SitesBLAST
Comparing 5210425 FitnessBrowser__PV4:5210425 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)
32% identity, 90% coverage: 56:565/569 of query aligns to 46:549/561 of P69451
- Y213 (= Y217) mutation to A: Loss of activity.
- T214 (= T218) mutation to A: 10% of wild-type activity.
- G216 (= G220) mutation to A: Decreases activity.
- T217 (= T221) mutation to A: Decreases activity.
- G219 (= G223) mutation to A: Decreases activity.
- K222 (= K226) mutation to A: Decreases activity.
- E361 (= E369) 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)
30% identity, 90% coverage: 56:569/569 of query aligns to 57:545/559 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.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
28% identity, 89% coverage: 60:567/569 of query aligns to 47:527/528 of 3ni2A
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), K519 (= K559)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ A269), S236 (≠ T273), G302 (≠ I341), A303 (≠ K342), P304 (≠ K343), G325 (≠ A364), G327 (= G366), T329 (= T368), P333 (≠ T372), V334 (≠ C373), D413 (= D454), K430 (= K471), K434 (= K475), Q439 (≠ S480)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
28% identity, 89% coverage: 60:567/569 of query aligns to 47:527/528 of 3a9vA
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), K519 (= K559)
- binding adenosine monophosphate: H230 (≠ W267), G302 (≠ I341), A303 (≠ K342), P304 (≠ K343), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), D413 (= D454), K430 (= K471), K434 (= K475), Q439 (≠ S480)
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)
27% identity, 95% coverage: 26:567/569 of query aligns to 25:538/546 of Q84P21
- K530 (= K559) mutation to N: Lossed enzymatic activity.
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)
28% identity, 90% coverage: 56:569/569 of query aligns to 61:550/556 of Q9S725
- K211 (= K226) mutation to S: Drastically reduces the activity.
- M293 (≠ I309) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ P336) mutation K->L,A: Affects the substrate specificity.
- E401 (= E421) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ Q423) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R469) mutation to Q: Drastically reduces the activity.
- K457 (≠ N477) mutation to S: Drastically reduces the activity.
- K540 (= K559) mutation to N: Abolishes the activity.
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
28% identity, 96% coverage: 25:569/569 of query aligns to 10:537/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (≠ W267), F245 (≠ A269), T249 (= T273), G314 (vs. gap), A315 (≠ I338), P316 (≠ S339), G337 (≠ A364), Y338 (= Y365), G339 (= G366), L340 (≠ M367), T341 (= T368), A346 (≠ C373), D420 (= D454), I432 (≠ Y466), K527 (= K559)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
28% identity, 96% coverage: 25:569/569 of query aligns to 10:537/539 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 (≠ W267), F245 (≠ A269), T249 (= T273), G314 (vs. gap), A315 (≠ I338), P316 (≠ S339), G337 (≠ A364), Y338 (= Y365), G339 (= G366), L340 (≠ M367), T341 (= T368), S345 (≠ T372), A346 (≠ C373), D420 (= D454), I432 (≠ Y466), K527 (= K559)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ A269), R335 (≠ E362), G337 (≠ A364), G339 (= G366), L340 (≠ M367), A346 (≠ C373)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
27% identity, 96% coverage: 26:569/569 of query aligns to 18:528/528 of 5bsrA
- active site: S181 (≠ T218), S201 (≠ T238), H229 (≠ W267), T328 (= T368), E329 (= E369), K433 (= K475), Q438 (≠ S480), K518 (= K559)
- binding adenosine monophosphate: A301 (≠ I341), G326 (= G366), T328 (= T368), D412 (= D454), K429 (= K471), K433 (= K475), Q438 (≠ S480)
