SitesBLAST
Comparing WP_035239666.1 NCBI__GCF_000745975.1:WP_035239666.1 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)
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)
35% identity, 96% coverage: 13:526/536 of query aligns to 10:533/541 of Q5SKN9
- T184 (= T180) binding Mg(2+)
- G302 (≠ T293) binding tetradecanoyl-AMP
- Q322 (= Q315) binding tetradecanoyl-AMP
- G323 (≠ T316) binding tetradecanoyl-AMP
- T327 (= T320) binding tetradecanoyl-AMP
- E328 (= E321) binding Mg(2+)
- D418 (= D412) binding tetradecanoyl-AMP
- K435 (= K429) binding tetradecanoyl-AMP
- K439 (≠ I433) binding tetradecanoyl-AMP
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 86% coverage: 13:475/536 of query aligns to 3:464/491 of 1v25A
- active site: T177 (= T180), H197 (≠ N200), H223 (= H224), T320 (= T320), E321 (= E321), K432 (≠ I433), W437 (≠ N438)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H224), V224 (≠ C225), G295 (≠ T293), S296 (≠ A294), A297 (≠ G295), Y317 (= Y317), G318 (= G318), L319 (= L319), T320 (= T320), D411 (= D412), I423 (= I424), K432 (≠ I433), W437 (≠ N438)
- binding magnesium ion: T177 (= T180), E321 (= E321)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 86% coverage: 13:473/536 of query aligns to 3:463/510 of 1v26B
- active site: T177 (= T180), H197 (≠ N200), H223 (= H224), T320 (= T320), E321 (= E321), K432 (≠ I433), W437 (≠ N438)
- binding adenosine monophosphate: G295 (≠ T293), S296 (≠ A294), A297 (≠ G295), G316 (≠ T316), Y317 (= Y317), G318 (= G318), L319 (= L319), T320 (= T320), D411 (= D412), K428 (= K429), K432 (≠ I433), W437 (≠ N438)
- binding magnesium ion: T177 (= T180), E321 (= E321)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
30% identity, 97% coverage: 7:525/536 of query aligns to 7:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T180), G174 (= G182), T175 (= T183), T176 (= T184), K180 (= K188), G293 (≠ A294), A294 (≠ G295), A295 (= A296), Y315 (= Y317), M317 (≠ L319), S318 (≠ T320), D408 (= D412), R423 (= R427)
8jylA Acyl-acp synthetase structure bound to c10-ams
30% identity, 97% coverage: 7:525/536 of query aligns to 5:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T320), E317 (= E321)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W228), G290 (≠ T293), G291 (≠ A294), A292 (≠ G295), A293 (= A296), G312 (≠ T316), Y313 (= Y317), G314 (= G318), M315 (≠ L319), S316 (≠ T320), I321 (≠ P325), D406 (= D412), R421 (= R427), K427 (≠ I433), W432 (≠ N438)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
30% identity, 97% coverage: 7:525/536 of query aligns to 7:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (≠ T293), G293 (≠ A294), A294 (≠ G295), A295 (= A296), G314 (≠ T316), Y315 (= Y317), M317 (≠ L319), S318 (≠ T320), D408 (= D412), R423 (= R427)
- binding 4'-phosphopantetheine: R93 (= R94), P220 (= P221), H223 (= H224)
8i49A Acyl-acp synthetase structure bound to atp
30% identity, 97% coverage: 7:525/536 of query aligns to 7:527/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
30% identity, 97% coverage: 7:525/536 of query aligns to 7:527/530 of 8i22A
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
30% identity, 97% coverage: 7:525/536 of query aligns to 5:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A294), A293 (= A296), G312 (≠ T316), Y313 (= Y317), G314 (= G318), M315 (≠ L319), S316 (≠ T320), D406 (= D412), R421 (= R427)
- binding magnesium ion: M315 (≠ L319), S316 (≠ T320), E317 (= E321)
8i51A Acyl-acp synthetase structure bound to amp-mc7
30% identity, 97% coverage: 7:525/536 of query aligns to 5:525/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A294), A293 (= A296), Y313 (= Y317), M315 (≠ L319), S316 (≠ T320), D406 (= D412), R421 (= R427)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W228), G290 (≠ T293), G312 (≠ T316), G314 (= G318), M315 (≠ L319), P320 (≠ G324), I321 (≠ P325)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
30% identity, 97% coverage: 7:525/536 of query aligns to 7:527/529 of 8i8dA
- binding adenosine monophosphate: G292 (≠ T293), G293 (≠ A294), A295 (= A296), G314 (≠ T316), Y315 (= Y317), G316 (= G318), M317 (≠ L319), S318 (≠ T320), D408 (= D412), K429 (≠ I433)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H224), W227 (= W228), G292 (≠ T293), G316 (= G318), P322 (≠ G324)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R94), P220 (= P221), H223 (= H224), I269 (= I270), G432 (= G436)
