SitesBLAST
Comparing RR42_RS18150 FitnessBrowser__Cup4G11:RR42_RS18150 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)
56% identity, 100% coverage: 1:559/560 of query aligns to 1:555/561 of P69451
- Y213 (= Y212) mutation to A: Loss of activity.
- T214 (= T213) mutation to A: 10% of wild-type activity.
- G216 (= G215) mutation to A: Decreases activity.
- T217 (= T216) mutation to A: Decreases activity.
- G219 (= G218) mutation to A: Decreases activity.
- K222 (= K221) mutation to A: Decreases activity.
- E361 (= E364) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 91% coverage: 49:558/560 of query aligns to 29:502/506 of 4gxqA
- active site: T163 (= T213), N183 (= N233), H207 (= H264), T303 (≠ S363), E304 (= E364), I403 (≠ L463), N408 (= N468), A491 (≠ K547)
- binding adenosine-5'-triphosphate: T163 (= T213), S164 (≠ G214), G165 (= G215), T166 (= T216), T167 (= T217), H207 (= H264), S277 (≠ G337), A278 (≠ M338), P279 (≠ A339), E298 (= E358), M302 (≠ L362), T303 (≠ S363), D382 (= D442), R397 (= R457)
- binding carbonate ion: H207 (= H264), S277 (≠ G337), R299 (≠ G359), G301 (= G361)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 90% coverage: 50:554/560 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T213), S201 (≠ N233), H229 (= H264), T328 (≠ S363), E329 (= E364), K433 (≠ L463), Q438 (≠ N468), K518 (= K547)
- binding adenosine monophosphate: A301 (vs. gap), G326 (= G361), T328 (≠ S363), D412 (= D442), K429 (= K459), K433 (≠ L463), Q438 (≠ N468)
- binding coenzyme a: L102 (= L106), P226 (= P261), H229 (= H264), Y231 (≠ F266), F253 (≠ R289), K435 (≠ S465), G436 (= G466), F437 (= F467), F498 (≠ G527)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 90% coverage: 50:554/560 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ S368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 90% coverage: 50:554/560 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), M299 (≠ N334), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 90% coverage: 50:554/560 of query aligns to 47:526/529 of 5bstA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ S368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 90% coverage: 50:554/560 of query aligns to 47:526/530 of 5bsmA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding adenosine-5'-triphosphate: S182 (≠ T213), S183 (≠ G214), G184 (= G215), T185 (= T216), T186 (= T217), K190 (= K221), H230 (= H264), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), D413 (= D442), I425 (= I454), R428 (= R457), K519 (= K547)
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)
32% identity, 90% coverage: 50:554/560 of query aligns to 54:533/542 of O24146
- S189 (≠ T213) binding
- S190 (≠ G214) binding
- G191 (= G215) binding
- T192 (= T216) binding
- T193 (= T217) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K221) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H264) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F266) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V270) binding ; binding ; binding
- K260 (≠ P288) binding
- A309 (vs. gap) binding ; binding ; binding
- Q331 (≠ E358) binding
- G332 (= G359) binding ; binding ; binding ; binding ; binding
- T336 (≠ S363) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ S368) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ T370) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D442) binding ; binding ; binding ; binding ; binding
- R435 (= R457) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K459) binding ; binding ; binding ; binding
- K441 (≠ L463) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S465) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G466) binding
- Q446 (≠ N468) binding
- K526 (= K547) binding ; mutation to A: Abolished activity against 4-coumarate.
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, 90% coverage: 50:554/560 of query aligns to 65:547/556 of Q9S725
- K211 (= K221) mutation to S: Drastically reduces the activity.
- M293 (≠ P307) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N334) mutation K->L,A: Affects the substrate specificity.
- E401 (= E409) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C411) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R457) mutation to Q: Drastically reduces the activity.
- K457 (≠ S465) mutation to S: Drastically reduces the activity.
- K540 (= K547) mutation to N: Abolishes the activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
32% identity, 90% coverage: 50:554/560 of query aligns to 46:522/527 of 5u95B
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, 90% coverage: 50:554/560 of query aligns to 61:542/559 of Q67W82
- G395 (= G408) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 90% coverage: 50:555/560 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F266), S236 (≠ V270), G302 (= G337), A303 (≠ M338), P304 (vs. gap), G325 (= G359), G327 (= G361), T329 (≠ S363), P333 (= P367), V334 (≠ S368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 90% coverage: 50:555/560 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding adenosine monophosphate: H230 (= H264), G302 (= G337), A303 (≠ M338), P304 (vs. gap), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 94% coverage: 26:554/560 of query aligns to 21:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H264), F245 (= F266), T249 (≠ V270), G314 (= G337), A315 (≠ M338), P316 (≠ A339), G337 (= G359), Y338 (= Y360), G339 (= G361), L340 (= L362), T341 (≠ S363), A346 (≠ S368), D420 (= D442), I432 (= I454), K527 (= K547)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 94% coverage: 26:554/560 of query aligns to 21:534/539 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 (= H264), F245 (= F266), T249 (≠ V270), G314 (= G337), A315 (≠ M338), P316 (≠ A339), G337 (= G359), Y338 (= Y360), G339 (= G361), L340 (= L362), T341 (≠ S363), S345 (≠ P367), A346 (≠ S368), D420 (= D442), I432 (= I454), K527 (= K547)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F266), R335 (≠ I357), G337 (= G359), G339 (= G361), L340 (= L362), A346 (≠ S368)
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: 46:559/560 of query aligns to 27:499/503 of P9WQ37
- K172 (= K221) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K247) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A249) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I265) 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 (= A267) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V270) 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 (≠ K302) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G361) 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 (≠ F437) 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 (= D442) 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 (= R457) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V464) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G466) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K547) 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.
