SitesBLAST
Comparing WP_012046884.1 NCBI__GCF_000015165.1:WP_012046884.1 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)
35% identity, 96% coverage: 23:552/553 of query aligns to 24:560/561 of P69451
- Y213 (= Y200) mutation to A: Loss of activity.
- T214 (= T201) mutation to A: 10% of wild-type activity.
- G216 (= G203) mutation to A: Decreases activity.
- T217 (= T204) mutation to A: Decreases activity.
- G219 (= G206) mutation to A: Decreases activity.
- K222 (= K209) mutation to A: Decreases activity.
- E361 (= E349) 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, 95% coverage: 24:547/553 of query aligns to 42:547/559 of Q67W82
- G395 (= G395) 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)
39% identity, 63% coverage: 193:543/553 of query aligns to 155:499/506 of 4gxqA
- active site: T163 (= T201), N183 (vs. gap), H207 (= H250), T303 (= T348), E304 (= E349), I403 (= I449), N408 (= N454), A491 (≠ K535)
- binding adenosine-5'-triphosphate: T163 (= T201), S164 (≠ G202), G165 (= G203), T166 (= T204), T167 (= T205), H207 (= H250), S277 (≠ G322), A278 (= A323), P279 (= P324), E298 (≠ S343), M302 (= M347), T303 (= T348), D382 (= D428), R397 (= R443)
- binding carbonate ion: H207 (= H250), S277 (≠ G322), R299 (≠ G344), G301 (= G346)
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: 19:542/553 of query aligns to 22:547/556 of Q9S725
- K211 (= K209) mutation to S: Drastically reduces the activity.
- M293 (≠ P292) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ G319) mutation K->L,A: Affects the substrate specificity.
- E401 (= E396) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ R398) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R443) mutation to Q: Drastically reduces the activity.
- K457 (≠ G451) mutation to S: Drastically reduces the activity.
- K540 (= K535) mutation to N: Abolishes the activity.
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)
32% identity, 91% coverage: 45:548/553 of query aligns to 27:500/503 of P9WQ37
- K172 (= K209) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R235) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E237) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I251) 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 (= A253) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ V256) 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 (= R287) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G346) 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 (≠ R423) 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 (= D428) 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 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K535) 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.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
32% identity, 88% coverage: 59:544/553 of query aligns to 57:528/528 of 3ni2A
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y252), S236 (≠ V256), G302 (= G322), A303 (= A323), P304 (= P324), G325 (= G344), G327 (= G346), T329 (= T348), P333 (vs. gap), V334 (≠ T350), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
32% identity, 88% coverage: 59:544/553 of query aligns to 57:528/528 of 3a9vA
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding adenosine monophosphate: H230 (= H250), G302 (= G322), A303 (= A323), P304 (= P324), Y326 (≠ W345), G327 (= G346), M328 (= M347), T329 (= T348), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
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)
33% identity, 91% coverage: 42:544/553 of query aligns to 37:535/542 of O24146
- S189 (≠ T201) binding ATP
- S190 (≠ G202) binding ATP
- G191 (= G203) binding ATP
- T192 (= T204) binding ATP
- T193 (= T205) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K209) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H250) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y252) 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 (≠ V256) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R273) binding CoA
- A309 (≠ G322) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ S343) binding ATP
- G332 (= G344) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T348) 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 (vs. gap) 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 (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D428) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R443) 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 (= K445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I449) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G451) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G452) binding CoA
- Q446 (≠ N454) binding AMP
- K526 (= K535) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
33% identity, 91% coverage: 42:544/553 of query aligns to 30:528/529 of 5bsvA
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H250), Y232 (= Y252), S236 (≠ V256), A302 (≠ G322), A303 (= A323), P304 (= P324), G325 (= G344), G327 (= G346), M328 (= M347), T329 (= T348), P333 (vs. gap), V334 (vs. gap), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
33% identity, 91% coverage: 42:544/553 of query aligns to 30:528/529 of 5bsuA
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H250), Y232 (= Y252), S236 (≠ V256), M299 (≠ G319), A302 (≠ G322), A303 (= A323), P304 (= P324), G325 (= G344), G327 (= G346), M328 (= M347), T329 (= T348), P333 (vs. gap), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
33% identity, 91% coverage: 42:544/553 of query aligns to 30:528/529 of 5bstA
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H250), Y232 (= Y252), S236 (≠ V256), A302 (≠ G322), A303 (= A323), P304 (= P324), G325 (= G344), Y326 (≠ W345), G327 (= G346), M328 (= M347), T329 (= T348), P333 (vs. gap), V334 (vs. gap), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
33% identity, 91% coverage: 42:544/553 of query aligns to 30:528/530 of 5bsmA
- active site: S182 (≠ T201), S202 (≠ A221), H230 (= H250), T329 (= T348), E330 (= E349), K434 (≠ I449), Q439 (≠ N454), K519 (= K535)
- binding adenosine-5'-triphosphate: S182 (≠ T201), S183 (≠ G202), G184 (= G203), T185 (= T204), T186 (= T205), K190 (= K209), H230 (= H250), A302 (≠ G322), A303 (= A323), P304 (= P324), Y326 (≠ W345), G327 (= G346), M328 (= M347), T329 (= T348), D413 (= D428), I425 (≠ L440), R428 (= R443), K519 (= K535)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
33% identity, 91% coverage: 42:544/553 of query aligns to 29:527/528 of 5bsrA
- active site: S181 (≠ T201), S201 (≠ A221), H229 (= H250), T328 (= T348), E329 (= E349), K433 (≠ I449), Q438 (≠ N454), K518 (= K535)
- binding adenosine monophosphate: A301 (≠ G322), G326 (= G346), T328 (= T348), D412 (= D428), K429 (= K445), K433 (≠ I449), Q438 (≠ N454)
- binding coenzyme a: L102 (= L105), P226 (= P247), H229 (= H250), Y231 (= Y252), F253 (= F274), K435 (≠ G451), G436 (= G452), F437 (= F453), F498 (≠ K515)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
31% identity, 91% coverage: 45:548/553 of query aligns to 30:500/502 of 3r44A
Sites not aligning to the query:
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, 94% coverage: 32:550/553 of query aligns to 38:545/546 of Q84P21
- K530 (= K535) mutation to N: Lossed enzymatic activity.