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)
31% identity, 96% coverage: 14:526/536 of query aligns to 13:532/539 of P0DX84
- H231 (= H224) mutation to A: Retains 74% of wild-type activity.
- W235 (= W228) mutation to A: Almost completely abolishes the activity.
- G302 (≠ M292) mutation to P: Almost completely abolishes the activity.
- G303 (≠ T293) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y317) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G324) mutation to A: Retains 69% of wild-type activity.
- R432 (= R427) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K429) mutation to A: Retains 36% of wild-type activity.
- D435 (= D430) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I433) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G435) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G436) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E437) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N438) mutation to A: Retains 60% of wild-type activity.
- E474 (= E469) mutation to A: Retains 33% of wild-type activity.
- K523 (= K517) 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 (= K520) 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)
30% identity, 96% coverage: 14:526/536 of query aligns to 13:532/538 of 6ijbB
- active site: T185 (= T180), H205 (≠ N200), H231 (= H224), S329 (≠ T320), E330 (= E321), K438 (≠ I433), W443 (≠ N438), A523 (≠ K517)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W228), G303 (≠ T293), A325 (≠ T316), W326 (≠ Y317), G327 (= G318), M328 (≠ L319)
- binding adenosine monophosphate: G303 (≠ T293), A304 (= A294), A305 (≠ G295), H324 (≠ Q315), W326 (≠ Y317), G327 (= G318), M328 (≠ L319), S329 (≠ T320), Q359 (= Q350), D417 (= D412)
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)
30% identity, 95% coverage: 15:525/536 of query aligns to 6:478/485 of 5x8fB
- active site: T151 (= T180), S171 (≠ N200), H195 (= H224), T288 (= T320), E289 (= E321), I387 (= I433), N392 (= N438), K470 (= K517)
- binding magnesium ion: Y23 (= Y32), E24 (≠ G33), H70 (≠ Y79), N178 (≠ E207), L202 (≠ T231), L214 (≠ C243), T296 (≠ D337), L297 (= L338), S298 (= S339)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R94), L191 (= L220), P192 (= P221), H195 (= H224), I196 (≠ C225), S197 (≠ N226), A237 (= A266), V238 (≠ A267), L260 (≠ I291), G262 (≠ T293), G286 (= G318), M287 (≠ L319), S292 (≠ D333), Q293 (≠ K334), S388 (= S434), G389 (= G435), G390 (= G436), E391 (= E437), K420 (= K466), W421 (= W467), K450 (≠ R498), Y451 (≠ F499)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 95% coverage: 15:525/536 of query aligns to 6:478/484 of 5gtdA
- active site: T151 (= T180), S171 (≠ N200), H195 (= H224), T288 (= T320), E289 (= E321)
- binding adenosine-5'-monophosphate: G263 (≠ A294), G264 (= G295), Y285 (= Y317), G286 (= G318), M287 (≠ L319), T288 (= T320), D366 (= D412), V378 (≠ I424)
- binding magnesium ion: F314 (≠ I355), S315 (≠ V356)
- binding 2-succinylbenzoate: H195 (= H224), S197 (≠ N226), A237 (= A266), L260 (≠ I291), G262 (≠ T293), G263 (≠ A294), G286 (= G318), M287 (≠ L319), S292 (≠ D333), Q293 (≠ K334)
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, 92% coverage: 34:526/536 of query aligns to 27:496/503 of P9WQ37
- K172 (= K188) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ D211) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ D213) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C225) 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 (≠ G227) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F230) 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 (≠ G260) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G318) 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 (= W407) 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 (= D412) 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 (= R427) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S434) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G436) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K517) 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.