- binding coenzyme a: L102 (= L116), P226 (= P264), H229 (≠ W267), Y231 (≠ A269), F253 (≠ W291), K435 (≠ N477), G436 (= G478), F437 (≠ M479), F498 (≠ I540)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
27% identity, 96% coverage: 26:569/569 of query aligns to 19:529/529 of 5bsvA
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), 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 (≠ W267), Y232 (≠ A269), S236 (≠ T273), A302 (≠ I341), A303 (≠ K342), P304 (≠ K343), G325 (≠ A364), G327 (= G366), M328 (= M367), T329 (= T368), P333 (≠ T372), V334 (≠ C373), D413 (= D454), K430 (= K471), K434 (= K475), Q439 (≠ S480)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
27% identity, 96% coverage: 26:569/569 of query aligns to 19:529/529 of 5bsuA
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), K519 (= K559)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (≠ W267), Y232 (≠ A269), S236 (≠ T273), M299 (≠ I338), A302 (≠ I341), A303 (≠ K342), P304 (≠ K343), G325 (≠ A364), G327 (= G366), M328 (= M367), T329 (= T368), P333 (≠ T372), D413 (= D454), K430 (= K471), K434 (= K475), Q439 (≠ S480)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
27% identity, 96% coverage: 26:569/569 of query aligns to 19:529/529 of 5bstA
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), K519 (= K559)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (≠ W267), Y232 (≠ A269), S236 (≠ T273), A302 (≠ I341), A303 (≠ K342), P304 (≠ K343), G325 (≠ A364), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), P333 (≠ T372), V334 (≠ C373), D413 (= D454), K430 (= K471), K434 (= K475), Q439 (≠ S480)
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)
27% identity, 96% coverage: 26:569/569 of query aligns to 26:536/542 of O24146
- S189 (≠ T218) binding
- S190 (= S219) binding
- G191 (= G220) binding
- T192 (= T221) binding
- T193 (= T222) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K226) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (≠ W267) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ A269) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ T273) binding ; binding ; binding
- K260 (≠ R290) binding
- A309 (≠ I341) binding ; binding ; binding
- Q331 (≠ V363) binding
- G332 (≠ A364) binding ; binding ; binding ; binding ; binding
- T336 (= T368) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ C373) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ F376) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D454) binding ; binding ; binding ; binding ; binding
- R435 (= R469) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K471) binding ; binding ; binding ; binding
- K441 (= K475) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ N477) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G478) binding
- Q446 (≠ S480) binding
- K526 (= K559) 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)
27% identity, 96% coverage: 26:569/569 of query aligns to 19:529/530 of 5bsmA
- active site: S182 (≠ T218), S202 (≠ T238), H230 (≠ W267), T329 (= T368), E330 (= E369), K434 (= K475), Q439 (≠ S480), K519 (= K559)
- binding adenosine-5'-triphosphate: S182 (≠ T218), S183 (= S219), G184 (= G220), T185 (= T221), T186 (= T222), K190 (= K226), H230 (≠ W267), A302 (≠ I341), A303 (≠ K342), P304 (≠ K343), Y326 (= Y365), G327 (= G366), M328 (= M367), T329 (= T368), D413 (= D454), I425 (≠ Y466), R428 (= R469), K519 (= K559)
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
28% identity, 92% coverage: 42:562/569 of query aligns to 6:494/506 of 4gxqA
- active site: T163 (= T218), N183 (vs. gap), H207 (≠ W267), T303 (= T368), E304 (= E369), I403 (≠ K475), N408 (≠ S480), A491 (≠ K559)