6m2uA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-chloro-1,3-thiazole-5-carboxylate-amp (see paper)
31% identity, 95% coverage: 24:555/560 of query aligns to 9:515/518 of 6m2uA
- active site: S176 (≠ T213), T196 (≠ Q236), T324 (≠ S363), E325 (= E364), K422 (≠ L463), Y427 (≠ N468), K507 (= K547)
- binding adenosine monophosphate: G298 (= G337), E299 (≠ M338), A300 (= A339), D319 (≠ E358), G320 (= G359), I321 (≠ Y360), G322 (= G361), T324 (≠ S363), D401 (= D442), R416 (= R457), K422 (≠ L463), Y427 (≠ N468)
- binding 2-chloranyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F266), A297 (≠ G336), G322 (= G361), S323 (≠ L362), A328 (≠ P367)
6m2tA The crystal structure of benzoate coenzyme a ligase double mutant (h333a/i334a) in complex with 2-methyl-thiazole-5 carboxylate-amp
31% identity, 95% coverage: 24:555/560 of query aligns to 9:515/518 of 6m2tA
- active site: S176 (≠ T213), T196 (≠ Q236), T324 (≠ S363), E325 (= E364), K422 (≠ L463), Y427 (≠ N468), K507 (= K547)
- binding 2-methyl-1,3-thiazole-5-carboxylic acid: Y223 (≠ F266), G322 (= G361), S323 (≠ L362), A328 (≠ P367)
- binding adenosine monophosphate: G298 (= G337), E299 (≠ M338), A300 (= A339), G320 (= G359), I321 (≠ Y360), S323 (≠ L362), T324 (≠ S363), D401 (= D442), R416 (= R457), K422 (≠ L463), Y427 (≠ N468)
4rmnA Crystal structure of a benzoate coenzyme a ligase with 2-thiophene carboxylic acid (see paper)
31% identity, 95% coverage: 24:555/560 of query aligns to 9:515/518 of 4rmnA
- active site: S176 (≠ T213), T196 (≠ Q236), T324 (≠ S363), E325 (= E364), K422 (≠ L463), Y427 (≠ N468), K507 (= K547)
- binding thiophene-2-carboxylic acid: A217 (≠ L260), F221 (≠ H264), Y223 (≠ F266), G269 (≠ A308), A270 (≠ V309), A297 (≠ G336), G298 (= G337), G322 (= G361), S323 (≠ L362), H328 (≠ P367), I329 (≠ S368), K422 (≠ L463), G425 (= G466)
4rm3A Crystal structure of a benzoate coenzyme a ligase with 2-furoic acid (see paper)
31% identity, 95% coverage: 24:555/560 of query aligns to 10:516/518 of 4rm3A
- active site: S177 (≠ T213), T197 (≠ Q236), T325 (≠ S363), E326 (= E364), K423 (≠ L463), Y428 (≠ N468), K508 (= K547)
- binding 2-furoic acid: A223 (≠ I265), Y224 (≠ F266), A298 (≠ G336), G323 (= G361), H329 (≠ P367), I330 (≠ S368), K423 (≠ L463)
Query Sequence
>RR42_RS18150 FitnessBrowser__Cup4G11:RR42_RS18150
MERLWLKHYPAGVPAEIDSSQFHSLAELLEASFRTYADRRAFVCMDKSITYGELDRMSRQ
FAAWLQSRGLKPGARVAIMMPNVLQYPVVLAAVLRAGFVVVNVNPLYTPRELEHQLKDSG
AEAIVILENFATTLQQVLPATPVKHVVVASMGDLLGGLKGAIVNFVVRNVKKMVPAWELP
NCVRFNAVLAEGRGMQLQPATTGPDDVAFLQYTGGTTGVSKGAVLLHRNIVSNVLQSEAW
MQPALAKGAPIDQVITITALPLYHIFALTVCCLLGMRSGGLSVLIPNPRDIPGFIKELQK
YKFNMFPAVNTLYNALINSPDIDKVDFSGLRVANGGGMAVQEAVAKKWLARTGCPIIEGY
GLSETSPSATCNPTDSDAFSGTIGLPLPSTDIAIRDDDGADVPLGQAGEICIRGPQVMAG
YWNRPDETAKVMTADGFFKSGDIGVMDARGYTKIVDRKKDMILVSGFNVYPNEVEGVAAE
CPGVLEVAAVGVPDEHSGEVVKLYVVRKDPALTEAELIAFCKERLTGYKRPKFVEFRSEL
PKTNVGKILRRELRDSRKAA
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