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
30% identity, 96% coverage: 14:526/536 of query aligns to 13:529/533 of 6ihkB
- active site: T185 (= T180), H202 (≠ N200), H228 (= H224), S326 (≠ T320), E327 (= E321), K435 (≠ I433), W440 (≠ N438), K520 (= K517)
- binding adenosine-5'-diphosphate: H228 (= H224), G300 (≠ T293), A301 (= A294), A302 (≠ G295), H321 (≠ Q315), A322 (≠ T316), W323 (≠ Y317), G324 (= G318), M325 (≠ L319), S326 (≠ T320), Q356 (= Q350), D414 (= D412), R429 (= R427), K520 (= K517)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
29% identity, 95% coverage: 15:525/536 of query aligns to 5:475/475 of 5burA
- active site: T150 (= T180), S170 (≠ N200), H194 (= H224), T287 (= T320), E288 (= E321)
- binding adenosine-5'-triphosphate: T150 (= T180), S151 (= S181), T153 (= T183), T154 (= T184), K158 (= K188), G263 (= G295), S283 (≠ T316), T287 (= T320), D365 (= D412), V377 (≠ I424), R380 (= R427)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 95% coverage: 15:525/536 of query aligns to 5:475/481 of 5busA
- active site: T150 (= T180), S170 (≠ N200), H194 (= H224), T287 (= T320), E288 (= E321)
- binding adenosine monophosphate: H194 (= H224), G262 (≠ A294), G263 (= G295), S283 (≠ T316), M286 (≠ L319), T287 (= T320), D365 (= D412), V377 (≠ I424), R380 (= R427), K467 (= K517)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 92% coverage: 34:526/536 of query aligns to 30:496/502 of 3r44A
Sites not aligning to the query:
Query Sequence
>WP_035239666.1 NCBI__GCF_000745975.1:WP_035239666.1
MSERSVNYEILSPTNFLDRSVKVYPEKTAVIYGDKTFTWAGFQERVFRLANGLKACGVGR
GDKVAFVCPNTPPMLEAHYAVPLLGAALVSINIRLSANEMSYIINHSDAKVVVADNEFGK
VLSKVVPELTAVKTFVNICDIDDSMPLDGPEYERFLADSPDDPVSLAIEDEREILALNYT
SGTTGLPKGVMYHHRGAYLNSLGELLEFKIDRDSKYLWTLPMFHCNGWCFTWAITAMGAT
HVCLRKVDPVEIYRIIADVGVTHLCAAPTILIGMSVFAKENAVQLSRRLEIMTAGAPPAP
MVIQNMEHIGANITQTYGLTEVFGPHSVCQWQDKWDDLSPMARAGIKARQGVPYIVAEHM
DVVDAVTMEPVPRDGTTMGEIVMRGNNVMLGYYKDAEASTEAFRGGWFHSGDLAVMHPDN
YVQIMDRKKDIIISGGENISTVEIENVLYAHPDVLEVAVISVPDEKWGEVPKAFILPRAG
ANPDPAQIIAYCKEKLARFKAPKYIEFGPLPKTATGKLQKFKLREKEWAGHDRMVN
Or try a new SitesBLAST search
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