- binding adenosine-5'-triphosphate: T163 (= T218), S164 (= S219), G165 (= G220), T166 (= T221), T167 (= T222), H207 (≠ W267), S277 (vs. gap), A278 (vs. gap), P279 (vs. gap), E298 (= E362), M302 (= M367), T303 (= T368), D382 (= D454), R397 (= R469)
- binding carbonate ion: H207 (≠ W267), S277 (vs. gap), R299 (≠ A364), G301 (= G366)
4wv3B Crystal structure of the anthranilate coa ligase auaeii in complex with anthranoyl-amp (see paper)
28% identity, 90% coverage: 58:568/569 of query aligns to 35:511/518 of 4wv3B
- active site: S175 (≠ T218), T320 (= T370), E321 (≠ H371), K418 (= K475), W423 (≠ S480), K502 (= K559)
- binding 5'-O-[(S)-[(2-aminobenzoyl)oxy](hydroxy)phosphoryl]adenosine: F220 (≠ W267), T221 (≠ I268), F222 (≠ A269), A293 (≠ F340), S294 (≠ I341), E295 (≠ K342), A296 (≠ K343), G316 (= G366), I317 (≠ M367), G318 (≠ T368), C319 (≠ E369), T320 (= T370), D397 (= D454), H409 (≠ Y466), R412 (= R469), K502 (= K559)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
27% identity, 96% coverage: 26:569/569 of query aligns to 18:525/527 of 5u95B
2d1sA Crystal structure of the thermostable japanese firefly luciferase complexed with high-energy intermediate analogue (see paper)
27% identity, 94% coverage: 25:560/569 of query aligns to 9:526/539 of 2d1sA
- active site: S194 (≠ T218), R214 (≠ T238), H241 (≠ P264), T339 (= T368), E340 (= E369), K439 (= K475), Q444 (≠ S480), K525 (= K559)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S194 (≠ T218), S195 (= S219), H241 (≠ P264), F243 (= F266), T247 (≠ G270), I282 (≠ M310), G312 (vs. gap), A313 (≠ I338), P314 (≠ S339), Q334 (≠ V363), G335 (≠ A364), Y336 (= Y365), G337 (= G366), L338 (≠ M367), T339 (= T368), S343 (≠ T372), A344 (≠ C373), D418 (= D454), R433 (= R469), K525 (= K559)
2d1rA Crystal structure of the thermostable japanese firefly luciferase complexed with oxyluciferin and amp (see paper)
27% identity, 94% coverage: 25:560/569 of query aligns to 9:526/539 of 2d1rA
- active site: S194 (≠ T218), R214 (≠ T238), H241 (≠ P264), T339 (= T368), E340 (= E369), K439 (= K475), Q444 (≠ S480), K525 (= K559)
- binding adenosine monophosphate: S194 (≠ T218), S195 (= S219), H241 (≠ P264), G312 (vs. gap), A313 (≠ I338), P314 (≠ S339), G335 (≠ A364), Y336 (= Y365), G337 (= G366), L338 (≠ M367), T339 (= T368), D418 (= D454), K525 (= K559)
- binding 2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazol-4(5h)-one: H241 (≠ P264), F243 (= F266), T247 (≠ G270), G335 (≠ A364), G337 (= G366), L338 (≠ M367), A344 (≠ C373)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
27% identity, 89% coverage: 58:563/569 of query aligns to 49:534/544 of 6q2mA
- active site: S197 (≠ T218), R217 (≠ T238), H244 (≠ W267), T342 (= T368), E343 (= E369), K442 (= K475), Q447 (≠ S480), K528 (= K559)
- binding (2S,5S)-hexane-2,5-diol: D186 (= D211), R187 (vs. gap), R260 (≠ T284), Y279 (≠ H303)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (= S219), H244 (≠ W267), F246 (≠ A269), T250 (= T273), G315 (vs. gap), A316 (≠ I338), P317 (≠ S339), G338 (≠ A364), Y339 (= Y365), G340 (= G366), L341 (≠ M367), T342 (= T368), S346 (≠ T372), A347 (≠ C373), D421 (= D454), K528 (= K559)
Sites not aligning to the query:
Query Sequence
>5210425 FitnessBrowser__PV4:5210425
MNEQTYLQQVKALQAARWPKGTTREPIYPHGEKPVTEYLSAWARLNPTKVAIQFYGYELT
YAQLDEMSTRFANVLRGLGVGQGDGVAVFMPNCPQFHIAFLGILKCGAVHMPVSPLSKEM
ELRHQLGDSQPKVALCYDALLPTMRPVCQELGIEHIITTSYTDVRPRAITAVLPDLFEIP
KTPLADGIIDFFEAIDNASKEVLDYIPALDDLAAINYTSGTTGMPKGVMHTHRNMIGTMA
SYYPVTFGEVGPEGTDLVMLSFLPEFWIAGEDTGLLLPLYSGATLVLMARWDTKAFMELV
HHHKVNMTIMLIDSVDEILNHPHLHQFDLTSLTTVPCISFIKKLNRDYRQRWRELTGTTL
FEVAYGMTETHTCDTFTRGFQVDDMDLSFDPAFLGLPVPGTEIKICDFVTGELMPLGVEG
EIQIRTPTLLKGYWNKPDLNKNLFEEGGWYRTGDLGMITEEGFFRYLGRRKEMLKVNGMS
VFPTEVESMLGQHPAIASCGVVGRPDERKGQVPVAFVTLKPGFDETQESLQAWCVNAMAI
FKVPEIRIQERLPMTATGKIRKVDLEKSL
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