SitesBLAST
Comparing WP_010175848.1 NCBI__GCF_000171615.1:WP_010175848.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
38% identity, 99% coverage: 5:534/538 of query aligns to 3:553/561 of P69451
- Y213 (= Y192) mutation to A: Loss of activity.
- T214 (= T193) mutation to A: 10% of wild-type activity.
- G216 (= G195) mutation to A: Decreases activity.
- T217 (= T196) mutation to A: Decreases activity.
- G219 (= G198) mutation to A: Decreases activity.
- K222 (= K201) mutation to A: Decreases activity.
- E361 (= E339) mutation to A: Loss of activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 92% coverage: 37:531/538 of query aligns to 15:484/486 of 8wevA
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 91% coverage: 48:537/538 of query aligns to 26:503/506 of 4gxqA
- active site: T163 (= T193), N183 (= N213), H207 (= H240), T303 (≠ S338), E304 (= E339), I403 (= I439), N408 (= N444), A491 (≠ K524)
- binding adenosine-5'-triphosphate: T163 (= T193), S164 (≠ G194), G165 (= G195), T166 (= T196), T167 (= T197), H207 (= H240), S277 (= S312), A278 (= A313), P279 (= P314), E298 (= E333), M302 (≠ L337), T303 (≠ S338), D382 (= D418), R397 (= R433)
- binding carbonate ion: H207 (= H240), S277 (= S312), R299 (≠ G334), G301 (= G336)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
34% identity, 90% coverage: 48:533/538 of query aligns to 43:528/528 of 3ni2A
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F242), S236 (≠ V246), G302 (≠ S312), A303 (= A313), P304 (= P314), G325 (= G334), G327 (= G336), T329 (≠ S338), P333 (= P342), V334 (= V343), D413 (= D418), K430 (= K435), K434 (≠ I439), Q439 (≠ N444)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
34% identity, 90% coverage: 48:533/538 of query aligns to 43:528/528 of 3a9vA
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding adenosine monophosphate: H230 (= H240), G302 (≠ S312), A303 (= A313), P304 (= P314), Y326 (= Y335), G327 (= G336), M328 (≠ L337), T329 (≠ S338), D413 (= D418), K430 (= K435), K434 (≠ I439), Q439 (≠ N444)
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)
34% identity, 90% coverage: 48:531/538 of query aligns to 61:547/556 of Q9S725
- K211 (= K201) mutation to S: Drastically reduces the activity.
- M293 (≠ P282) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N309) mutation K->L,A: Affects the substrate specificity.
- E401 (= E383) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I388) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R433) mutation to Q: Drastically reduces the activity.
- K457 (≠ G441) mutation to S: Drastically reduces the activity.
- K540 (= K524) mutation to N: Abolishes the 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)
34% identity, 90% coverage: 48:531/538 of query aligns to 57:542/559 of Q67W82
- G395 (= G385) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
35% identity, 87% coverage: 64:531/538 of query aligns to 58:525/528 of 5bsrA
- active site: S181 (≠ T193), S201 (≠ N213), H229 (= H240), T328 (≠ S338), E329 (= E339), K433 (≠ I439), Q438 (≠ N444), K518 (= K524)
- binding adenosine monophosphate: A301 (≠ S312), G326 (= G336), T328 (≠ S338), D412 (= D418), K429 (= K435), K433 (≠ I439), Q438 (≠ N444)
- binding coenzyme a: L102 (≠ M107), P226 (= P237), H229 (= H240), Y231 (≠ F242), F253 (= F264), K435 (≠ G441), G436 (= G442), F437 (= F443), F498 (≠ A504)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
35% identity, 87% coverage: 64:531/538 of query aligns to 59:526/530 of 5bsmA
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding adenosine-5'-triphosphate: S182 (≠ T193), S183 (≠ G194), G184 (= G195), T185 (= T196), T186 (= T197), K190 (= K201), H230 (= H240), A302 (≠ S312), A303 (= A313), P304 (= P314), Y326 (= Y335), G327 (= G336), M328 (≠ L337), T329 (≠ S338), D413 (= D418), I425 (= I430), R428 (= R433), K519 (= K524)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
35% identity, 87% coverage: 64:531/538 of query aligns to 59:526/529 of 5bsvA
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H240), Y232 (≠ F242), S236 (≠ V246), A302 (≠ S312), A303 (= A313), P304 (= P314), G325 (= G334), G327 (= G336), M328 (≠ L337), T329 (≠ S338), P333 (= P342), V334 (= V343), D413 (= D418), K430 (= K435), K434 (≠ I439), Q439 (≠ N444)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
35% identity, 87% coverage: 64:531/538 of query aligns to 59:526/529 of 5bsuA
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H240), Y232 (≠ F242), S236 (≠ V246), M299 (≠ N309), A302 (≠ S312), A303 (= A313), P304 (= P314), G325 (= G334), G327 (= G336), M328 (≠ L337), T329 (≠ S338), P333 (= P342), D413 (= D418), K430 (= K435), K434 (≠ I439), Q439 (≠ N444)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
35% identity, 87% coverage: 64:531/538 of query aligns to 59:526/529 of 5bstA
- active site: S182 (≠ T193), S202 (≠ N213), H230 (= H240), T329 (≠ S338), E330 (= E339), K434 (≠ I439), Q439 (≠ N444), K519 (= K524)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H240), Y232 (≠ F242), S236 (≠ V246), A302 (≠ S312), A303 (= A313), P304 (= P314), G325 (= G334), Y326 (= Y335), G327 (= G336), M328 (≠ L337), T329 (≠ S338), P333 (= P342), V334 (= V343), D413 (= D418), K430 (= K435), K434 (≠ I439), Q439 (≠ N444)
