SitesBLAST
Comparing 3607591 FitnessBrowser__Dino:3607591 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)
47% identity, 97% coverage: 8:565/573 of query aligns to 5:552/561 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 (= E375) mutation to A: Loss of activity.
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)
32% identity, 96% coverage: 18:565/573 of query aligns to 24:544/559 of Q67W82
- G395 (= G418) 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)
33% identity, 85% coverage: 78:563/573 of query aligns to 49:498/506 of 4gxqA
- active site: T163 (= T229), N183 (= N249), H207 (= H275), T303 (= T374), E304 (= E375), I403 (≠ V472), N408 (= N477), A491 (≠ K556)
- binding adenosine-5'-triphosphate: T163 (= T229), S164 (≠ G230), G165 (= G231), T166 (= T232), T167 (= T233), H207 (= H275), S277 (≠ G348), A278 (≠ M349), P279 (≠ A350), E298 (≠ Q369), M302 (≠ L373), T303 (= T374), D382 (= D451), R397 (= R466)
- binding carbonate ion: H207 (= H275), S277 (≠ G348), R299 (≠ G370), G301 (= G372)
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)
29% identity, 95% coverage: 18:564/573 of query aligns to 28:548/556 of Q9S725
- K211 (= K237) mutation to S: Drastically reduces the activity.
- M293 (≠ S318) mutation M->A,P: Affects the substrate specificity.
- K320 (= K342) mutation K->L,A: Affects the substrate specificity.
- E401 (= E419) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A421) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R466) mutation to Q: Drastically reduces the activity.
- K457 (≠ S474) mutation to S: Drastically reduces the activity.
- K540 (= K556) mutation to N: Abolishes the activity.
5ie2A Crystal structure of a plant enzyme (see paper)
30% identity, 88% coverage: 57:560/573 of query aligns to 31:499/506 of 5ie2A
- active site: T165 (= T229), S185 (≠ N249), H209 (= H275), T310 (= T374), E311 (= E375), N410 (≠ V472), K415 (≠ N477), K495 (= K556)
- binding adenosine-5'-triphosphate: T165 (= T229), S166 (≠ G230), G167 (= G231), T168 (= T232), T169 (= T233), S284 (≠ G348), A285 (≠ M349), S286 (≠ A350), Y307 (= Y371), A308 (≠ G372), M309 (≠ L373), T310 (= T374), D389 (= D451), L401 (≠ I463), R404 (= R466), K495 (= K556)
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)
30% identity, 88% coverage: 57:562/573 of query aligns to 58:536/546 of Q84P21
- K530 (= K556) mutation to N: Lossed enzymatic activity.
Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 88% coverage: 57:560/573 of query aligns to 31:504/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 229:233) binding
- H214 (= H275) binding ; mutation to A: Abolished activity.
- S289 (≠ G348) binding ; mutation to A: Abolished activity.
- SAS 289:291 (≠ GMA 348:350) binding
- EA 310:311 (≠ QG 369:370) binding
- M314 (≠ L373) binding
- T315 (= T374) binding
- H319 (≠ P378) binding ; mutation to A: Abolished activity.
- D394 (= D451) binding
- R409 (= R466) binding ; mutation to A: Abolished activity.
- K500 (= K556) binding ; binding ; mutation to A: Abolished activity.
5ie3A Crystal structure of a plant enzyme (see paper)
30% identity, 88% coverage: 57:560/573 of query aligns to 31:497/504 of 5ie3A
- active site: T163 (= T229), S183 (≠ N249), H207 (= H275), T308 (= T374), E309 (= E375), N408 (≠ V472), K413 (≠ N477), K493 (= K556)
- binding adenosine monophosphate: S164 (≠ G230), S282 (≠ G348), A283 (≠ M349), S284 (≠ A350), Y305 (= Y371), A306 (≠ G372), M307 (≠ L373), T308 (= T374), D387 (= D451), L399 (≠ I463), R402 (= R466), K493 (= K556)
- binding oxalic acid: V208 (≠ I276), S282 (≠ G348), A306 (≠ G372), M307 (≠ L373), H312 (≠ P378), K493 (= K556)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 96% coverage: 18:565/573 of query aligns to 9:527/528 of 5bsrA
- active site: S181 (≠ T229), S201 (≠ N249), H229 (= H275), T328 (= T374), E329 (= E375), K433 (≠ V472), Q438 (≠ N477), K518 (= K556)
- binding adenosine monophosphate: A301 (≠ G348), G326 (= G372), T328 (= T374), D412 (= D451), K429 (= K468), K433 (≠ V472), Q438 (≠ N477)
- binding coenzyme a: L102 (= L115), P226 (= P272), H229 (= H275), Y231 (≠ F277), F253 (≠ R300), K435 (≠ S474), G436 (= G475), F437 (= F476), F498 (≠ A536)
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)
29% identity, 96% coverage: 18:565/573 of query aligns to 17:535/542 of O24146
- S189 (≠ T229) binding
- S190 (≠ G230) binding
- G191 (= G231) binding
- T192 (= T232) binding
- T193 (= T233) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K237) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H275) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F277) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ L281) binding ; binding ; binding
- K260 (≠ P299) binding
- A309 (≠ G348) binding ; binding ; binding
- Q331 (= Q369) binding
- G332 (= G370) binding ; binding ; binding ; binding ; binding
- T336 (= T374) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ I379) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ L382) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D451) binding ; binding ; binding ; binding ; binding
- R435 (= R466) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K468) binding ; binding ; binding ; binding
