SitesBLAST
Comparing WP_041590142.1 NCBI__GCF_000023025.1:WP_041590142.1 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)
52% identity, 98% coverage: 7:534/540 of query aligns to 21:550/561 of P69451
- Y213 (= Y198) mutation to A: Loss of activity.
- T214 (= T199) mutation to A: 10% of wild-type activity.
- G216 (= G201) mutation to A: Decreases activity.
- T217 (= T202) mutation to A: Decreases activity.
- G219 (= G204) mutation to A: Decreases activity.
- K222 (= K207) mutation to A: Decreases activity.
- E361 (= E346) 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)
31% identity, 94% coverage: 27:535/540 of query aligns to 47:543/559 of Q67W82
- G395 (= G388) 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, 98% coverage: 5:534/540 of query aligns to 18:526/528 of 3ni2A
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (= Y248), S236 (≠ L252), G302 (= G319), A303 (≠ M320), P304 (≠ A321), G325 (= G341), G327 (= G343), T329 (= T345), P333 (= P349), V334 (= V350), D413 (= D422), K430 (= K439), K434 (≠ L443), Q439 (≠ N448)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 98% coverage: 5:534/540 of query aligns to 18:526/528 of 3a9vA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding adenosine monophosphate: H230 (= H246), G302 (= G319), A303 (≠ M320), P304 (≠ A321), Y326 (= Y342), G327 (= G343), M328 (≠ L344), T329 (= T345), D413 (= D422), K430 (= K439), K434 (≠ L443), Q439 (≠ N448)
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, 98% coverage: 10:539/540 of query aligns to 34:552/556 of Q9S725
- K211 (= K207) mutation to S: Drastically reduces the activity.
- M293 (≠ V289) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ S316) mutation K->L,A: Affects the substrate specificity.
- E401 (= E389) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C391) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R437) mutation to Q: Drastically reduces the activity.
- K457 (≠ S445) mutation to S: Drastically reduces the activity.
- K540 (= K527) mutation to N: Abolishes the activity.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 93% coverage: 33:535/540 of query aligns to 44:527/530 of 5bsmA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding adenosine-5'-triphosphate: S182 (≠ T199), S183 (≠ G200), G184 (= G201), T185 (= T202), T186 (= T203), K190 (= K207), H230 (= H246), A302 (≠ G319), A303 (≠ M320), P304 (≠ A321), Y326 (= Y342), G327 (= G343), M328 (≠ L344), T329 (= T345), D413 (= D422), I425 (= I434), R428 (= R437), K519 (= K527)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 93% coverage: 33:535/540 of query aligns to 44:527/529 of 5bsvA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H246), Y232 (= Y248), S236 (≠ L252), A302 (≠ G319), A303 (≠ M320), P304 (≠ A321), G325 (= G341), G327 (= G343), M328 (≠ L344), T329 (= T345), P333 (= P349), V334 (= V350), D413 (= D422), K430 (= K439), K434 (≠ L443), Q439 (≠ N448)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 93% coverage: 33:535/540 of query aligns to 44:527/529 of 5bsuA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H246), Y232 (= Y248), S236 (≠ L252), M299 (≠ S316), A302 (≠ G319), A303 (≠ M320), P304 (≠ A321), G325 (= G341), G327 (= G343), M328 (≠ L344), T329 (= T345), P333 (= P349), D413 (= D422), K430 (= K439), K434 (≠ L443), Q439 (≠ N448)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 93% coverage: 33:535/540 of query aligns to 44:527/529 of 5bstA
- active site: S182 (≠ T199), S202 (≠ N219), H230 (= H246), T329 (= T345), E330 (= E346), K434 (≠ L443), Q439 (≠ N448), K519 (= K527)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H246), Y232 (= Y248), S236 (≠ L252), A302 (≠ G319), A303 (≠ M320), P304 (≠ A321), G325 (= G341), Y326 (= Y342), G327 (= G343), M328 (≠ L344), T329 (= T345), P333 (= P349), V334 (= V350), D413 (= D422), K430 (= K439), K434 (≠ L443), Q439 (≠ N448)
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)
31% identity, 93% coverage: 33:535/540 of query aligns to 51:534/542 of O24146
- S189 (≠ T199) binding ATP
- S190 (≠ G200) binding ATP
- G191 (= G201) binding ATP
- T192 (= T202) binding ATP
- T193 (= T203) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K207) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H246) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (= Y248) 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 (≠ L252) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P270) binding CoA
- A309 (≠ G319) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E340) binding ATP
- G332 (= G341) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T345) 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 (= V350) 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 (= D422) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R437) 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 (= K439) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L443) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S445) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G446) binding CoA
- Q446 (≠ N448) binding AMP
- K526 (= K527) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 93% coverage: 33:535/540 of query aligns to 43:526/528 of 5bsrA
- active site: S181 (≠ T199), S201 (≠ N219), H229 (= H246), T328 (= T345), E329 (= E346), K433 (≠ L443), Q438 (≠ N448), K518 (= K527)
- binding adenosine monophosphate: A301 (≠ G319), G326 (= G343), T328 (= T345), D412 (= D422), K429 (= K439), K433 (≠ L443), Q438 (≠ N448)
- binding coenzyme a: L102 (= L93), P226 (= P243), H229 (= H246), Y231 (= Y248), F253 (≠ R271), K435 (≠ S445), G436 (= G446), F437 (= F447), F498 (≠ A507)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 93% coverage: 33:535/540 of query aligns to 43:523/527 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, 94% coverage: 32:540/540 of query aligns to 55:543/546 of Q84P21
- K530 (= K527) mutation to N: Lossed enzymatic 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)
31% identity, 93% coverage: 35:534/540 of query aligns to 30:494/503 of P9WQ37
- K172 (= K207) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ A230) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K235) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ I247) 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 (= A249) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ L252) 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 (≠ F285) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G343) 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 (= W417) 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 (= D422) 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 (= R437) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (≠ V444) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G446) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K527) 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.
