SitesBLAST
Comparing HSERO_RS19285 HSERO_RS19285 long-chain fatty acid--CoA ligase 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)
59% identity, 98% coverage: 1:556/566 of query aligns to 1:552/561 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)
30% identity, 90% coverage: 46:555/566 of query aligns to 26:499/506 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)
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, 90% coverage: 46:554/566 of query aligns to 61:547/556 of Q9S725
- K211 (= K221) mutation to S: Drastically reduces the activity.
- M293 (≠ P307) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V334) mutation K->L,A: Affects the substrate specificity.
- E401 (= E409) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A411) 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.
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)
28% identity, 92% coverage: 36:553/566 of query aligns to 43:536/546 of Q84P21
- K530 (= K547) mutation to N: Lossed enzymatic activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 36:525/528 of 5bsrA
- active site: S181 (≠ T213), S201 (≠ N233), H229 (= H264), T328 (≠ S363), E329 (= E364), K433 (≠ L463), Q438 (≠ N468), K518 (= K547)
- binding adenosine monophosphate: A301 (≠ G337), 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)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 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 (≠ G337), A303 (≠ M338), P304 (≠ A339), G325 (= G359), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ I368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 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 (≠ V334), A302 (≠ G337), A303 (≠ M338), P304 (≠ A339), 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)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 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 (≠ G337), A303 (≠ M338), P304 (≠ A339), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ I368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/530 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 (≠ G337), A303 (≠ M338), P304 (≠ A339), 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)
30% identity, 92% coverage: 33:554/566 of query aligns to 44:533/542 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 (≠ G337) 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 (≠ I368) 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 ; 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.
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: 46:554/566 of query aligns to 57:542/559 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)
29% identity, 90% coverage: 46:556/566 of query aligns to 43:528/528 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 (≠ A339), G325 (= G359), G327 (= G361), T329 (≠ S363), P333 (= P367), V334 (≠ I368), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
29% identity, 90% coverage: 46:556/566 of query aligns to 43:528/528 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 (≠ A339), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), D413 (= D442), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
30% identity, 92% coverage: 33:554/566 of query aligns to 36:522/527 of 5u95B
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
29% identity, 89% coverage: 49:554/566 of query aligns to 49:534/539 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 (≠ N272), G314 (= G337), A315 (≠ M338), P316 (≠ A339), G337 (= G359), Y338 (= Y360), G339 (= G361), L340 (= L362), T341 (≠ S363), S345 (≠ P367), A346 (≠ I368), 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 (≠ I368)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
29% identity, 89% coverage: 49:554/566 of query aligns to 49:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H264), F245 (= F266), T249 (≠ N272), G314 (= G337), A315 (≠ M338), P316 (≠ A339), G337 (= G359), Y338 (= Y360), G339 (= G361), L340 (= L362), T341 (≠ S363), A346 (≠ I368), D420 (= D442), I432 (= I454), K527 (= K547)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 94% coverage: 22:555/566 of query aligns to 9:510/518 of 4wv3B
- active site: S175 (≠ T213), T320 (≠ S363), E321 (= E364), K418 (≠ L463), W423 (≠ N468), K502 (= K547)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ H264), T221 (≠ I265), F222 (= F266), A293 (≠ G336), S294 (≠ G337), E295 (≠ M338), A296 (= A339), G316 (= G359), I317 (≠ Y360), G318 (= G361), C319 (≠ L362), T320 (≠ S363), D397 (= D442), H409 (≠ I454), R412 (= R457), K502 (= K547)
6e97B Crystal structure of the aryl acid adenylating enzyme fscc from fuscachelin nrps in complex with dhb-adenylate
29% identity, 93% coverage: 35:559/566 of query aligns to 34:534/537 of 6e97B
- active site: S190 (≠ T213), S210 (≠ N233), H234 (= H264), A336 (≠ S363), E337 (= E364), N437 (≠ L463), K442 (≠ N468), K522 (= K547)
- binding 5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine: H234 (= H264), N235 (≠ I265), F236 (= F266), S240 (≠ V270), G310 (= G337), A311 (≠ M338), K312 (≠ A339), V332 (≠ G359), F333 (≠ Y360), G334 (= G361), M335 (≠ L362), A336 (≠ S363), D416 (= D442), K433 (= K459), K442 (≠ N468)
P40871 2,3-dihydroxybenzoate-AMP ligase; Dihydroxybenzoic acid-activating enzyme; EC 6.2.1.71 from Bacillus subtilis (strain 168) (see paper)
27% identity, 94% coverage: 22:555/566 of query aligns to 27:527/539 of P40871
- G191 (= G214) binding
- HN 234:235 (≠ HI 264:265) binding
- S240 (≠ V270) binding
- G307 (= G337) binding
- V329 (≠ G359) binding
- D413 (= D442) binding
- R428 (= R457) binding
- K519 (= K547) binding ; binding
1md9A Crystal structure of dhbe in complex with dhb and amp (see paper)
27% identity, 94% coverage: 22:555/566 of query aligns to 27:527/536 of 1md9A
- active site: S190 (≠ T213), S210 (≠ N233), H234 (= H264), A333 (≠ S363), E334 (= E364), N434 (≠ L463), K439 (≠ N468), K519 (= K547)
- binding adenosine monophosphate: G191 (= G214), G307 (= G337), A308 (≠ M338), K309 (≠ A339), V329 (≠ G359), F330 (≠ Y360), G331 (= G361), M332 (≠ L362), D413 (= D442), V425 (≠ I454), R428 (= R457), K519 (= K547)
- binding 2,3-dihydroxy-benzoic acid: H234 (= H264), N235 (≠ I265), Y236 (≠ F266), S240 (≠ V270), G307 (= G337), V329 (≠ G359), G331 (= G361), M332 (≠ L362), K519 (= K547)
Query Sequence
>HSERO_RS19285 HSERO_RS19285 long-chain fatty acid--CoA ligase
MERFWLASYPAGVPAEIDPGRYGSLVQMIDEAFVQHADRQAYVCMGKYLSYRELDSLSRA
LGGWLQGLGLQKGARVAIMMPNVLQYPIAIAAILRAGYTVVNVNPLYTARELEHQLKDSG
AEAIFVLENFACTLQKVVAHTNIKHIVVASMGELLGALKGTLVNLVVRHVKKLVPAWSLP
NAITFSQALSQARGKTLQPVTLTHDDIAFLQYTGGTTGVAKGAVLTHRNLVANVLQAEEW
LTPALKAGKPIDQLVFVCALPLYHIFALTVCNMLGTREGALNLLIPNPRDIPGFVKELAK
YKVNTFPAVNTLYNALLNNADFARLDFSGYRCCVGGGMAVQKSVADKWKKLTGCPIIEGY
GLSETSPIASANPCTIDEYTGTIGLPLPSTEFAILDDDGQPVPLGQPGEIAIRGPQVMPG
YWQRPDETAKVMTPDGFFKTGDIGVMDERGYTKIVDRKKDMILVSGFNVYPNEVEGVVAQ
HPGVLECACVGVPDEHTGEAVKLFVVRKDKTLSAAQLMDYCKEQFTGYKKPKYIEFRDEL
PKTNVGKILRRELRDEPAKAQQKQAA
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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