299) mutation to P: Almost completely abolishes the activity.
- G303 (= G300) 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 (= K520) 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 (= K523) 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, 98% coverage: 4:534/544 of query aligns to 3:537/538 of 6ijbB
- active site: T185 (= T182), H205 (= H202), H231 (= H228), S329 (≠ T326), E330 (= E327), K438 (= K436), W443 (= W441), A523 (≠ K520)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W232), G303 (= G300), A325 (≠ L322), W326 (= W323), G327 (= G324), M328 (= M325)
- binding adenosine monophosphate: G303 (= G300), A304 (≠ S301), A305 (= A302), H324 (≠ Q321), W326 (= W323), G327 (= G324), M328 (= M325), S329 (≠ T326), Q359 (= Q357), D417 (= D415)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
47% identity, 97% coverage: 4:532/544 of query aligns to 3:532/533 of 6ihkB
- active site: T185 (= T182), H202 (= H202), H228 (= H228), S326 (≠ T326), E327 (= E327), K435 (= K436), W440 (= W441), K520 (= K520)
- binding adenosine-5'-diphosphate: H228 (= H228), G300 (= G300), A301 (≠ S301), A302 (= A302), H321 (≠ Q321), A322 (≠ L322), W323 (= W323), G324 (= G324), M325 (= M325), S326 (≠ T326), Q356 (= Q357), D414 (= D415), R429 (= R430), K520 (= K520)
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)
42% identity, 98% coverage: 3:533/544 of query aligns to 10:537/541 of Q5SKN9
- T184 (= T182) binding
- G302 (= G300) binding
- Q322 (= Q321) binding
- G323 (≠ L322) 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: 3:533/544 of query aligns to 3:506/510 of 1v26B
- active site: T177 (= T182), H197 (= H202), H223 (= H228), T320 (= T326), E321 (= E327), K432 (= K436), W437 (= W441)
- binding adenosine monophosphate: G295 (= G300), S296 (= S301), A297 (= A302), G316 (≠ L322), Y317 (≠ W323), G318 (= G324), L319 (≠ M325), T320 (= T326), D411 (= D415), K428 (= K432), K432 (= K436), W437 (= W441)
- binding magnesium ion: T177 (= T182), E321 (= E327)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 98% coverage: 3:533/544 of query aligns to 3:487/491 of 1v25A
- active site: T177 (= T182), H197 (= H202), H223 (= H228), T320 (= T326), E321 (= E327), K432 (= K436), W437 (= W441)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H228), V224 (≠ G229), G295 (= G300), S296 (= S301), A297 (= A302), Y317 (≠ W323), G318 (= G324), L319 (≠ M325), T320 (= T326), D411 (= D415), I423 (= I427), K432 (= K436), W437 (= W441)
- binding magnesium ion: T177 (= T182), E321 (= E327)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
35% identity, 96% coverage: 8:528/544 of query aligns to 7:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G299), G293 (= G300), A295 (= A302), G314 (≠ L322), Y315 (≠ W323), G316 (= G324), M317 (= M325), S318 (≠ T326), D408 (= D415), K429 (= K436)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H228), W227 (= W232), G292 (= G299), G316 (= G324), P322 (= P330)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R98), P220 (≠ S225), H223 (= H228), I269 (= I275), G432 (= G439)
8i3iA Acyl-acp synthetase structure bound to amp-pnp
35% identity, 96% coverage: 8:528/544 of query aligns to 7:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T182), G174 (= G184), T175 (= T185), T176 (= T186), K180 (= K190), G293 (= G300), A294 (≠ S301), A295 (= A302), Y315 (≠ W323), M317 (= M325), S318 (≠ T326), D408 (= D415), R423 (= R430)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
35% identity, 96% coverage: 8:528/544 of query aligns to 7:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G299), G293 (= G300), A294 (≠ S301), A295 (= A302), G314 (≠ L322), Y315 (≠ W323), M317 (= M325), S318 (≠ T326), D408 (= D415), R423 (= R430)
- binding 4'-phosphopantetheine: R93 (= R98), P220 (≠ S225), H223 (= H228)
8i49A Acyl-acp synthetase structure bound to atp
35% identity, 96% coverage: 8:528/544 of query aligns to 7:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
35% identity, 96% coverage: 8:528/544 of query aligns to 7:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
35% identity, 96% coverage: 8:528/544 of query aligns to 5:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G300), A293 (= A302), G312 (≠ L322), 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