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 94% coverage: 28:534/540 of query aligns to 53:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 94% coverage: 29:536/540 of query aligns to 23:500/506 of 4gxqA
- active site: T163 (= T199), N183 (= N219), H207 (= H246), T303 (= T345), E304 (= E346), I403 (≠ L443), N408 (= N448), A491 (≠ K527)
- binding adenosine-5'-triphosphate: T163 (= T199), S164 (≠ G200), G165 (= G201), T166 (= T202), T167 (= T203), H207 (= H246), S277 (≠ G319), A278 (≠ M320), P279 (≠ A321), E298 (= E340), M302 (≠ L344), T303 (= T345), D382 (= D422), R397 (= R437)
- binding carbonate ion: H207 (= H246), S277 (≠ G319), R299 (≠ G341), G301 (= G343)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 93% coverage: 35:534/540 of query aligns to 33:494/502 of 3r44A
Sites not aligning to the query:
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
26% identity, 93% coverage: 33:534/540 of query aligns to 47:534/539 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 (= H246), F245 (≠ L250), T249 (≠ G254), G314 (= G319), A315 (≠ M320), P316 (≠ A321), G337 (= G341), Y338 (= Y342), G339 (= G343), L340 (= L344), T341 (= T345), S345 (≠ P349), A346 (≠ V350), D420 (= D422), I432 (= I434), K527 (= K527)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (≠ L250), R335 (≠ C339), G337 (= G341), G339 (= G343), L340 (= L344), A346 (≠ V350)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
26% identity, 93% coverage: 33:534/540 of query aligns to 47:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H246), F245 (≠ L250), T249 (≠ G254), G314 (= G319), A315 (≠ M320), P316 (≠ A321), G337 (= G341), Y338 (= Y342), G339 (= G343), L340 (= L344), T341 (= T345), A346 (≠ V350), D420 (= D422), I432 (= I434), K527 (= K527)
6q2mA Crystal structure of photinus pyralis luciferase pps6 mutant in complex with dlsa (see paper)
27% identity, 93% coverage: 35:534/540 of query aligns to 50:535/544 of 6q2mA
- active site: S197 (≠ T199), R217 (≠ N219), H244 (= H246), T342 (= T345), E343 (= E346), K442 (≠ L443), Q447 (≠ N448), K528 (= K527)
- binding (2S,5S)-hexane-2,5-diol: D186 (≠ P188), R187 (≠ D189), R260 (≠ N264), Y279 (= Y283)
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: S198 (≠ G200), H244 (= H246), F246 (≠ L250), T250 (≠ G254), G315 (= G319), A316 (≠ M320), P317 (≠ A321), G338 (= G341), Y339 (= Y342), G340 (= G343), L341 (= L344), T342 (= T345), S346 (≠ P349), A347 (≠ V350), D421 (= D422), K528 (= K527)
Sites not aligning to the query:
Query Sequence
>WP_041590142.1 NCBI__GCF_000023025.1:WP_041590142.1
MVALIPRYKNVLEILDHAFTSYGPSPAYSCLGQTMTYAQLDELSLRAARYFRNVLGLQEG
DRIAIQLPNLLQYPVVLYGAFRAGLVVVNINPLYTPREIKHQLVDSGSRALVVLSNIAHN
AAEIIRETAVEAVIVTDIGDCHGFVKRTLMNFVVKHVKKMVPPFHFPSAISFDDIVASHG
EAFPKVVPDPETLLILQYTGGTTGLAKGAMLSHRNMAENVWQMVSFIPEAFDESKEIYVC
CLPLYHIYALNLHGLCAFSTGGHNVLIPNPRDLASMVKALKPYKFTVFVGINTLYTALCR
YEPFKSLDFSALDVSSAGGMALNEAAASCWEKMTGCEVCEGYGLTETSPVVAGNRPGHIR
QGYVGSALPETEVKLIDENGNIVVDQAGELCVRGPQVMQGYWHREDETLNVLDKDGWLKT
GDIAEISEDGFIKIVDRKKDMILVSGFNVYPNEIEDMVTQLPEVLEAAAIGVPNEKCGEV
VKLFVVAADETLSKQQIVDFCRKNLTAYKVPKEIEFRESLPKSNVGKILRKDLRSTEHNN
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