- K441 (≠ V472) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S474) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G475) binding
- Q446 (≠ N477) binding
- K526 (= K556) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 96% coverage: 18:565/573 of query aligns to 10:528/530 of 5bsmA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- binding adenosine-5'-triphosphate: S182 (≠ T229), S183 (≠ G230), G184 (= G231), T185 (= T232), T186 (= T233), K190 (= K237), H230 (= H275), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (= T374), D413 (= D451), I425 (= I463), R428 (= R466), K519 (= K556)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 96% coverage: 18:565/573 of query aligns to 10:528/529 of 5bsvA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- 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 (≠ L281), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), M328 (≠ L373), T329 (= T374), P333 (= P378), V334 (≠ I379), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
29% identity, 96% coverage: 18:565/573 of query aligns to 10:528/529 of 5bsuA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- 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 (≠ L281), M299 (≠ A345), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), M328 (≠ L373), T329 (= T374), P333 (= P378), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
29% identity, 96% coverage: 18:565/573 of query aligns to 10:528/529 of 5bstA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- 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 (≠ L281), A302 (≠ G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (= T374), P333 (= P378), V334 (≠ I379), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
29% identity, 95% coverage: 18:563/573 of query aligns to 10:526/528 of 3ni2A
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F277), S236 (≠ L281), G302 (= G348), A303 (≠ M349), P304 (≠ A350), G325 (= G370), G327 (= G372), T329 (= T374), P333 (= P378), V334 (≠ I379), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 95% coverage: 18:563/573 of query aligns to 10:526/528 of 3a9vA
- active site: S182 (≠ T229), S202 (≠ N249), H230 (= H275), T329 (= T374), E330 (= E375), K434 (≠ V472), Q439 (≠ N477), K519 (= K556)
- binding adenosine monophosphate: H230 (= H275), G302 (= G348), A303 (≠ M349), P304 (≠ A350), Y326 (= Y371), G327 (= G372), M328 (≠ L373), T329 (= T374), D413 (= D451), K430 (= K468), K434 (≠ V472), Q439 (≠ N477)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 94% coverage: 27:563/573 of query aligns to 19:534/539 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 (≠ N282), G314 (= G348), A315 (≠ M349), P316 (≠ A350), G337 (= G370), Y338 (= Y371), G339 (= G372), L340 (= L373), T341 (= T374), S345 (≠ P378), A346 (≠ I379), D420 (= D451), I432 (= I463), K527 (= K556)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F277), R335 (≠ L368), G337 (= G370), G339 (= G372), L340 (= L373), A346 (≠ I379)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 94% coverage: 27:563/573 of query aligns to 19:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H275), F245 (= F277), T249 (≠ N282), G314 (= G348), A315 (≠ M349), P316 (≠ A350), G337 (= G370), Y338 (= Y371), G339 (= G372), L340 (= L373), T341 (= T374), A346 (≠ I379), D420 (= D451), I432 (= I463), K527 (= K556)
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)
31% identity, 89% coverage: 57:565/573 of query aligns to 30:496/503 of P9WQ37
- K172 (= K237) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R262) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (= R264) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I276) 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 (≠ M283) 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 (= R313) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G372) 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 (= W446) 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 (= D451) 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 (= R466) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V473) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G475) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K556) 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.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
29% identity, 96% coverage: 18:565/573 of query aligns to 9:524/527 of 5u95B
Query Sequence
>3607591 FitnessBrowser__Dino:3607591
MEDPTRPWMAFYGPDVRPDIDTPAYRTLGDMIGAVAATYGTAPAFTTCLPNGMNGTLSFA
QVDEMSDAFAVYLREVAGLNPGDRVALQMPNCLSFPVAAFGVFKAGCVLVNVNPLYTAEE
MGKQFLDAEPHALVIVDMFADKIPEATRGHPIPNIVVTRIAEFLPALPRGIVGLVQKYWD
RSVAEIEVPHIRLPDALEAGRRHQADERIEVEGYHQAVAPDDVAVLQYTGGTTGVAKGAM
LTHANLIVNMEQTMELIEGLERGREVVLTALPLYHIFAFSLNMLGFYWMGARNILIPSPR
PLANLKRAFENYRITWMSGVNTLFNGLTNEIWFTDTPPRHLKFAAAGGMALQSSVAERWR
EITGTDVLQGYGLTETSPILSLEPLGKTRSGSIGIPLPATRLACLDDDGKQVAIGDRGEI
AAKGPQVMKGYWNKPEETANVLQNGWFLTGDIGVMDADGYFHIVDRKKDMVVVSGFNVYP
NEVEDCLASHPGIIEAAVIGVPDGATGEAVKAFVVKGDSGLSEADIRAHCKEHLTAYKVP
KRVEFRDELPKSNVGKILRKDLRAEELARTGGA
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