SitesBLAST
Comparing WP_028315232.1 NCBI__GCF_000429905.1:WP_028315232.1 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)
39% identity, 98% coverage: 9:560/562 of query aligns to 3:556/561 of P69451
- Y213 (= Y216) mutation to A: Loss of activity.
- T214 (= T217) mutation to A: 10% of wild-type activity.
- G216 (= G219) mutation to A: Decreases activity.
- T217 (= T220) mutation to A: Decreases activity.
- G219 (= G222) mutation to A: Decreases activity.
- K222 (= K225) mutation to A: Decreases activity.
- E361 (= E362) mutation to A: Loss of 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)
31% identity, 95% coverage: 20:555/562 of query aligns to 27:548/556 of Q9S725
- K211 (= K225) mutation to S: Drastically reduces the activity.
- M293 (≠ P305) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ F332) mutation K->L,A: Affects the substrate specificity.
- E401 (= E409) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ I411) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R456) mutation to Q: Drastically reduces the activity.
- K457 (≠ G464) mutation to S: Drastically reduces the activity.
- K540 (= K547) mutation to N: Abolishes the activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
33% identity, 92% coverage: 40:554/562 of query aligns to 14:498/506 of 4gxqA
- active site: T163 (= T217), N183 (≠ R236), H207 (= H263), T303 (= T361), E304 (= E362), I403 (≠ L462), N408 (= N467), A491 (≠ K547)
- binding adenosine-5'-triphosphate: T163 (= T217), S164 (≠ G218), G165 (= G219), T166 (= T220), T167 (= T221), H207 (= H263), S277 (= S335), A278 (= A336), P279 (= P337), E298 (= E356), M302 (= M360), T303 (= T361), D382 (= D441), R397 (= R456)
- binding carbonate ion: H207 (= H263), S277 (= S335), R299 (≠ G357), G301 (= G359)
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)
31% identity, 90% coverage: 51:553/562 of query aligns to 55:536/546 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)
31% identity, 96% coverage: 20:556/562 of query aligns to 8:527/528 of 5bsrA
- active site: S181 (≠ T217), S201 (≠ R236), H229 (= H263), T328 (= T361), E329 (= E362), K433 (≠ L462), Q438 (≠ N467), K518 (= K547)
- binding adenosine monophosphate: A301 (≠ S335), G326 (= G359), T328 (= T361), D412 (= D441), K429 (= K458), K433 (≠ L462), Q438 (≠ N467)
- binding coenzyme a: L102 (= L111), P226 (= P260), H229 (= H263), Y231 (≠ F265), F253 (≠ P287), K435 (≠ G464), G436 (= G465), F437 (≠ Y466), F498 (≠ K527)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 96% coverage: 20:556/562 of query aligns to 9:528/529 of 5bsvA
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), 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 (= H263), Y232 (≠ F265), S236 (≠ T269), A302 (≠ S335), A303 (= A336), P304 (= P337), G325 (= G357), G327 (= G359), M328 (= M360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 96% coverage: 20:556/562 of query aligns to 9:528/529 of 5bsuA
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), K519 (= K547)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ T269), M299 (≠ F332), A302 (≠ S335), A303 (= A336), P304 (= P337), G325 (= G357), G327 (= G359), M328 (= M360), T329 (= T361), P333 (= P365), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 96% coverage: 20:556/562 of query aligns to 9:528/529 of 5bstA
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), K519 (= K547)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ T269), A302 (≠ S335), A303 (= A336), P304 (= P337), G325 (= G357), Y326 (≠ F358), G327 (= G359), M328 (= M360), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
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, 96% coverage: 20:559/562 of query aligns to 16:538/542 of O24146
- S189 (≠ T217) binding ATP
- S190 (≠ G218) binding ATP
- G191 (= G219) binding ATP
- T192 (= T220) binding ATP
- T193 (= T221) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K225) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H263) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F265) 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 (≠ T269) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (= K286) binding CoA
- A309 (≠ S335) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E356) binding ATP
- G332 (= G357) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T361) 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 (= V366) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ I369) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D441) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R456) 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 (= K458) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L462) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G464) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G465) binding CoA
- Q446 (≠ N467) binding AMP
- K526 (= K547) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 96% coverage: 20:556/562 of query aligns to 9:528/530 of 5bsmA
