SitesBLAST
Comparing WP_245281768.1 NCBI__GCF_001541235.1:WP_245281768.1 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)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
36% identity, 96% coverage: 20:572/575 of query aligns to 5:556/561 of P69451
- Y213 (= Y228) mutation to A: Loss of activity.
- T214 (= T229) mutation to A: 10% of wild-type activity.
- G216 (= G231) mutation to A: Decreases activity.
- T217 (= T232) mutation to A: Decreases activity.
- G219 (= G234) mutation to A: Decreases activity.
- K222 (= K237) mutation to A: Decreases activity.
- E361 (= E374) mutation to A: Loss of activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 90% coverage: 52:566/575 of query aligns to 19:484/486 of 8wevA
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)
31% identity, 94% coverage: 29:567/575 of query aligns to 29:548/556 of Q9S725
- K211 (= K237) mutation to S: Drastically reduces the activity.
- M293 (≠ P317) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L344) mutation K->L,A: Affects the substrate specificity.
- E401 (= E421) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C423) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R468) mutation to Q: Drastically reduces the activity.
- K457 (≠ S476) mutation to S: Drastically reduces the activity.
- K540 (= K559) mutation to N: Abolishes the activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
32% identity, 94% coverage: 29:566/575 of query aligns to 11:526/528 of 3ni2A
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F277), S236 (≠ V281), G302 (= G347), A303 (= A348), P304 (≠ A349), G325 (= G369), G327 (= G371), T329 (≠ S373), P333 (= P377), V334 (= V378), D413 (= D453), K430 (= K470), K434 (≠ I474), Q439 (≠ N479)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
32% identity, 94% coverage: 29:566/575 of query aligns to 11:526/528 of 3a9vA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding adenosine monophosphate: H230 (= H275), G302 (= G347), A303 (= A348), P304 (≠ A349), Y326 (= Y370), G327 (= G371), M328 (≠ L372), T329 (≠ S373), D413 (= D453), K430 (= K470), K434 (≠ I474), Q439 (≠ N479)
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 18:535/542 of O24146
- S189 (≠ T229) binding ATP
- S190 (≠ G230) binding ATP
- G191 (= G231) binding ATP
- T192 (= T232) binding ATP
- T193 (= T233) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K237) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H275) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F277) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V281) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R298) binding CoA
- A309 (≠ G347) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E368) binding ATP
- G332 (= G369) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S373) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V378) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D453) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R468) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K470) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I474) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S476) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G477) binding CoA
- Q446 (≠ N479) binding AMP
- K526 (= K559) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 11:528/529 of 5bsvA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), A302 (≠ G347), A303 (= A348), P304 (≠ A349), G325 (= G369), G327 (= G371), M328 (≠ L372), T329 (≠ S373), P333 (= P377), V334 (= V378), D413 (= D453), K430 (= K470), K434 (≠ I474), Q439 (≠ N479)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 11:528/529 of 5bsuA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), M299 (≠ L344), A302 (≠ G347), A303 (= A348), P304 (≠ A349), G325 (= G369), G327 (= G371), M328 (≠ L372), T329 (≠ S373), P333 (= P377), D413 (= D453), K430 (= K470), K434 (≠ I474), Q439 (≠ N479)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 11:528/529 of 5bstA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H275), Y232 (≠ F277), S236 (≠ V281), A302 (≠ G347), A303 (= A348), P304 (≠ A349), G325 (= G369), Y326 (= Y370), G327 (= G371), M328 (≠ L372), T329 (≠ S373), P333 (= P377), V334 (= V378), D413 (= D453), K430 (= K470), K434 (≠ I474), Q439 (≠ N479)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 11:528/530 of 5bsmA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (≠ S373), E330 (= E374), K434 (≠ I474), Q439 (≠ N479), K519 (= K559)