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
33% identity, 91% coverage: 42:544/553 of query aligns to 29:524/527 of 5u95B
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
31% identity, 95% coverage: 18:543/553 of query aligns to 14:535/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H250), F245 (≠ Y252), T249 (≠ V257), G314 (= G322), A315 (= A323), P316 (= P324), G337 (= G344), Y338 (≠ W345), G339 (= G346), L340 (≠ M347), T341 (= T348), A346 (≠ P353), D420 (= D428), I432 (≠ L440), K527 (= K535)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
31% identity, 95% coverage: 18:543/553 of query aligns to 14:535/539 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 (= H250), F245 (≠ Y252), T249 (≠ V257), G314 (= G322), A315 (= A323), P316 (= P324), G337 (= G344), Y338 (≠ W345), G339 (= G346), L340 (≠ M347), T341 (= T348), S345 (= S352), A346 (≠ P353), D420 (= D428), I432 (≠ L440), K527 (= K535)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ Y252), R335 (≠ K342), G337 (= G344), G339 (= G346), L340 (≠ M347), A346 (≠ P353)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
31% identity, 92% coverage: 37:542/553 of query aligns to 17:477/484 of 5gtdA
- active site: T151 (= T201), S171 (= S220), H195 (= H250), T288 (= T348), E289 (= E349)
- binding adenosine-5'-monophosphate: G263 (= G322), G264 (≠ A323), Y285 (≠ W345), G286 (= G346), M287 (= M347), T288 (= T348), D366 (= D428), V378 (≠ L440)
- binding magnesium ion: F314 (≠ P373), S315 (≠ G374)
- binding 2-succinylbenzoate: H195 (= H250), S197 (≠ Y252), A237 (≠ G293), L260 (≠ G319), G262 (= G321), G263 (= G322), G286 (= G346), M287 (= M347), S292 (= S352), Q293 (≠ P353)
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, 94% coverage: 23:544/553 of query aligns to 5:509/514 of Q9SMT7
- TSGTT 170:174 (≠ TGGTT 201:205) binding ATP
- H214 (= H250) binding ATP; mutation to A: Abolished activity.
- S289 (≠ G319) binding oxalate; mutation to A: Abolished activity.
- SAS 289:291 (≠ GSG 319:321) binding ATP
- EA 310:311 (≠ SG 343:344) binding ATP
- M314 (= M347) binding oxalate
- T315 (= T348) binding ATP
- H319 (≠ S352) binding oxalate; mutation to A: Abolished activity.
- D394 (= D428) binding ATP
- R409 (= R443) binding ATP; mutation to A: Abolished activity.
- K500 (= K535) binding ATP; binding oxalate; mutation to A: Abolished activity.
Query Sequence
>WP_012046884.1 NCBI__GCF_000015165.1:WP_012046884.1
MTHPGEQFYPEGVRWDAPIARGTLPELLAKAVSDFGDRGALEFRDRPISFNALAGLVDQA
AAAFLRAGFGKGASIALFLGNSPDHPINFFGALKAGARVVHLSPLDGEIALSHKLSDSGA
RILVTSNLSALLPMALKFLEKGLLDRLIVCEDDHWGQVGTPQTALPDSPAVITHRAFVDG
AVAPAVWPAISPDDIALLQYTGGTTGLPKGAMLTHGNLTSAVSIIEIWSRATRTRSEGGD
RVICVLPLFHIYALTVVLLTALRIGSLVSLHQRFDLEAVMRDIEHKRATYFPGVPTMWIA
IANLPDLDKRDLSSLTSVGSGGAPLPVEVARILERRVGMKLKSGWGMTETCSPGTSHPKE
GPDKPGSIGIALPGIEMDVVSLEDPTRVLGVNEVGEIRVKGPNVTKGYWNRPEETAQSFV
GDRFLTGDIGYVDADGFYFLVDRKKDMIISGGFNVYPQMIEQAIYIHPAVQEVIVIGIPD
AYRGEAAKAFIKLRDGFAPFPVEDLREFLTGKLGKHELPAAVEFVDELPRTPVGKLSRHE
LRQQQSSTSQSKH
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