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)
35% identity, 87% coverage: 64:531/538 of query aligns to 66:533/542 of O24146
- S189 (≠ T193) binding ATP
- S190 (≠ G194) binding ATP
- G191 (= G195) binding ATP
- T192 (= T196) binding ATP
- T193 (= T197) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K201) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H240) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F242) 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 (≠ V246) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R263) binding CoA
- A309 (≠ S312) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E333) binding ATP
- G332 (= G334) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S338) 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 (= V343) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ S346) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D418) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R433) 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 (= K435) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G441) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G442) binding CoA
- Q446 (≠ N444) binding AMP
- K526 (= K524) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
34% identity, 87% coverage: 64:531/538 of query aligns to 58:522/527 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)
30% identity, 90% coverage: 48:530/538 of query aligns to 55:536/546 of Q84P21
- K530 (= K524) mutation to N: Lossed enzymatic activity.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 94% coverage: 28:532/538 of query aligns to 5:478/484 of 5gtdA
- active site: T151 (= T193), S171 (≠ E219), H195 (= H240), T288 (≠ S338), E289 (= E339)
- binding adenosine-5'-monophosphate: G263 (≠ S312), G264 (≠ A313), Y285 (= Y335), G286 (= G336), M287 (≠ L337), T288 (≠ S338), D366 (= D418), V378 (≠ I430)
- binding magnesium ion: F314 (≠ P363), S315 (≠ Q364)
- binding 2-succinylbenzoate: H195 (= H240), S197 (≠ F242), A237 (≠ G283), L260 (≠ N309), G262 (= G311), G263 (≠ S312), G286 (= G336), M287 (≠ L337), S292 (≠ A341), Q293 (≠ P342)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
33% identity, 89% coverage: 52:531/538 of query aligns to 50:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H240), F245 (= F242), T249 (≠ V246), G314 (≠ S312), A315 (= A313), P316 (= P314), G337 (= G334), Y338 (= Y335), G339 (= G336), L340 (= L337), T341 (≠ S338), A346 (≠ V343), D420 (= D418), I432 (= I430), K527 (= K524)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
33% identity, 89% coverage: 52:531/538 of query aligns to 50:534/539 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 (= H240), F245 (= F242), T249 (≠ V246), G314 (≠ S312), A315 (= A313), P316 (= P314), G337 (= G334), Y338 (= Y335), G339 (= G336), L340 (= L337), T341 (≠ S338), S345 (≠ P342), A346 (≠ V343), D420 (= D418), I432 (= I430), K527 (= K524)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F242), R335 (≠ T332), G337 (= G334), G339 (= G336), L340 (= L337), A346 (≠ V343)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
31% identity, 94% coverage: 28:532/538 of query aligns to 5:478/485 of 5x8fB
- active site: T151 (= T193), S171 (≠ E219), H195 (= H240), T288 (≠ S338), E289 (= E339), I387 (= I439), N392 (= N444), K470 (= K524)
- binding magnesium ion: Y23 (≠ F46), E24 (≠ Y47), H70 (≠ Y92), N178 (≠ Q226), L202 (≠ C247), L214 (≠ M260), T296 (≠ H345), L297 (≠ S346), S298 (≠ N347)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ M107), L191 (≠ I236), P192 (= P237), H195 (= H240), I196 (≠ V241), S197 (≠ F242), A237 (≠ G283), V238 (= V284), L260 (≠ N309), G262 (= G311), G286 (= G336), M287 (≠ L337), S292 (≠ A341), Q293 (≠ P342), S388 (≠ A440), G389 (= G441), G390 (= G442), E391 (≠ F443), K420 (≠ Y472), W421 (≠ R473), K450 (≠ A504), Y451 (= Y505)
5burA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with atp and magnesium ion (see paper)
31% identity, 94% coverage: 28:532/538 of query aligns to 4:475/475 of 5burA
- active site: T150 (= T193), S170 (≠ E219), H194 (= H240), T287 (≠ S338), E288 (= E339)
- binding adenosine-5'-triphosphate: T150 (= T193), S151 (≠ G194), T153 (= T196), T154 (= T197), K158 (= K201), G263 (≠ A313), S283 (≠ G334), T287 (≠ S338), D365 (= D418), V377 (≠ I430), R380 (= R433)
Query Sequence
>WP_010175848.1 NCBI__GCF_000171615.1:WP_010175848.1
MSNVKNWLAKYPEGTVTHDISIPEISLPQMLQQSVVKYSEHIATSFYGRTTSYKELYHYV
VGFASSLQKQVSKGDRLAIMLPNCPQYVIAYYGTLLAGGIVTQINPMLVERELEYILKNS
GSTAIVSFDALYPRVKAVQERTHVETVLTVSLHEEFTPDLPDLTFTHFLQSSDGNFTPID
IDPKHDVAVLQYTGGTTGRSKGAMLTHFNLMANTSQSFEFYQKEFQVGNDKCLTVIPIFH
VFGMSVCMNLTLFCGSEIVMLPRFDLQEVLETIKREQPTVFPGVPTMYVAIANHPNAESY
GIDSIRVCNSGSAPMPVEVMKAFEQKTGAKITEGYGLSEAAPVTHSNPPFSKRKPGTCGL
GYPQTEYKVVDIATGTMECKPGELGELIIRGPQIMKGYWNMPEETENTIRDGWLLTGDIV
SVDEEGYLSIVDRKKDMIIAGGFNIYPRDIEEVLYEHPVIQEAVVIGVPDEYRGETVKAF
LVFKEGKQATEEELLEYCRANLSAYKVPTFFEIRDELPKTSVGKILRRALRDETVKQS
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