- binding adenosine-5'-triphosphate: S182 (≠ T229), S183 (≠ G230), G184 (= G231), T185 (= T232), T186 (= T233), K190 (= K237), H230 (= H275), A302 (≠ G347), A303 (= A348), P304 (≠ A349), Y326 (= Y370), G327 (= G371), M328 (≠ L372), T329 (≠ S373), D413 (= D453), I425 (= I465), R428 (= R468), K519 (= K559)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 94% coverage: 29:568/575 of query aligns to 10:527/528 of 5bsrA
- active site: S181 (≠ T229), S201 (≠ N249), H229 (= H275), T328 (≠ S373), E329 (= E374), K433 (≠ I474), Q438 (≠ N479), K518 (= K559)
- binding adenosine monophosphate: A301 (≠ G347), G326 (= G371), T328 (≠ S373), D412 (= D453), K429 (= K470), K433 (≠ I474), Q438 (≠ N479)
- binding coenzyme a: L102 (= L120), P226 (= P272), H229 (= H275), Y231 (≠ F277), F253 (= F299), K435 (≠ S476), G436 (= G477), F437 (= F478), F498 (≠ R539)
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
30% identity, 89% coverage: 60:568/575 of query aligns to 57:544/559 of Q67W82
- G395 (= G420) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
29% identity, 92% coverage: 37:566/575 of query aligns to 3:498/506 of 4gxqA
- active site: T163 (= T229), N183 (= N249), H207 (= H275), T303 (≠ S373), E304 (= E374), I403 (= I474), N408 (= N479), A491 (≠ K559)
- binding adenosine-5'-triphosphate: T163 (= T229), S164 (≠ G230), G165 (= G231), T166 (= T232), T167 (= T233), H207 (= H275), S277 (≠ G347), A278 (= A348), P279 (≠ A349), E298 (= E368), M302 (≠ L372), T303 (≠ S373), D382 (= D453), R397 (= R468)
- binding carbonate ion: H207 (= H275), S277 (≠ G347), R299 (≠ G369), G301 (= G371)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 94% coverage: 29:568/575 of query aligns to 10:524/527 of 5u95B
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 88% coverage: 60:565/575 of query aligns to 55:536/546 of Q84P21
- K530 (= K559) mutation to N: Lossed enzymatic activity.
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)
31% identity, 90% coverage: 50:566/575 of query aligns to 50:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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, 89% coverage: 63:571/575 of query aligns to 30:499/503 of P9WQ37
- K172 (= K237) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ E261) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ G263) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V276) 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 (= A278) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V281) 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 (≠ K312) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G371) 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 (≠ Y448) 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 (= D453) 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 (= R468) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S475) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G477) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K559) 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, 89% coverage: 63:571/575 of query aligns to 33:499/502 of 3r44A
Sites not aligning to the query:
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 92% coverage: 38:566/575 of query aligns to 11:534/539 of 6k4dA
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate: H243 (= H275), F245 (= F277), T249 (≠ V281), G314 (= G347), A315 (= A348), P316 (≠ A349), G337 (= G369), Y338 (= Y370), G339 (= G371), L340 (= L372), T341 (≠ S373), S345 (≠ P377), A346 (≠ V378), D420 (= D453), I432 (= I465), K527 (= K559)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F277), R335 (≠ K365), G337 (= G369), G339 (= G371), L340 (= L372), A346 (≠ V378)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 92% coverage: 38:566/575 of query aligns to 11:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H275), F245 (= F277), T249 (≠ V281), G314 (= G347), A315 (= A348), P316 (≠ A349), G337 (= G369), Y338 (= Y370), G339 (= G371), L340 (= L372), T341 (≠ S373), A346 (≠ V378), D420 (= D453), I432 (= I465), K527 (= K559)
Query Sequence
>WP_245281768.1 NCBI__GCF_001541235.1:WP_245281768.1
MMTTVRPPAPAAAAEPTLPWQVHYPSGIDWHMPLKVAPLYALLDDAVRDYGHLPCTNFLG
RTLSYGEIGDLVGQTAAALQRQGVRKGTKVGLFLPNSPTFIIYFFAVLKAGGTVVNFNPL
YTVAELTHQVEDSDTELMITLDLKVLFDKVEALLQSGCLARALVAPFPSLLPATKAALFR
LFRSRELARPLSSPVANRVTLEGEALAGAATMQPVAIDPENDVAVLQYTGGTTGTPKGAM
LTHANVYINVQQVAATAPDLEPGVERVLGVLPFFHVFALTVVMNLGIAKAAEIIIMPRFA
LDDALKLIDRTKPTIMPGVPTLFNAIMNHPKIASFDLSSLKFCLSGGAALPIEVKQRFEA
ITGCKVVEGYGLSEASPVVACNPIDGPARAGSIGIPLVGTTISLRDLNNPELEVPLGEKG
EICVKGPQVMKGYYKRPEDTAAQMVGEYLRTGDVACMDADGFFYIKDRIKDLIISSGFNV
YPRRVEEALYEHPAVAEVTVIGIRDKKRGEAPKAFVRLKTDTTVTVAELMEHLQTRISRI
ELPAEIEFRAELPKTLIGKLSKKELKAEEDAKALA
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