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), K519 (= K547)
- binding adenosine-5'-triphosphate: S182 (≠ T217), S183 (≠ G218), G184 (= G219), T185 (= T220), T186 (= T221), K190 (= K225), H230 (= H263), A302 (≠ S335), A303 (= A336), P304 (= P337), Y326 (≠ F358), G327 (= G359), M328 (= M360), T329 (= T361), D413 (= D441), I425 (= I453), R428 (= R456), K519 (= K547)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 94% coverage: 26:554/562 of query aligns to 16:526/528 of 3ni2A
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), K519 (= K547)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F265), S236 (≠ T269), G302 (≠ S335), A303 (= A336), P304 (= P337), G325 (= G357), G327 (= G359), T329 (= T361), P333 (= P365), V334 (= V366), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 94% coverage: 26:554/562 of query aligns to 16:526/528 of 3a9vA
- active site: S182 (≠ T217), S202 (≠ R236), H230 (= H263), T329 (= T361), E330 (= E362), K434 (≠ L462), Q439 (≠ N467), K519 (= K547)
- binding adenosine monophosphate: H230 (= H263), G302 (≠ S335), A303 (= A336), P304 (= P337), Y326 (≠ F358), G327 (= G359), M328 (= M360), T329 (= T361), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
6k4cA Ancestral luciferase anclamp in complex with dlsa (see paper)
32% identity, 92% coverage: 36:554/562 of query aligns to 29:534/538 of 6k4cA
- binding 5'-o-[n-(dehydroluciferyl)-sulfamoyl] adenosine: H243 (= H263), F245 (= F265), T249 (= T269), G314 (≠ S335), A315 (= A336), P316 (= P337), G337 (= G357), Y338 (≠ F358), G339 (= G359), L340 (≠ M360), T341 (= T361), A346 (≠ V366), D420 (= D441), I432 (= I453), K527 (= K547)
6k4dA Ancestral luciferase anclamp in complex with atp and d-luciferin (see paper)
32% identity, 92% coverage: 36:554/562 of query aligns to 29:534/539 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 (= H263), F245 (= F265), T249 (= T269), G314 (≠ S335), A315 (= A336), P316 (= P337), G337 (= G357), Y338 (≠ F358), G339 (= G359), L340 (≠ M360), T341 (= T361), S345 (≠ P365), A346 (≠ V366), D420 (= D441), I432 (= I453), K527 (= K547)
- binding (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid: F245 (= F265), R335 (≠ V355), G337 (= G357), G339 (= G359), L340 (≠ M360), A346 (≠ V366)
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, 91% coverage: 51:559/562 of query aligns to 57:547/559 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.
7kydA Drosophila melanogaster long-chain fatty-acyl-coa synthetase cg6178 (see paper)
31% identity, 95% coverage: 26:560/562 of query aligns to 22:534/534 of 7kydA
- binding 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine: H240 (= H263), F242 (= F265), A311 (≠ S335), A312 (= A336), P313 (= P337), G334 (= G357), Y335 (≠ F358), G336 (= G359), L337 (≠ M360), S338 (≠ T361), S343 (≠ V366), D416 (= D441), I428 (= I453)
5u95B Structure of the open conformation of 4-coumarate-coa ligase from nicotiana tabacum
31% identity, 96% coverage: 20:559/562 of query aligns to 8:527/527 of 5u95B
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, 90% coverage: 53:559/562 of query aligns to 29:499/503 of P9WQ37
- K172 (= K225) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R250) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ K252) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (= V264) 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 (≠ G266) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (= T269) 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 (≠ K300) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G359) 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 (= W436) 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 (= D441) 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 (= R456) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S463) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G465) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K547) 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)
30% identity, 91% coverage: 46:554/562 of query aligns to 55:570/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 90% coverage: 53:559/562 of query aligns to 32:499/502 of 3r44A
Sites not aligning to the query:
Query Sequence
>WP_028315232.1 NCBI__GCF_000429905.1:WP_028315232.1
MPLNNDSPKPWTKHYEPEVVPELKFENRTILDYLGQSFSDFPNNAALVFQGYKLSFAGLK
DMVDRFASALSGFGIEKGDAVAILLPNSIPCVAAYYAILKIGGVVVMNNPLYSDRELSHQ
FNDSGAKALITLDLLANRMIDLRPMTRVRQIVYTSMGDYLPFPKNLLFPLIGKKKGLAAD
VKQASDVYKWKELISGSSPASVQADLDLDDLAMFQYTGGTTGVSKGVMLTHGNLSRQFQQ
VRAWFNGFDRGKEVMLGALPFFHVFGLTTSMNMAACQGWTNVLVPKPQAEPLLDAISKFK
PTFAPLVPTMYIGMLSDPRIKTTDLTSISACFSGSAPLPVEVIKEFEKITGATIVEGFGM
TESSPVTHINPLRGTRKPGSIGIPIPNTDAKIVDLETGDNELPQGESGELIIRGPQVMKG
YWNRMDDTAETIRDGWLYTGDIAKMDDDGYFYIVDRKKDMILSGGYNVYPRDIDEVYYLN
DKVQEVCTVGIPHPSRGEAAKVFIVLKEGVKATEKEMLDFVKDRLAKYKWPVEIEFRTEL
PKTNVGKILRKDLRAEEMAKRG
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