35% identity, 96% coverage: 8:528/544 of query aligns to 5:525/528 of 8i51A
- binding adenosine monophosphate: G291 (= G300), A293 (= A302), Y313 (≠ W323), M315 (= M325), S316 (≠ T326), D406 (= D415), R421 (= R430)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W232), G290 (= G299), G312 (≠ L322), G314 (= G324), M315 (= M325), P320 (= P330), I321 (≠ L331)
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, 90% coverage: 40:530/544 of query aligns to 29:497/503 of P9WQ37
- K172 (= K190) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ S215) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ F217) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ G229) 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 (= A231) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ I234) 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 (≠ G265) 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 (= K520) 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)
27% identity, 90% coverage: 40:530/544 of query aligns to 32:497/502 of 3r44A
Sites not aligning to the query:
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
27% identity, 90% coverage: 40:528/544 of query aligns to 64:571/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
5wm6A Crystal structure of cahj in complex with benzoyl adenylate (see paper)
30% identity, 93% coverage: 22:529/544 of query aligns to 36:533/535 of 5wm6A
- active site: S193 (≠ T182), N213 (≠ H202), H237 (≠ S225), A336 (≠ T326), E337 (= E327), N437 (≠ K436), K442 (≠ W441), K524 (= K520)
- binding magnesium ion: S301 (≠ G291), L303 (= L293), G326 (= G316)
- binding 5'-O-[(R)-(benzoyloxy)(hydroxy)phosphoryl]adenosine: F239 (≠ Y227), G310 (= G300), S311 (= S301), K312 (≠ A302), V332 (≠ L322), F333 (≠ W323), G334 (= G324), M335 (= M325), A336 (≠ T326), D416 (= D415), K433 (= K432), K442 (≠ W441)
5wm2A Crystal structure of cahj in complex with salicylic acid and amp (see paper)
30% identity, 93% coverage: 22:529/544 of query aligns to 36:533/536 of 5wm2A
- active site: S193 (≠ T182), N213 (≠ H202), H237 (≠ S225), A336 (≠ T326), E337 (= E327), N437 (≠ K436), K442 (≠ W441), K524 (= K520)
- binding adenosine monophosphate: G310 (= G300), S311 (= S301), K312 (≠ A302), V332 (≠ L322), F333 (≠ W323), G334 (= G324), M335 (= M325), A336 (≠ T326), E337 (= E327), D416 (= D415), V428 (≠ I427), K433 (= K432), K442 (≠ W441)
5wm3A Crystal structure of cahj in complex with salicyl adenylate (see paper)
30% identity, 93% coverage: 22:529/544 of query aligns to 36:533/537 of 5wm3A
- active site: S193 (≠ T182), N213 (≠ H202), H237 (≠ S225), A336 (≠ T326), E337 (= E327), N437 (≠ K436), K442 (≠ W441), K524 (= K520)
- binding 9-(5-O-{(S)-hydroxy[(2-hydroxybenzene-1-carbonyl)oxy]phosphoryl}-alpha-L-lyxofuranosyl)-9H-purin-6-amine: N238 (≠ L226), F239 (≠ Y227), G310 (= G300), S311 (= S301), K312 (≠ A302), V332 (≠ L322), F333 (≠ W323), G334 (= G324), M335 (= M325), A336 (≠ T326), D416 (= D415), K433 (= K432), K442 (≠ W441)
- binding magnesium ion: S301 (≠ G291), L303 (= L293), G326 (= G316)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
30% identity, 91% coverage: 40:534/544 of query aligns to 47:536/537 of 6e97B
- active site: S190 (≠ T182), S210 (≠ H202), H234 (≠ S225), A336 (≠ T326), E337 (= E327), N437 (≠ K436), K442 (≠ W441), K522 (= K520)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (≠ S225), N235 (≠ L226), F236 (≠ Y227), S240 (≠ A231), G310 (= G300), A311 (≠ S301), K312 (≠ A302), V332 (≠ L322), F333 (≠ W323), G334 (= G324), M335 (= M325), A336 (≠ T326), D416 (= D415), K433 (= K432), K442 (≠ W441)
Query Sequence
>GFF2396 FitnessBrowser__psRCH2:GFF2396
MQPGLMQNAPLLISSIVTHAARAHGDREIVSRLVDEPLWRYDYACLAARSAQAASMLGKL
GIGPGDCVSSLAWNTHRHYELFFAVPGIGAVLHTANPRLSDEQIVYTINHAGSQVLLFDS
SFAACVARLRPRLGNIRHFIELAAQPSSGLQDVLGYEQLIAAEQPLDWPQFDENAGAVLC
YTSGTTGDPKGVLYSHRSVVLHAMAAGLSGAFGLSAFDCIMPCSSLYHGTAWGIPFAAAI
NGCKFVLPCDKMDGASLQELIKTEGVTLSGGVPTIWTMYLAHLERSGEDSGSLARLVIGG
SAVPRAMAETFQTKYGVAVCQLWGMTETSPLGVVATPTPKLAERGQQATNDTIWTRQGRL
QFGIELKIVDEEGRELPCDGVSSGSLKVRGPWTVERYYRSEKSALDEDGWFDTGDIATLD
ADGFMRITDRSKDVIKSGGEWVSSIDIENVAAACPGVKVAAVVGVFHPKWEERPVLVIEP
HADAEVTVETILAHLEPNIVKWWMPDAVIFDAVPLTATGKIDKKVLRERYRNHLVENQPS
AVNQ
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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